<?xml version="1.0" encoding="iso-8859-1"?>
<!-- generator="FeedCreator 1.7.2" -->
<rss version="2.0">
    <channel>
        <title>Matrix Biology via MedWorm.com</title>
        <description>MedWorm.com provides a medical RSS filtering service. Over 6000 RSS medical sources are combined and output via different filters. This feed contains the latest items from the 'Matrix Biology' source.</description>
        <link><![CDATA[http://www.medworm.com/rss/search.php?qu=Matrix+Biology&t=Matrix+Biology&s=Search&f=source]]></link>
        <lastBuildDate>Mon, 06 Feb 2012 16:52:13 +0100</lastBuildDate>
        <item>
            <title>Thrombospondins as key regulators of synaptogenesis in the central nervous system.</title>
            <link>http://www.medworm.com/index.php?rid=5657382&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22285841%26dopt%3DAbstract</link>
            <description>Authors: Risher WC, Eroglu C
    Abstract
    Thrombospondins (TSPs) are a family of large, oligomeric multidomain glycoproteins that participate in a variety of biological functions as part of the extracellular matrix (ECM). Through their associations with a number of binding partners, TSPs mediate complex cell-cell and cell-matrix interactions in such diverse processes as angiogenesis, inflammation, osteogenesis, cell proliferation, and apoptosis. It was recently shown in the developing central nervous system (CNS) that TSPs promote the formation of new synapses, which are the unique cell-cell adhesions between neurons in the brain. This increase in synaptogenesis is mediated by the interaction between astrocyte-secreted TSPs and their neuronal receptor, calcium channel subunit α2δ-1. ...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5657382</comments>
            <pubDate>Sat, 21 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5657382</guid>        </item>
        <item>
            <title>Adhesion-modulating/matricellular ECM protein families: A structural, functional and evolutionary appraisal.</title>
            <link>http://www.medworm.com/index.php?rid=5637755&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22265890%26dopt%3DAbstract</link>
            <description>Authors: Mosher DF, Adams JC
    Abstract
    The thrombospondins are a family of secreted, oligomeric glycoproteins that interact with cell surfaces, multiple components of the extracellular matrix, growth factors and proteases. These interactions underlie complex roles in cell interactions and tissue homeostasis in animals. Thrombospondins have been grouped functionally with SPARCs, tenascins and CCN proteins as adhesion-modulating or matricellular components of the extracellular milieu. Although all these multi-domain proteins share various commonalities of domains, the grouping is not based on structural homologies. Instead, the terms emphasise the general observations that these proteins do not form large-scale ECM structures, yet act at cell surfaces and function in coordination with...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5637755</comments>
            <pubDate>Sat, 14 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5637755</guid>        </item>
        <item>
            <title>New insights into cartilage repair - The role of migratory progenitor cells in osteoarthritis.</title>
            <link>http://www.medworm.com/index.php?rid=5637752&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22266025%26dopt%3DAbstract</link>
            <description>Authors: Gerter R, Kruegel J, Miosge N
    Abstract
    Osteoarthritis is one of the most common musculo-skeletal diseases with a complex patholoy and a strong impact on cell biology, differentiation and migration behavior of mesenchymal stem cell-derived progenitor cells. In this review, we elucidate the influence of the pathologically altered extracellular matrix on progenitor cell behavior. Moreover, we discuss the modulation of progenitor cells especially of previously characterized chondrogenic progenitor cells (Koelling et al., 2009) in situ to enhance their regeneration potential. These options comprise the application of growth factors like fibroblast growth factor-2, a Runx-2 knock down and a contemporary anti-inflammatory therapy. This supports endogenous regeneration on behalf o...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5637752</comments>
            <pubDate>Sat, 14 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5637752</guid>        </item>
        <item>
            <title>Thrombospondin1 in tissue repair and fibrosis: TGF-β-dependent and independent mechanisms.</title>
            <link>http://www.medworm.com/index.php?rid=5637751&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22266026%26dopt%3DAbstract</link>
            <description>Authors: Sweetwyne MT, Murphy-Ullrich JE
    Abstract
    Thrombospondin 1 (TSP1) plays major roles in both physiologic and pathologic tissue repair. TSP1 through its type 1 repeats is a known regulator of latent TGF-β activation and plays a role in wound healing and fibrosis. Binding of the TSP N-terminal domain to cell surface calreticulin in complex with LDL-receptor related protein 1 stimulates intermediate cell adhesion, cell migration, anoikis resistance and collagen expression and matrix deposition in an in vivo model of the foreign body response. There is also emerging evidence that TSP EGF-like repeats alter endothelial cell-cell interactions and stimulate epithelial migration through transactivation of EGF receptors. The mechanisms underlying these functions of TSP1 and the impl...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5637751</comments>
            <pubDate>Sat, 14 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5637751</guid>        </item>
        <item>
            <title>The matricellular protein thrombospondin-1 globally regulates cardiovascular function and responses to stress via CD47.</title>
            <link>http://www.medworm.com/index.php?rid=5637750&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22266027%26dopt%3DAbstract</link>
            <description>Authors: Roberts DD, Miller TW, Rogers NM, Yao M, Isenberg JS
    Abstract
    Matricellular proteins play diverse roles in modulating cell behavior by engaging specific cell surface receptors and interacting with extracellular matrix proteins, secreted enzymes, and growth factors. Studies of such interactions involving thrombospondin-1 have revealed several physiological functions and roles in the pathogenesis of injury responses and cancer, but the relatively mild phenotypes of mice lacking thrombospondin-1 suggested that thrombospondin-1 would not be a central player that could be exploited therapeutically. Recent research focusing on signaling through its receptor CD47, however, has uncovered more critical roles for thrombospondin-1 in acute regulation of cardiovascular dynamics, hemos...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5637750</comments>
            <pubDate>Sat, 14 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5637750</guid>        </item>
        <item>
            <title>Thrombospondins in physiology and disease: New tricks for old dogs.</title>
            <link>http://www.medworm.com/index.php?rid=5637754&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22265891%26dopt%3DAbstract</link>
            <description>Authors: Murphy-Ullrich JE, Iozzo RV
    PMID: 22265891 [PubMed - as supplied by publisher] (Source: Matrix Biology)</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5637754</comments>
            <pubDate>Thu, 12 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5637754</guid>        </item>
        <item>
            <title>Maladaptive matrix remodeling and regional biomechanical dysfunction in a mouse model of aortic valve disease.</title>
            <link>http://www.medworm.com/index.php?rid=5637753&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22265892%26dopt%3DAbstract</link>
            <description>The objective of this study was to examine extracellular matrix (ECM) remodeling and biomechanical properties in regional aortic valve tissue and determine the impact of early AVM on late AVD in the Eln+/- mouse model. Aortic valve ECM composition and remodeling from juvenile, adult, and aged stages were evaluated in Eln+/- mice using histology, ELISA, immunohistochemistry and gelatin zymography. Aortic valve tissue biomechanical properties were determined using micropipette aspiration. Cartilage-like nodules were demonstrated within the valve annulus region at all stages identifying a developmental abnormality preceding AVD. Interestingly, maladaptive ECM remodeling was observed in early AVM without AVD and worsened with late AVD, as evidenced by increased MMP-2 and MMP-9 expression and a...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5637753</comments>
            <pubDate>Thu, 12 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5637753</guid>        </item>
        <item>
            <title>Disruption of the developmentally-regulated Col2a1 pre-mRNA alternative splicing switch in a transgenic knock-in mouse model.</title>
            <link>http://www.medworm.com/index.php?rid=5619420&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22248926%26dopt%3DAbstract</link>
            <description>Authors: Lewis R, Ravindran S, Wirthlin L, Traeger G, Fernandes RJ, McAlinden A
    Abstract
    The present study describes the generation of a knock-in mouse model to address the role of type II procollagen (Col2a1) alternative splicing in skeletal development and maintenance. Alternative splicing of Col2a1 precursor mRNA is a developmentally-regulated event that only occurs in chondrogenic tissue. Normally, chondroprogenitor cells synthesize predominantly exon 2-containing mRNA isoforms (type IIA and IID) while Col2a1 mRNA devoid of exon 2 (type IIB) is the major isoform produced by differentiated chondrocytes. Another isoform, IIC, has also been identified that contains a truncated exon 2 and is not translated into protein. The biological significance of this IIA/IID to IIB splicing sw...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619420</comments>
            <pubDate>Mon, 09 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619420</guid>        </item>
        <item>
            <title>From the Editor's Desk Thank you!</title>
            <link>http://www.medworm.com/index.php?rid=5619421&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22244545%26dopt%3DAbstract</link>
            <description>Authors: 
    PMID: 22244545 [PubMed - in process] (Source: Matrix Biology)</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5619421</comments>
            <pubDate>Sun, 01 Jan 2012 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5619421</guid>        </item>
        <item>
            <title>The γ3 chain of laminin is widely but differentially expressed in murine basement membranes: Expression and functional studies.</title>
            <link>http://www.medworm.com/index.php?rid=5577287&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22222602%26dopt%3DAbstract</link>
            <description>This study investigates the expression pattern of the γ3 chain in mouse. We developed three new γ3-reactive antibodies, and we show that the γ3 chain is present in BMs. The distribution pattern is considerably more restricted than that of the γ1 chain and within any tissue there is differential deposition into BM compartments. This is particularly true in the retina and brain, where γ3 is uniquely expressed in a subset of the vascular basement membranes and the pial surface. We used conventional genetic ablation techniques to remove the γ3 chain in mice; unlike other laminin null mice (α5, β2, γ1 nulls) (Noakes et al., 1995; Miner et al., 1998; Smyth et al., 1999), these mice live a normal lifespan and have only minor abnormalities, the most striking of which are ectopic granule c...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5577287</comments>
            <pubDate>Sat, 24 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5577287</guid>        </item>
        <item>
            <title>Determination of a molecular shape for netrin-4 from hydrodynamic and small angle X-ray scattering measurements.</title>
            <link>http://www.medworm.com/index.php?rid=5558860&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22210009%26dopt%3DAbstract</link>
            <description>Authors: Patel TR, Reuten R, Xiong S, Meier M, Winzor DJ, Koch M, Stetefeld J
    Abstract
    As part of a continuing investigation of netrins, an emerging class of extracellular matrix proteins that are involved in axon guidance activity, we have used dynamic light scattering (DLS) and small angle X-ray scattering to investigate the solution conformation of a truncated version of netrin-4 (Δnetrin-4) that lacks the C-terminal portion. The protein is characterized by a hydrodynamic (Stokes) radius (r(H)) of 4.60 (±0.20) nm, a radius of gyration (r(G)) of 4.42 (±0.20) nm and a maximum particle dimension (D(max)) of 16nm. More detailed ab initio modeling of the SAXS data indicates an extended rod like conformation for Δnetrin-4 in solution-a concept supported by the excellent agreement ...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5558860</comments>
            <pubDate>Sat, 24 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5558860</guid>        </item>
        <item>
            <title>Viscoelastic properties of model segments of collagen molecules.</title>
            <link>http://www.medworm.com/index.php?rid=5558861&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22204879%26dopt%3DAbstract</link>
            <description>Authors: Gautieri A, Vesentini S, Redaelli A, Buehler MJ
    Abstract
    Collagen is the prime construction material in vertebrate biology, determining the mechanical behavior of connective tissues such as tendon, bone and skin. Despite extensive efforts in the investigation of the origin of collagen unique mechanical properties, a deep understanding of the relationship between molecular structure and mechanical properties remains elusive, hindered by the complex hierarchical structure of collagen-based tissues. In particular, although extensive studies of viscoelastic properties have been pursued at the macroscopic (fiber/tissue) level, fewer investigations have been performed at the smaller scales, including in particular collagen molecules and fibrils. These scales are, however, import...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5558861</comments>
            <pubDate>Wed, 21 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5558861</guid>        </item>
        <item>
            <title>Molecular responses of choroidal endothelial cells to elastin derived peptides through the elastin-binding protein (GLB1).</title>
            <link>http://www.medworm.com/index.php?rid=5528811&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22178079%26dopt%3DAbstract</link>
            <description>CONCLUSIONS: EDPs may play a role in neovascular AMD by binding to and inducing neovascular phenotypes in choroidal endothelial cells through their receptor, GLB1. These peptides also cause an increased mRNA expression and deposition of collagen IV in the RPE/choroid, which may alter diffusion properties between the retina and choriocapillaris.
    PMID: 22178079 [PubMed - as supplied by publisher] (Source: Matrix Biology)</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5528811</comments>
            <pubDate>Fri, 02 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5528811</guid>        </item>
        <item>
            <title>Effects of decorin and biglycan on human airway smooth muscle cell adhesion.</title>
            <link>http://www.medworm.com/index.php?rid=5509864&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22155154%26dopt%3DAbstract</link>
            <description>Authors: D'Antoni ML, Risse PA, Ferraro P, Martin JG, Ludwig MS
    Abstract
    Growth on a decorin matrix results in decreased human airway smooth muscle cell (HASMC) number, by decreasing proliferation and increasing apoptosis. We questioned whether these effects were related to abnormal extracellular matrix (ECM)-cell adhesion. HASMCs were seeded on decorin, biglycan, collagen type I or plastic. Actin organization and focal adhesion formation were assessed by staining for filamentous (F) and globular (G) actin, and vinculin, respectively. Gene expression for focal adhesion proteins, ECM molecules and HASMC receptors was measured. Protein levels for fibronectin, α(2), α(5), α(v) and β(3) integrin subunits and, focal adhesion kinase (FAK) were assessed. F-actin filaments were promine...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5509864</comments>
            <pubDate>Fri, 02 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5509864</guid>        </item>
        <item>
            <title>A comprehensive model of hyaluronan turnover in the mouse.</title>
            <link>http://www.medworm.com/index.php?rid=5509866&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22142621%26dopt%3DAbstract</link>
            <description>Authors: Jadin L, Bookbinder LH, Frost GI
    Abstract
    The metabolism of hyaluronan (HA), especially its catabolism, is still far from elucidated. Although several studies suggest HA is degraded locally in tissues and through lymphatic or circulatory systems, much needs to be learned about the enzymes, receptors and cell types that support this dynamic process. In the current work, the clearance of exogenously administered HA was examined in a C57BL/6 mouse model. Hyaluronidase-sensitive fluorescein-labeled 1.2MDa hyaluronan (flHA) was administered either intravenously (i.v.) or subcutaneously (s.c.) into wild type C57BL/6 mice. Plasma was sampled for pharmacokinetic analysis and tissues harvested for histological examination of the cell types responsible for uptake using immunofluores...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5509866</comments>
            <pubDate>Sat, 26 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5509866</guid>        </item>
        <item>
            <title>Hyaluronan and versican in the control of human T lymphocyte adhesion and migration.</title>
            <link>http://www.medworm.com/index.php?rid=5509865&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22155153%26dopt%3DAbstract</link>
            <description>Authors: Evanko SP, Potter-Perigo S, Bollyky PL, Nepom GT, Wight TN
    Abstract
    The ability of lymphocytes to migrate freely through connective tissues is vital to efficient immune function. How the extracellular matrix (ECM) may affect T cell adhesion and migration is not well understood. We have examined the adhesion and migration of activated human T lymphocytes on extracellular matrix made by fibroblast-like synoviocytes and lung fibroblasts. These cells were minimally interactive until treated with a viral mimetic, Poly I:C. This treatment promoted myofibroblast formation and engendered a higher-order structured ECM rich in versican and hyaluronan to which T cells avidly adhered in a hyaluronidase-sensitive manner. This Poly I:C-induced matrix impeded T-cell spreading and migrati...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5509865</comments>
            <pubDate>Sun, 20 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5509865</guid>        </item>
        <item>
            <title>Random phage-epitope library based identification of a peptide antagonist of Mac-1 β2 integrin ligand binding.</title>
            <link>http://www.medworm.com/index.php?rid=5454284&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22100634%26dopt%3DAbstract</link>
            <description>Authors: Houimel M, Mazzucchelli L
    Abstract
    The leukocyte β2 integrin Mac-1 (CD11b/CD18) plays a pivotal role in inflammation and host defense. To develop peptide antagonists selectively inhibiting the function of Mac-1, we used a random constrained 6-mer (cys-6aa-cys) peptide library to map the structural features of CD11b, by determining the epitope of neutralizing monoclonal antibody mAb 44a (anti-CD11b). We have used a stringent phage display strategy, which resulted in the identification of one disulfide C-RLKEKH-C constrained peptide by direct biopanning of library on decreasing amounts of purified mAb 44a. The selected peptide mimics a discontinuous epitope, a peculiar shape on the CD11b-I-domain surface. Competitive ELISA experiments with different Mac-1 ligands showed tha...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5454284</comments>
            <pubDate>Fri, 11 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5454284</guid>        </item>
        <item>
            <title>Glycomic analyses of ovarian follicles during development and atresia.</title>
            <link>http://www.medworm.com/index.php?rid=5417184&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22057033%26dopt%3DAbstract</link>
            <description>Authors: Hatzirodos N, Nigro J, Irving-Rodgers HF, Vashi AV, Hummitzsch K, Caterson B, Sullivan TR, Rodgers RJ
    Abstract
    To examine the detailed composition of glycosaminoglycans during bovine ovarian follicular development and atresia, the specialized stromal theca layers were separated from the stratified epithelial granulosa cells of healthy (n=6) and atretic (n=6) follicles in each of three size ranges: small (3-5mm), medium (6-9mm) and large (10mm or more) (n=29 animals). Fluorophore-assisted carbohydrate electrophoresis analyses (on a per cell basis) and immunohistochemistry (n=14) were undertaken. We identified the major disaccharides in thecal layers and the membrana granulosa as chondroitin sulfate-derived ∆uronic acid with 4-sulfated N-acetylgalactosamine and ∆uronic a...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5417184</comments>
            <pubDate>Wed, 19 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5417184</guid>        </item>
        <item>
            <title>Drosophila basement membrane collagen col4a1 mutations cause severe myopathy.</title>
            <link>http://www.medworm.com/index.php?rid=5377999&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22037604%26dopt%3DAbstract</link>
            <description>In conclusion, our Drosophila mutant series may serve as an effective model to uncover the mechanisms by which COL4A1 mutations result in compromised myofiber-basement membrane interactions and aberrant muscle function.
    PMID: 22037604 [PubMed - as supplied by publisher] (Source: Matrix Biology)</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5377999</comments>
            <pubDate>Tue, 18 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5377999</guid>        </item>
        <item>
            <title>Molecular functions of syndecan-1 in disease.</title>
            <link>http://www.medworm.com/index.php?rid=5358427&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22033227%26dopt%3DAbstract</link>
            <description>Authors: Teng YH, Aquino RS, Park PW
    Abstract
    Syndecan-1 is a cell surface heparan sulfate proteoglycan that binds to many mediators of disease pathogenesis. Through these molecular interactions, syndecan-1 can modulate leukocyte recruitment, cancer cell proliferation and invasion, angiogenesis, microbial attachment and entry, host defense mechanisms, and matrix remodeling. The significance of syndecan-1 interactions in disease is underscored by the striking pathological phenotypes seen in the syndecan-1 null mice when they are challenged with disease-instigating agents or conditions. This review discusses the key molecular functions of syndecan-1 in modulating the onset, progression, and resolution of inflammatory diseases, cancer, and infection.
    PMID: 22033227 [PubMed - as su...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5358427</comments>
            <pubDate>Tue, 18 Oct 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5358427</guid>        </item>
        <item>
            <title>Laminin α1 is essential for mouse cerebellar development.</title>
            <link>http://www.medworm.com/index.php?rid=5325041&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21983115%26dopt%3DAbstract</link>
            <description>In this study, we generated conditional Lama1 knockout (Lama1(CKO)) mice in the epiblast lineage using Sox2-Cre mice. These Lama1(CKO) mice survived, but displayed behavioral disorders and impaired formation of the cerebellum. Deficiency of Lama1 in the pial basement membrane of the meninges resulted in defects in the conformation of the meninges. During cerebellar development, Lama1 deficiency also caused a decrease in the proliferation and migration of granule cell precursors, disorganization of Bergmann glial fibers and endfeet, and a transient reduction in the activity of Akt. A marked reduction in numbers of dendritic processes in Purkinje cells was observed in Lama1(CKO) mice. Together, these results indicate that Lama1 is required for cerebellar development and functions.
    PMID: ...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5325041</comments>
            <pubDate>Thu, 29 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5325041</guid>        </item>
        <item>
            <title>Neutrophil elastase cleaves the murine hemidesmosomal protein BP180/type XVII collagen and generates degradation products that modulate experimental bullous pemphigoid.</title>
            <link>http://www.medworm.com/index.php?rid=5294741&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21979170%26dopt%3DAbstract</link>
            <description>Authors: Lin L, Betsuyaku T, Heimbach L, Li N, Rubenstein D, Shapiro SD, An L, Giudice GJ, Diaz LA, Senior RM, Liu Z
    Abstract
    Bullous pemphigoid (BP) is an autoimmune subepidermal blistering disease associated with autoantibodies against the hemidesmosomal proteins BP180 and BP230. In the IgG passive transfer model of BP, blister formation is triggered by anti-BP180 IgG and depends on complement activation, mast cell degranulation, and neutrophil recruitment. Mice lacking neutrophil elastase (NE) do not develop experimental BP. Here, we demonstrated that NE degrades recombinant mouse BP180 within the immunodominant extracellular domain at amino acid positions 506 and 561, generating peptide p561 and peptide p506. Peptide p561 is chemotactic for neutrophils both in vitro and in vivo...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5294741</comments>
            <pubDate>Sun, 25 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5294741</guid>        </item>
        <item>
            <title>Morphogenetic roles of perlecan in the tooth enamel organ: An analysis of overexpression using transgenic mice.</title>
            <link>http://www.medworm.com/index.php?rid=5244415&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21933708%26dopt%3DAbstract</link>
            <description>Authors: Ida-Yonemochi H, Satokata I, Ohshima H, Sato T, Yokoyama M, Yamada Y, Saku T
    Abstract
    Perlecan, a heparan sulfate proteoglycan, is enriched in the intercellular space of the enamel organ. To understand the role of perlecan in tooth morphogenesis, we used a keratin 5 promoter to generate transgenic (Tg) mice that over-express perlecan in epithelial cells, and examined their tooth germs at tissue and cellular levels. Immunohistochemistry showed that perlecan was more strongly expressed in the enamel organ cells of Tg mice than in wild-type mice. Histopathology showed wider intercellular spaces in the stellate reticulum of the Tg molars and loss of cellular polarity in the enamel organ, especially in its cervical region. Hertwig's epithelial root sheath (HERS) cells in Tg mic...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5244415</comments>
            <pubDate>Tue, 13 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5244415</guid>        </item>
        <item>
            <title>Interstitial fibrosis is associated with increased COL1A2 transcription in AA-injured renal tubular epithelial cells in vivo.</title>
            <link>http://www.medworm.com/index.php?rid=5173463&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21864682%26dopt%3DAbstract</link>
            <description>Authors: Fragiadaki M, Witherden AS, Kaneko T, Sonnylal S, Pusey CD, Bou-Gharios G, Mason RM
    Abstract
    Accumulation of type I collagen is a key event in renal interstitial fibrosis. As there is no effective treatment, understanding the site where collagen is transcribed and the factors driving it in response to disease in vivo is critical for designing future therapies. The present research investigated the transcriptional activity of the COL1A2 gene in a mouse model of progressive fibrosis induced by aristolochic acid (aristolochic acid nephropathy, AAN). To achieve this we genetically modified mice to express a reporter gene (LacZ) and CCN2 (connective tissue growth factor) under the transcriptional control of the COL1A2 promoter /enhancer sequences. Using these mice we asked wher...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5173463</comments>
            <pubDate>Thu, 11 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5173463</guid>        </item>
        <item>
            <title>Peptide from the C-terminal domain of tissue inhibitor of matrix metalloproteinases-2 (TIMP-2) inhibits membrane activation of matrix metalloproteinase-2 (MMP-2).</title>
            <link>http://www.medworm.com/index.php?rid=5140547&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21839835%26dopt%3DAbstract</link>
            <description>In this study, we tested the feasibility of inhibiting activation of proMMP-2 by exogenous inhibitors, which block the binding between PEX and TIMP-2. The recombinant C-TIMP-2 and synthetic peptides from C-TIMP-2 were used as inhibitors for proMMP-2 activation. Recombinant C-TIMP-2 bound specifically to both the catalytically inactive MMP-2(E404A) and the C-terminal domain of MMP-2 (PEX) in a concentration dependent manner with apparent K(d) of 3.9×10(-7)M and 1.7×10(-7)M, respectively. Moreover, C-TIMP-2 competed the binding between MMP-2(E404A) and full-length TIMP-2. Finally, activity assays showed that addition of C-TIMP-2 to HT-1080 fibrosarcoma cells inhibited proMMP-2 activation in a concentration-dependent manner. We then designed a synthetic peptide, P175L, consisting of 20 resi...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5140547</comments>
            <pubDate>Wed, 03 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5140547</guid>        </item>
        <item>
            <title>The effect of hyaluronan on airway mucus transport and airway epithelial barrier integrity: Potential application to the cytoprotection of airway tissue.</title>
            <link>http://www.medworm.com/index.php?rid=5140548&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21839834%26dopt%3DAbstract</link>
            <description>Authors: Zahm JM, Milliot M, Bresin A, Coraux C, Birembaut P
    Abstract
    The lubricating abilities and the protective functions of hyaluronan, a structural component of interstitial and connective tissues, were assessed in in vitro models of airway mucus transport and epithelial barrier. We found that hyaluronan enhanced the transport of airway mucus by cilia and by cough: the lower the hyaluronan molecular weight, the higher the increase. By immunofluorescence and western blot, we observed a significant dose-dependent (0.1, 1, 5 and 10mg/ml) increase by low molecular weight hyaluronan (40kDa) in the expression of tight junction proteins such as ZO-1, as well as an increase in the trans-epithelial resistance. Incubation of airway epithelial cells with hyaluronan 40kDa also significant...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5140548</comments>
            <pubDate>Tue, 02 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5140548</guid>        </item>
        <item>
            <title>Ucmaa (Grp-2) is required for zebrafish skeletal development. Evidence for a functional role of its glutamate γ-carboxylation.</title>
            <link>http://www.medworm.com/index.php?rid=5140549&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21839171%26dopt%3DAbstract</link>
            <description>Authors: Neacsu CD, Grosch M, Tejada M, Winterpacht A, Paulsson M, Wagener R, Tagariello A
    Abstract
    UCMA (alternatively named GRP) is a novel member of the family of γ-carboxyglutamate (Gla) containing proteins that is mainly expressed in cartilage. We have used the zebrafish as a model organism to study UCMA function. Due to the whole genome duplication two Ucma genes are present in zebrafish, ucmaa and ucmab, located on chromosomes 25 and 4, respectively. UCMA gene structure, alternative splicing and protein sequence are highly conserved between mammals and zebrafish and Ucmaa and Ucmab are expressed in zebrafish skeletal tissues. Ucmaa is first detected in the notochord at 18 hpf and expression continues during notochord development. In addition, it is widely present in the dev...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5140549</comments>
            <pubDate>Sun, 31 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5140549</guid>        </item>
        <item>
            <title>Cell-matrix adhesions in 3D.</title>
            <link>http://www.medworm.com/index.php?rid=4999005&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21723391%26dopt%3DAbstract</link>
            <description>Authors: Harunaga JS, Yamada KM
    Cells in a three-dimensional (3D) extracellular matrix environment often display different properties and behavior compared to cells cultured on a two-dimensional (2D) substrate. Recent studies characterizing the cell-matrix adhesions formed by cells within a 3D matrix have arrived at contradictory conclusions regarding the presence and composition of adhesions. Here we review this literature, and provide a comparative compilation of information found in published studies from the 3D cell-matrix adhesion field in order to identify shared and divergent conclusions and conceptually important areas that require further research. Although there is a general consensus that discrete cell-matrix adhesions exist in various 3D matrix environments, there are speci...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4999005</comments>
            <pubDate>Wed, 22 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4999005</guid>        </item>
        <item>
            <title>Emerging roles for ADAMTS5 during development and disease.</title>
            <link>http://www.medworm.com/index.php?rid=4952653&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21683141%26dopt%3DAbstract</link>
            <description>Authors: Kintakas C, McCulloch DR
    
    PMID: 21683141 [PubMed - as supplied by publisher] (Source: Matrix Biology)</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4952653</comments>
            <pubDate>Sat, 11 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4952653</guid>        </item>
        <item>
            <title>Caveolin-1 modulates TGF-β1 signaling in cardiac remodeling.</title>
            <link>http://www.medworm.com/index.php?rid=4903515&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21641995%26dopt%3DAbstract</link>
            <description>Authors: Miyasato SK, Loeffler J, Shohet R, Zhang J, Lindsey M, Le Saux CJ
    The cardiac response to myocardial injury includes fibrotic and hypertrophic processes and a key mediator in this response is transforming growth factor-β1 (TGF-β1). Caveolin-1 (cav1), the main structural protein of caveolae, is an inhibitor of the TGF-β1 signaling pathway. To examine the role of cav1 in cardiac repair, cav1 deficient (Cav1(-/-)) and wild type (WT) mice were subjected to cryoinjury of the left ventricle (LV). At baseline the two groups exhibited no inflammation, similar collagen content, and similar cardiac function. After injury, Cav1(-/-) animals displayed enhanced TGF-β1 signaling, as reflected by a 3-fold increase in the activation of the Smad2-dependent pathway and more widespread colla...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4903515</comments>
            <pubDate>Thu, 26 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4903515</guid>        </item>
        <item>
            <title>Molecular simulations predict novel collagen conformations during cross-link loading.</title>
            <link>http://www.medworm.com/index.php?rid=4903516&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21620686%26dopt%3DAbstract</link>
            <description>Authors: Bourne JW, Torzilli PA
    Collagen cross-linking mechanically strengthens tissues during development and aging, but there is limited data describing how force transmitted across cross-links affects molecular conformation. We used Steered Molecular Dynamics (SMD) to model perpendicular force through a side chain. Results predicted that collagen peptides have negligible bending resistance and that mechanical force causes helix disruption below covalent bond failure strength, suggesting alternative molecular conformations precede cross-link rupture and macroscopic damage during mechanical loading.
    PMID: 21620686 [PubMed - as supplied by publisher] (Source: Matrix Biology)</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4903516</comments>
            <pubDate>Tue, 24 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4903516</guid>        </item>
        <item>
            <title>Implication of the oligomeric state of the N-terminal PTX3 domain in cumulus matrix assembly.</title>
            <link>http://www.medworm.com/index.php?rid=4903517&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21619930%26dopt%3DAbstract</link>
            <description>In conclusion, the data strength the view that PTX3 acts as a nodal molecule in cross-linking HA in the matrix.
    PMID: 21619930 [PubMed - as supplied by publisher] (Source: Matrix Biology)</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4903517</comments>
            <pubDate>Tue, 17 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4903517</guid>        </item>
        <item>
            <title>Sequence variants within the 3'-UTR of the COL5A1 gene alters mRNA stability: Implications for musculoskeletal soft tissue injuries.</title>
            <link>http://www.medworm.com/index.php?rid=4903518&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21609763%26dopt%3DAbstract</link>
            <description>Authors: Laguette MJ, Abrahams Y, Prince S, Collins M
    COL5A1 encodes the α1 chain of type V collagen, a quantitatively minor fibrillar collagen that regulates fibrillogenesis. A variant within the 3'-UTR of COL5A1 is associated with chronic Achilles tendinopathy (AT) and other exercise-related phenotypes but the functional significance of this is unknown. The aim of this study was therefore to identify functional differences between the COL5A1 3'-UTR from patients with AT and asymptomatic controls. To this end we have used a reporter assay in which the COL5A1 3'-UTR from AT patients and controls were cloned downstream of the firefly luciferase gene and luciferase activity measured as an indication of mRNA stability. When the cloned COL5A13'-UTRs were sequenced, two major forms named C...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4903518</comments>
            <pubDate>Fri, 13 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4903518</guid>        </item>
        <item>
            <title>Heparin stimulates elastogenesis: Application to silk-based vascular grafts.</title>
            <link>http://www.medworm.com/index.php?rid=4853749&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21600981%26dopt%3DAbstract</link>
            <description>Authors: Baughman C, Kaplan DL, Castellot JJ
    With over 500,000 coronary artery bypass grafts (CABG) performed annually in the United States alone, there is a significant clinical need for a small diameter tissue engineered vascular graft. A principle goal in tissue engineering is to develop materials and growth conditions that encourage appropriate recellularization and extracellular matrix formation in vivo. A particular challenge in vascular engineering results from the inability of adult cells to produce elastin, as its expression is developmentally limited. We investigated factors to stimulate elastogenesis in vitro, and found that heparin treatment of adult human vascular smooth muscle cells promoted the formation of elastic fibers. This effect was heparin-specific, and dependent ...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4853749</comments>
            <pubDate>Tue, 10 May 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4853749</guid>        </item>
        <item>
            <title>Scarless skin wound healing in FOXN1 deficient (nude) mice is associated with distinctive matrix metalloproteinase expression.</title>
            <link>http://www.medworm.com/index.php?rid=4801627&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21539913%26dopt%3DAbstract</link>
            <description>In this study, we analyzed the temporal and spatial expression patterns of these molecules during the incisional skin wounds in adult nude mice. Macroscopic and histological analyses of skin wounds revealed an accelerated wound healing process, minimal granulation tissue formation and markedly diminished scarring in nude mice. Quantitative RT-PCR (Mmp-2, -3, -8, -9, -10, -12, -13, -14 and Timp-1, -2, -3), Western blots (MMP-13) and gelatin zymography (MMP-9) revealed that MMP-9 and MMP-13 showed a unique, bimodal pattern of up-regulation during the early and late phases of wound healing in nude mice. Immunohistochemically MMP-9 and MMP-13 were generally detected in epidermis during the early phase and in dermis during the late (remodeling) phase. Consistent with these in vivo observations,...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4801627</comments>
            <pubDate>Thu, 21 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4801627</guid>        </item>
        <item>
            <title>Divergent upstream osteogenic events contribute to the differential modulation of MG63 cell osteoblast differentiation by MMP-1 (collagenase-1) and MMP-13 (collagenase-3).</title>
            <link>http://www.medworm.com/index.php?rid=4801626&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21539914%26dopt%3DAbstract</link>
            <description>Authors: Hayami T, Kapila YL, Kapila S
    Previously we showed that MMP-1 (collagenase-1) and MMP-13 (collagenase-3) differentially regulate the expression of osteoblastic markers in a heterogenous population of primary human periodontal ligament cells. The mechanisms for these differential responses are not known, but may result from divergence in regulation of early osteogenic transcription factors. The purpose of this study was to elucidate where in the hierarchy of osteoblast-specific transcription factors and markers the differences in MMP-1- and -13-mediated regulation of osteoblastic differentiation arise. We found that the overexpression of MMP-1 resulted in significant decreases in BMP-2, Dlx5, AP, OP and BSP and increases in TGF-β1 and MSX2. In contrast, MMP-13 overexpression r...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4801626</comments>
            <pubDate>Thu, 21 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4801626</guid>        </item>
        <item>
            <title>Matrilin-4 is processed by ADAMTS-5 in late Golgi vesicles present in growth plate chondrocytes of defined differentiation state.</title>
            <link>http://www.medworm.com/index.php?rid=4801625&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21539915%26dopt%3DAbstract</link>
            <description>In this study, the processing and degradation of matrilin-4 during cartilage remodeling in the growth plate of the developing mouse long bones were studied in greater detail. We show that ADAMTS-5 and a matrilin-4 neoepitope, revealed upon ADAMTS cleavage, colocalize in prehypertrophic/hypertrophic chondrocytes while they are not detected in proliferating chondrocytes of the growth plate. ADAMTS-5 and the cleaved matrilin-4 are preferentially detected in vesicles derived from the Golgi apparatus. The matrilin-4 neoepitope was not observed in the growth plate of ADAMTS-5 deficient mice. We propose that in the growth plate ADAMTS-5, and not ADAMTS-4, has a physiological function in the intracellular processing of matrilins and potentially of other extracellular matrix proteins.
    PMID: 215...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4801625</comments>
            <pubDate>Thu, 21 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4801625</guid>        </item>
        <item>
            <title>Regional differences in the expression of laminin isoforms during mouse neural tube development.</title>
            <link>http://www.medworm.com/index.php?rid=4801628&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21524702%26dopt%3DAbstract</link>
            <description>Authors: Copp AJ, Carvalho R, Wallace A, Sorokin L, Sasaki T, Greene ND, Ybot-Gonzalez P
    Many significant human birth defects originate around the time of neural tube closure or early during post-closure nervous system development. For example, failure of the neural tube to close generates anencephaly and spina bifida, faulty cell cycle progression is implicated in primary microcephaly, while defective migration of neuroblasts can lead to neuronal migration disorders such as lissencephaly. At the stage of neural tube closure, basement membranes are becoming organised around the neuroepithelium, and beneath the adjacent non-neural surface ectoderm. While there is circumstantial evidence to implicate basement membrane dynamics in neural tube and surface ectodermal development, we have an...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4801628</comments>
            <pubDate>Fri, 15 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4801628</guid>        </item>
        <item>
            <title>Early growth response transcription factors: Key mediators of fibrosis and novel targets for anti-fibrotic therapy.</title>
            <link>http://www.medworm.com/index.php?rid=4801630&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21511034%26dopt%3DAbstract</link>
            <description>Authors: Bhattacharyya S, Wu M, Fang F, Tourtellotte W, Feghali-Bostwick C, Varga J
    Fibrosis is a deregulated and ultimately defective form of tissue repair that underlies a large number of chronic human diseases, as well as obesity and aging. The pathogenesis of fibrosis involves multiple cell types and extracellular signals, of which transforming growth factor-ß (TGF-ß) is pre-eminent. The prevalence of fibrosis is rising worldwide, and to date no agents has shown clinical efficacy in the attenuating or reversing the process. Recent studies implicate the immediate-early response transcription factor Egr-1 in the pathogenesis of fibrosis. Egr-1 couples acute changes in the cellular environment to sustained alterations in gene expression, and mediates a broad spectrum of biological r...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4801630</comments>
            <pubDate>Tue, 12 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4801630</guid>        </item>
        <item>
            <title>Formation of lamellar cross bridges in the annulus fibrosus of the intervertebral disc is a consequence of vascular regression.</title>
            <link>http://www.medworm.com/index.php?rid=4801632&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21504791%26dopt%3DAbstract</link>
            <description>In this study we present evidence that the pathways left by receding blood vessels remain as lamellar cross bridges. It is unclear whether the presence of cross bridges in the aging and degenerating intervertebral disc would be advantageous or detrimental, and this question should be addressed by future studies.
    PMID: 21504791 [PubMed - as supplied by publisher] (Source: Matrix Biology)</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4801632</comments>
            <pubDate>Mon, 11 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4801632</guid>        </item>
        <item>
            <title>Differential and restricted expression of novel collagen VI chains in mouse.</title>
            <link>http://www.medworm.com/index.php?rid=4801635&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21477648%26dopt%3DAbstract</link>
            <description>Authors: Gara SK, Grumati P, Squarzoni S, Sabatelli P, Urciuolo A, Bonaldo P, Paulsson M, Wagener R
    Recently, three novel collagen VI chains, α4, α5 and α6, were identified. These are thought to substitute for the collagen VI α3 chain, probably forming α1α2α4, α1α2α5 or α1α2α6 heterotrimers. The expression pattern of the novel chains is so far largely unknown. In the present study, we compared the tissue distribution of the novel collagen VI chains in mouse with that of the α3 chain by immunohistochemistry, immunoelectron microscopy and immunoblots. In contrast to the widely expressed α3 chain, the novel chains show a highly differential, restricted and often complementary expression. The α4 chain is strongly expressed in the intestinal smooth muscle, surrounding the fo...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4801635</comments>
            <pubDate>Tue, 05 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4801635</guid>        </item>
        <item>
            <title>Discoidin domain receptor 2 is a critical regulator of epithelial-mesenchymal transition.</title>
            <link>http://www.medworm.com/index.php?rid=4801634&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21477649%26dopt%3DAbstract</link>
            <description>Authors: Walsh LA, Nawshad A, Medici D
    Discoidin domain receptor 2 (DDR2) is a collagen receptor that is expressed during epithelial-mesenchymal transition (EMT), a cellular transformation that mediates many stages of embryonic development and disease. However, the functional significance of this receptor in EMT is unknown. Here we show that Transforming Growth Factor-beta1 (TGF-β1), a common stimulator of EMT, promotes increased expression of type I collagen and DDR2. Inhibiting expression of COL1A1 or DDR2 with siRNA is sufficient to perturb activity of the NF-κB and LEF-1 transcription factors and to inhibit EMT and cell migration induced by TGF-β1. Furthermore, knockdown of DDR2 expression with siRNA inhibits EMT directly induced by type I collagen. These data establish a critic...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4801634</comments>
            <pubDate>Tue, 05 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4801634</guid>        </item>
        <item>
            <title>Drosophila type XV/XVIII collagen, Mp, is involved in Wingless distribution.</title>
            <link>http://www.medworm.com/index.php?rid=4801633&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21477650%26dopt%3DAbstract</link>
            <description>Authors: Momota R, Naito I, Ninomiya Y, Ohtsuka A
    Multiplexin (Mp) is the Drosophila orthologue of vertebrate collagens XV and XVIII. Like them, Mp is widely distributed in the basement membranes of the developing embryos, including those of neuroblasts in the central and peripheral nervous systems, visceral muscles of the gut, and contractile cardioblasts. Here we report the identification of mutant larvae bearing piggyBac transposon insertions that exhibit decrease Mp production associated with abdominal cuticular and wing margin defects, malformation of sensory organs and impaired sensitivity to physical stimuli. Additional findings include the abnormal ultrastructure of fatbody associated with abnormal collagen IV deposition, and reduced Wingless deposition. Collectively, these fin...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4801633</comments>
            <pubDate>Tue, 05 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4801633</guid>        </item>
        <item>
            <title>Material and mechanical properties of bones deficient for fibrillin-1 or fibrillin-2 microfibrils.</title>
            <link>http://www.medworm.com/index.php?rid=4801636&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21440062%26dopt%3DAbstract</link>
            <description>Authors: Arteaga-Solis E, Sui-Arteaga L, Kim M, Schaffler MB, Jepsen KJ, Pleshko N, Ramirez F
    The contribution of non-collagenous components of the extracellular matrix to bone strength is largely undefined. Here we report that deficiency of fibrillin-1 or fibrillin-2 microfibrils causes distinct changes in bone material and mechanical properties. Morphometric examination of mice with hypomorphic or null mutations in fibrillin-1 or fibrillin-2, respectively, revealed appreciable differences in the postnatal shaping and growth of long bones. Fourier transform infrared imaging spectroscopy indicated that fibrillin-1 plays a predominantly greater role than fibrillin-2 in determining the material properties of bones. Biomechanical tests demonstrated that fibrillin-2 exerts a greater positi...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4801636</comments>
            <pubDate>Thu, 31 Mar 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4801636</guid>        </item>
        <item>
            <title>Syndecan-1 and -4 differentially regulate oncogenic K-ras dependent cell invasion into collagen through α2β1 integrin and MT1-MMP.</title>
            <link>http://www.medworm.com/index.php?rid=4637628&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21414405%26dopt%3DAbstract</link>
            <description>Authors: Vuoriluoto K, Högnäs G, Meller P, Lehti K, Ivaska J
    Syndecans function as co-receptors for integrins on different matrixes. Recently, syndecan-1 has been shown to be important for α2β1 integrin-mediated adhesion to collagen in tumor cells by regulating cell adhesion and migration on two-dimensional collagen. However, the function of syndecans in supporting α2β1 integrin interactions with three-dimensional (3D) collagen is less well studied. Using loss-of-function and overexpression experiments we show that in 3D collagen syndecan-4 supports α2β1-mediated collagen matrix contraction. Cell invasion through type I collagen containing 3D extracellular matrix (ECM) is driven by α2β1 integrin and membrane type-1 matrix metalloproteinase (MT1-MMP). Here we show that mutatio...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4637628</comments>
            <pubDate>Mon, 14 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4637628</guid>        </item>
        <item>
            <title>Collagen VI is a basement membrane component that regulates epithelial cell-fibronectin interactions.</title>
            <link>http://www.medworm.com/index.php?rid=4637644&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21406227%26dopt%3DAbstract</link>
            <description>Authors: Groulx JF, Gagné D, Benoit YD, Martel D, Basora N, Beaulieu JF
    Collagen VI is a heterotrimer composed of three α chains ( α1, α2, α3) widely expressed throughout various interstitial matrices. Collagen VI is also found near the basement membranes of many tissues where it serves as an anchoring meshwork. The aim of this study was to investigate the distribution and role of collagen VI at the epithelial-stromal interface in the intestine. Results showed that collagen VI is a bona fide epithelial basal lamina component and constitutes the major collagen type of epithelial origin in this organ. In vitro, collagen VI co-distributes with fibronectin. Targeted knockdown of collagen VI expression in intestinal epithelial cells was used to investigate its function. Depletion of co...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4637644</comments>
            <pubDate>Sat, 12 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4637644</guid>        </item>
        <item>
            <title>β1 integrin regulates MMP-10 dependant tubulogenesis in human lymphatic endothelial cells.</title>
            <link>http://www.medworm.com/index.php?rid=4637636&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21406228%26dopt%3DAbstract</link>
            <description>Authors: Steele MM, Schieler AM, Kelley PM, Tempero RM
    Lymphatic vessel growth requires extensive remodeling of the extracellular matrix, a process hypothesized to be related to the expression and function of the matrix metalloproteinases. We used a protein based screening strategy to demonstrate increased matrix matalloproteinase-10 expression in human lymphatic endothelial cells undergoing collagen I induced tubulogenesis. Knock-down experiments showed that matrix metalloproteinase-10 regulated lymphatic endothelial cell tubulogenesis. β1 integrin signaling via the ERK/MAPK pathway increased matrix metalloproteinase-10 mRNA and protein expression in human lymphatic endothelial cells. These findings demonstrate a novel mechanism by which β1 integrin regulates matrix metalloproteinas...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4637636</comments>
            <pubDate>Sat, 12 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4637636</guid>        </item>
        <item>
            <title>SMOC1 is a tenascin-C interacting protein over-expressed in brain tumors.</title>
            <link>http://www.medworm.com/index.php?rid=4522782&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21349332%26dopt%3DAbstract</link>
            <description>Authors: Brellier F, Ruggiero S, Zwolanek D, Martina E, Hess D, Brown-Luedi M, Hartmann U, Koch M, Merlo A, Lino M, Chiquet-Ehrismann R
    Tenascin-C is an extracellular matrix protein over-expressed in a large variety of cancers. In the present study, we aimed at identifying new interactors of tenascin-C by purifying secreted proteins on a tenascin-C affinity column. Analysis of eluates by mass spectrometry revealed phosphoglycerate kinase 1, clusterin, fibronectin, SPARC-related modular calcium-binding protein 1 (SMOC1) and nidogen-2 as potential interactors of tenascin-C. The interaction between tenascin-C and SMOC1 was confirmed by co-immunoprecipitation and further analyzed by surface plasmon resonance spectroscopy, which revealed an apparent dissociation constant (K(D)) value of 2.5...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4522782</comments>
            <pubDate>Mon, 21 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4522782</guid>        </item>
        <item>
            <title>Reduced chondrogenic matrix accumulation by 4-methylumbelliferone reveals the potential for selective targeting of UDP-glucose dehydrogenase.</title>
            <link>http://www.medworm.com/index.php?rid=4464981&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21292001%26dopt%3DAbstract</link>
            <description>Authors: Clarkin CE, Allen S, Wheeler-Jones CP, Bastow ER, Pitsillides AA
    4-Methylumbelliferone (4-MU) is described as a selective inhibitor of hyaluronan (HA) production. It is thought that 4-MU depletes UDP-glucuronic acid (UDP-GlcUA) substrate for HA synthesis and also suppresses HA-synthase expression. The possibility that 4-MU exerts at least some of its actions via regulation of UDP-glucose dehydrogenase (UGDH), a key enzyme required for both HA and sulphated-glycosaminoglycan (sGAG) production, remains unexplored. We therefore examined the effects of 4-MU on basal and retroviral UGDH-driven HA and sGAG release in cells derived from chick articular cartilage and its influence upon UGDH protein and mRNA expression and HA and sGAG production. We found that 4-MU: i) suppressed UGDH ...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4464981</comments>
            <pubDate>Tue, 01 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4464981</guid>        </item>
        <item>
            <title>Differential in vivo zymography: A method for observing matrix metalloproteinase activity in the zebrafish embryo.</title>
            <link>http://www.medworm.com/index.php?rid=4464980&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21292002%26dopt%3DAbstract</link>
            <description>Authors: Keow JY, Herrmann KM, Crawford BD
    Investigations into the molecular mechanisms of, and cellular signaling pathways modulating ECM remodeling are especially challenging due to the complex post-translational regulation of the primary effectors of ECM catabolism - the matrix metalloproteinases (MMPs). Recently a variety of approaches to the detection of MMP activity have been developed, and the prospect of visualizing ECM remodeling activity in living tissues is now opening exciting avenues of research for matrix biologists. In particular the use of FRET-quenched MMP substrates, which generate a fluorescent signal upon hydrolysis, are becoming increasingly popular, especially because linkers with defined and/or restricted proteolytic sensitivity can be used to bind fluorophore-qu...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4464980</comments>
            <pubDate>Mon, 31 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4464980</guid>        </item>
        <item>
            <title>Age-Dependent Regulation of Skeletal Muscle Mitochondria by the Thrombospondin-1 Receptor CD47.</title>
            <link>http://www.medworm.com/index.php?rid=4397813&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21256215%26dopt%3DAbstract</link>
            <description>Authors: Frazier EP, Isenberg JS, Shiva S, Zhao L, Schlesinger P, Dimitry J, Abu-Asab MS, Tsokos M, Roberts DD, Frazier WA
    CD47, a receptor for thrombospondin-1, limits two important regulatory axes: nitric oxide-cGMP signaling and cAMP signaling, both of which can promote mitochondrial biogenesis. Electron microscopy revealed increased mitochondrial densities in skeletal muscle from both CD47 null and thrombospondin-1 null mice. We further assessed the mitochondria status of CD47-null vs WT mice. Quantitative RT-PCR of RNA extracted from tissues of 3month-old mice revealed dramatically elevated expression of mRNAs encoding mitochondrial proteins and PGC-1α in both fast and slow twitch skeletal muscle from CD47-null mice, but modest to no elevation in other tissues. These observations...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4397813</comments>
            <pubDate>Wed, 19 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4397813</guid>        </item>
        <item>
            <title>Induction of type XVI collagen expression facilitates proliferation of oral cancer cells.</title>
            <link>http://www.medworm.com/index.php?rid=4397815&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21251976%26dopt%3DAbstract</link>
            <description>Authors: Ratzinger S, Grässel S, Dowejko A, Reichert TE, Bauer RJ
    Type XVI collagen belongs to the family of fibril-associated collagens with interrupted triple helices (FACIT). Recently, high affinity to integrin alpha1beta1 has been shown allowing cells expressing those integrins to attach and spread on recombinant type XVI collagen. Here, we show that type XVI collagen is overexpressed in dysplastic areas of mucosal epithelium from oral squamous cell carcinoma (OSCC) patients. Induction of its expression in OSCC cell lines (COLXVI cells) leads to an increased expression of Kindlin-1. Moreover, we demonstrate a significantly increased Kindlin-1/beta1-integrin interaction. Additionally, we detected a higher number of activated beta1-integrins in COLXVI cells and found a neo-expressio...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4397815</comments>
            <pubDate>Mon, 17 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4397815</guid>        </item>
        <item>
            <title>Hyaluronan deposition and correlation with inflammation in a murine ovalbumin model of asthma.</title>
            <link>http://www.medworm.com/index.php?rid=4397814&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21251977%26dopt%3DAbstract</link>
            <description>Authors: Cheng G, Swaidani S, Sharma M, Lauer ME, Hascall VC, Aronica MA
    Asthma is a chronic inflammatory disease of the airways characterized by airway remodeling, which includes changes in the extracellular matrix (ECM). However the role of the ECM in mediating these changes is poorly understood. Hyaluronan (HA), a major component of the ECM, has been implicated in asthma as well as in many other biological processes. Our study investigates the processes involved in HA synthesis, deposition, localization and degradation during an acute and chronic murine model of ovalbumin (OVA)-induced allergic pulmonary inflammation. Mice were sensitized, challenged to OVA and sacrificed at various time points during an 8-week challenge protocol. Bronchoalveolar lavage (BAL) fluids, blood, and lung...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4397814</comments>
            <pubDate>Mon, 17 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4397814</guid>        </item>
        <item>
            <title>Lysyl oxidase-like 3b is Critical for Cartilage Maturation During Zebrafish Craniofacial Development.</title>
            <link>http://www.medworm.com/index.php?rid=4397816&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21244857%26dopt%3DAbstract</link>
            <description>Authors: van Boxtel AL, Gansner JM, Hakvoort HW, Snell H, Legler J, Gitlin JD
    Vertebrate craniofacial development requires coordinated morphogenetic interactions between the extracellular matrix (ECM) and the differentiating chondrocytes essential for cartilage formation. Recent studies reveal a critical role for specific lysyl oxidases in ECM integrity required for embryonic development. We now demonstrate that loxl3b is abundantly expressed within the head mesenchyme of the zebrafish and is critically important for maturation of neural crest derived cartilage elements. Histological and ultrastructural analysis of cartilage elements in loxl3b morphant embryos reveals abnormal maturation of cartilage and altered chondrocyte morphology. Spatiotemporal analysis of craniofacial markers in...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4397816</comments>
            <pubDate>Sat, 15 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4397816</guid>        </item>
        <item>
            <title>The Multiple Fuctions of Collagen Xviii in Development and Disease.</title>
            <link>http://www.medworm.com/index.php?rid=4273617&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21163348%26dopt%3DAbstract</link>
            <description>Authors: Seppinen L, Pihlajaniemi T
    Collagen XVIII is a heparan sulphate proteoglycan which is expressed ubiquitously in different basement membranes throughout the body. Its C-terminal fragment, endostatin, has been found to inhibit angiogenesis and tumor growth by restricting endothelial proliferation and migration and inducing apoptosis of endothelial cells. Collagen XVIII has three variants, of which the shortest one is found in most vascular and epithelial BM structures, whereas the longer variants are found especially in the liver. The longest or frizzled variant has a cysteine-rich domain in its N-terminus that has been shown to inhibit Wnt signaling in vitro. The presence of collagen XVIII homologues in organisms such as C. elegans, Xenopus laevis, zebrafish and chick suggests ...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4273617</comments>
            <pubDate>Mon, 13 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4273617</guid>        </item>
        <item>
            <title>Syndecans as cell surface receptors: Unique structure equates with functional diversity.</title>
            <link>http://www.medworm.com/index.php?rid=4165262&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21062643%26dopt%3DAbstract</link>
            <description>Authors: Choi Y, Chung H, Jung H, Couchman JR, Oh ES
    An increasing number of functions for syndecan cell surface heparan sulfate proteoglycans have been proposed over the last decade. Moreover, aberrant syndecan regulation has been found to play a critical role in multiple pathologies, including cancers, as well as wound healing and inflammation. As receptors, they have much in common with other molecules on the cell surface. Syndecans are type I transmembrane molecules with cytoplasmic domains that link to the actin cytoskeleton and can interact with a number of regulators. However, they are also highly complex by virtue of their external glycosaminoglycan chains, especially heparan sulfate. This heterodisperse polysaccharide has the potential to interact with many ligands from divers...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4165262</comments>
            <pubDate>Sat, 06 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4165262</guid>        </item>
        <item>
            <title>Decorin modulates collagen I-stimulated, but not fibronectin-stimulated, migration of C2C12 myoblasts.</title>
            <link>http://www.medworm.com/index.php?rid=4165263&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21059388%26dopt%3DAbstract</link>
            <description>In this study we looked at the effects decorin on fibronectin- and collagen I-stimulated myoblast migration. Dose response studies demonstrated 10μg/ml, 5μg/ml and 25μg/ml as the optimal stimulatory concentrations of decorin (1.2 fold increase), fibronectin (3.5 fold increase) and collagen I (2.4 fold increase), when compared with control respectively. A synergistic effect was identified when decorin and collagen I were added in combination; this effect was not evident when decorin was added with fibronectin. The effects of these factors on the ROCK signalling pathway were also analyzed. ROCK-2 was identified as the key Rho-activated kinase isoform involved in migration, due to its higher expression levels and localisation to focal points within migrating C2C12 myoblasts. Decorin and co...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4165263</comments>
            <pubDate>Fri, 05 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4165263</guid>        </item>
        <item>
            <title>Substrate stiffness regulates apoptosis and the mRNA expression of extracellular matrix regulatory genes in the rat annular cells.</title>
            <link>http://www.medworm.com/index.php?rid=4165265&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21055467%26dopt%3DAbstract</link>
            <description>Authors: Zhang YH, Zhao CQ, Jiang LS, Dai LY
    Cells are subjected to static tension of different magnitudes when cultured on substrates with different stiffnesses. It has long been recognized that mechanical stress is an important modulator of the intervertebral disc degeneration. Here we studied the influence of substrate stiffness on cell morphology, apoptosis and extracellular matrix (ECM) metabolism of the rat annulus fibrosus (AF) cells which are known to be mechanosensitive cells. Polyacrylamide gel substrates with three different stiffnesses were prepared by varying the concentration of acrylamide and bisacrylamide, and the elastic modulus of the different gel substrates were measured with atomic force microscopy (AFM). First-passage rat annular cells were cultured on soft, inter...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4165265</comments>
            <pubDate>Tue, 02 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4165265</guid>        </item>
        <item>
            <title>MMPs are less efficient than ADAMTS5 in cleaving aggrecan core protein.</title>
            <link>http://www.medworm.com/index.php?rid=4165264&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21055468%26dopt%3DAbstract</link>
            <description>This study also uncovered a potential role for MMPs in the C-terminal truncation of aggrecan.
    PMID: 21055468 [PubMed - as supplied by publisher] (Source: Matrix Biology)</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4165264</comments>
            <pubDate>Tue, 02 Nov 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4165264</guid>        </item>
        <item>
            <title>Collagen binding specificity of the discoidin domain receptors: Binding sites on collagens II and III and molecular determinants for collagen IV recognition by DDR1.</title>
            <link>http://www.medworm.com/index.php?rid=4137916&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21044884%26dopt%3DAbstract</link>
            <description>Authors: Xu H, Raynal N, Stathopoulos S, Myllyharju J, Farndale RW, Leitinger B
    The discoidin domain receptors, DDR1 and DDR2 are cell surface receptor tyrosine kinases that are activated by triple-helical collagen. While normal DDR signalling regulates fundamental cellular processes, aberrant DDR signalling is associated with several human diseases. We previously identified GVMGFO (O is hydroxyproline) as a major DDR2 binding site in collagens I-III, and located two additional DDR2 binding sites in collagen II. Here we extend these studies to the homologous DDR1 and the identification of DDR binding sites on collagen III. Using sets of overlapping triple-helical peptides, the Collagen II and Collagen III Toolkits, we located several DDR2 binding sites on both collagens. The interactio...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4137916</comments>
            <pubDate>Thu, 28 Oct 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4137916</guid>        </item>
        <item>
            <title>Type XVII collagen (BP180) can function as a cell-matrix adhesion molecule via binding to laminin 332.</title>
            <link>http://www.medworm.com/index.php?rid=4137917&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21034821%26dopt%3DAbstract</link>
            <description>Authors: Van den Bergh F, Eliason SL, Giudice GJ
    Collagen XVII (COL17) is a transmembrane glycoprotein that is expressed on the basal surface of basal epidermal keratinocytes. Previous observations have led to the hypothesis that an interaction between COL17 and laminin 332, an extracellular matrix protein, contributes to the attachment of the basal keratinocyte to the basement membrane. In order to isolate and manipulate COL17 interactions with ECM components, we induced COL17 expression in two cells lines, SK-MEL1 and K562, that exhibit little or no capacity to attach to our test substrates, including laminin 332, types I and IV collagen, and fibronectin. Cells expressing high levels of COL17 preferentially adhered to a laminin 332 matrix, and, to a lesser extent, type IV collagen, w...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4137917</comments>
            <pubDate>Tue, 26 Oct 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4137917</guid>        </item>
        <item>
            <title>Fibrillin-3 expression in human development.</title>
            <link>http://www.medworm.com/index.php?rid=4107606&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20970500%26dopt%3DAbstract</link>
            <description>Authors: Sabatier L, Miosge N, Hubmacher D, Lin G, Davis EC, Reinhardt DP
    Fibrillin proteins are the major components of extracellular microfibrils found in many connective tissues. Fibrillin-1 and fibrillin-2 are well studied and mutations in these proteins cause a number of fibrillinopathies including Marfan syndrome and congenital contractural arachnodactyly, respectively. Fibrillin-3 was more recently discovered and is much less well characterized. Fibrillin-1 is expressed throughout life, whereas fibrillin-2 and -3 are thought to be primarily present during development. Here, we report detailed fibrillin-3 expression patterns in early human development. A polyclonal antiserum against a C-terminal recombinant half of human fibrillin-3 was produced in rabbit. Anti-fibrillin-3 antibo...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4107606</comments>
            <pubDate>Tue, 19 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4107606</guid>        </item>
        <item>
            <title>Dimerization of human lysyl hydroxylase 3 (LH3) is mediated by the amino acids 541-547.</title>
            <link>http://www.medworm.com/index.php?rid=4088092&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20955792%26dopt%3DAbstract</link>
            <description>Authors: Heikkinen J, Risteli M, Lampela O, Alavesa P, Karppinen M, Juffer AH, Myllylä R
    Lysyl hydroxylases (LH), which catalyze the post-translational modifications of lysines in collagen and collagen -like proteins, function as dimers. However, the amino acids responsible for dimerization and the role of dimer formation in the enzymatic activities of LH have not yet been identified. We have localized the region responsible for the dimerization of lysyl hydroxylase 3 (LH3), a multifunctional enzyme of collagen biosynthesis, to a sequence of amino acids between the glycosyltransferase activity and the lysyl hydroxylase activity domains. This area is covered by amino acids 541-547 in human LH3, but contains no cysteine residues. The region is highly conserved among LH isoforms, and is ...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4088092</comments>
            <pubDate>Thu, 14 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4088092</guid>        </item>
        <item>
            <title>Clonal overgrowth of esophageal smooth muscle cells in diffuse leiomyomatosis-Alport syndrome caused by partial deletion in COL4A5 and COL4A6 genes.</title>
            <link>http://www.medworm.com/index.php?rid=4088094&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20951201%26dopt%3DAbstract</link>
            <description>Authors: Oohashi T, Naito I, Ueki Y, Tomoki Y, Tanaka PR, Yoshio N, Ninomiya Y
    This is a study of a patient who manifests all of the features of a diffuse leiomyomatosis-Alport syndrome (DL-ATS), and her two-year-old son who has already been diagnosed with Alport syndrome. Fourteen years ago, the patient underwent a partial esophageal resection followed by a replacement with jejunum. Recently, she underwent a surgical resection of the esophagus due to esophageal dysfunction. Genetic analyses of COL4A5 and COL4A6 on the X-chromosome were efficiently performed using the genomic DNA of her son. We have identified a novel deletion of 194-kb in length, encompassing COL4A5-COL4A6 promoters as well as nearly the entire large intron 1 of COL4A5 and intron 2 of COL4A6. To uncover the relationsh...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4088094</comments>
            <pubDate>Tue, 12 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4088094</guid>        </item>
        <item>
            <title>Dysfunctional Tendon Collagen Fibrillogenesis in Collagen VI Null Mice.</title>
            <link>http://www.medworm.com/index.php?rid=4088093&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20951202%26dopt%3DAbstract</link>
            <description>Authors: Izu Y, Ansorge HL, Zhang G, Soslowsky LJ, Bonaldo P, Chu ML, Birk DE
    Tendons are composed of fibroblasts and collagen fibrils. The fibrils are organized uniaxially and grouped together into fibers. Collagen VI is a non-fibrillar collagen expressed in developing and adult tendons. Human collagen VI mutations result in muscular dystrophy, joint hyperlaxity and contractures. The purpose of this study is to determine the functional roles of collagen VI in tendon matrix assembly. During tendon development, collagen VI was expressed throughout the extracellular matrix, but enriched around fibroblasts and their processes. To analyze the functional roles of collagen VI a mouse model with a targeted inactivation of Col6a1 gene was utilized. Ultrastructural analysis of Col6a1-/- versus ...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4088093</comments>
            <pubDate>Tue, 12 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4088093</guid>        </item>
        <item>
            <title>Angiotensin converting enzyme inhibition blocks interstitial hyaluronan dissipation in the neonatal rat kidney via hyaluronan synthase 2 and hyaluronidase 1.</title>
            <link>http://www.medworm.com/index.php?rid=4061610&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20933085%26dopt%3DAbstract</link>
            <description>In conclusion, the high renal HA content is rapidly reduced due to reduced HAS2 and increased Hyal1 mRNA expressions. Normal angiotensin II-function is crucial for inducing these changes. Due to the extreme water-attracting and proinflammatory properties of HA, accumulation in the neonatally ACEI-treated kidneys may partly explain the pathological renal phenotype of the adult kidney, which include reduced urinary concentration ability and tubulointerstitial inflammation.
    PMID: 20933085 [PubMed - as supplied by publisher] (Source: Matrix Biology)</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4061610</comments>
            <pubDate>Mon, 04 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4061610</guid>        </item>
        <item>
            <title>Crystal Structure of the Human Collagen XV Trimerization Domain: A Potent Trimerizing Unit Common to Multiplexin Collagens.</title>
            <link>http://www.medworm.com/index.php?rid=4061612&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20932905%26dopt%3DAbstract</link>
            <description>Authors: Wirz JA, Boudko SP, Lerch TF, Chapman MS, Bächinger HP
    Correct folding of the collagen triple helix requires a self-association step which selects and binds α-chains into trimers. Here we report the crystal structure of the trimerization domain of human type XV collagen. The trimerization domain of type XV collagen contains three monomers each composed of four β-sheets and an α-helix. The hydrophobic core of the trimer is devoid of solvent molecules and is shaped by β-sheet planes from each monomer. The trimerization domain is extremely stable and forms at picomolar concentrations. It is found that the trimerization domain of type XV collagen is structurally similar to that of type XVIII, despite only 32 % sequence identity. High structural conservation indicates that the...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4061612</comments>
            <pubDate>Sun, 03 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4061612</guid>        </item>
        <item>
            <title>Fragmentation of Fibronectin by Inherent Autolytic and Matrix Metalloproteinase Activities.</title>
            <link>http://www.medworm.com/index.php?rid=4061611&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20932906%26dopt%3DAbstract</link>
            <description>Authors: Steffensen B, Chen Z, Pal S, Mikhailova M, Su J, Wang Y, Xu X
    Fibronectin (FN) purified by gelatin affinity chromatography is unstable and undergoes fragmentation. The cleavage has been ascribed to inherent autolytic protease activities as well as co-purified matrix metalloproteinases (MMP). Understanding the mechanism by which the proteolysis of FN occurs is important, because the FN fragments have biological activities that differ from those of intact FN. Having excluded contributions of other plasma-derived proteases, the present experiments demonstrated that cleavage of FN by MMP-2 to distinct fragments occurred in synergy with inherent FN activities. Limited heat treatment of FN at 56°C for 30min inactivated the inherent protease activities sharply reducing autolysis of ...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4061611</comments>
            <pubDate>Sun, 03 Oct 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4061611</guid>        </item>
        <item>
            <title>Sp7/Osterix is involved in the up-regulation of the mouse pro-α1(V) collagen gene (Col5a1) in osteoblastic cells.</title>
            <link>http://www.medworm.com/index.php?rid=4061613&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20888414%26dopt%3DAbstract</link>
            <description>Authors: Wu YF, Matsuo N, Sumiyoshi H, Yoshioka H
    Sp7/Osterix, a transcription factor whose expression is restricted in osteoblasts, belongs to the Sp family of transcription factor that bind to G/C-rich sequences. Previous studies have identified a Sp1binding site in the proximal promoter region of the mouse Col5a1 gene, but it did not activate or repress this gene in a mouse fibroblast cell line and a human rhabdomyosarcoma cell line. The purpose of the present study was to clarify the involvement of Sp7/Osterix in the mouse Col5a1 gene. A functional analysis revealed that mutation of the Sp1 binding site specifically decreased the promoter activity in osteoblastic cells. An overexpression of Sp7/Osterix significantly increased the promoter activity and the endogenous mRNA levels of ...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4061613</comments>
            <pubDate>Thu, 30 Sep 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4061613</guid>        </item>
        <item>
            <title>Regulation of Valvular Interstitial Cell Phenotype and Function by Hyaluronic Acid in 2-D and 3-D Culture Environments.</title>
            <link>http://www.medworm.com/index.php?rid=4061614&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20884350%26dopt%3DAbstract</link>
            <description>This study examines the contributions of exogenous and endogenous hyaluronic acid (HA), in both two-dimensional (2D) and 3D environments, in regulating the phenotype and calcification of VICs. VIC calcification was first assessed in a 2D setting in which the cells were exposed to different molecular weights of exogenous HA presented in either an immobilized or soluble form. Delivery of HA suppressed nodule formation in a molecular weight-dependent manner, while blocking VIC recognition of HA via an antibody to CD44 abolished these nodule-suppressive effects and stimulated other hallmarks of valvular dysfunction. These 2D results were then validated in a more physiologically-relevant setting, using an approach that allowed the characterization of VIC phenotype in response to HA alterations ...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4061614</comments>
            <pubDate>Thu, 23 Sep 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4061614</guid>        </item>
        <item>
            <title>Matrix remodeling stem cell recruitment: A novel in vitro model for homing of human bone marrow stromal cells to the site of injury shows crucial role of extracellular collagen matrix.</title>
            <link>http://www.medworm.com/index.php?rid=3962267&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20828613%26dopt%3DAbstract</link>
            <description>Authors: Mauney J, Olsen BR, Volloch V
    The goal of the present study was to devise an in vitro model suitable for investigations of the homing of mesenchymal stem cells to sites of injury. Such a model was designed on the basis of a &quot;transwell&quot;assay, with an insert seeded with human bone marrow stromal cells and a well with a desired cell type. To mimic physiological environment and to simulate &quot;injury&quot;, cells in a well were maintained not only on tissue culture plastic but also on collagens I and IV, major matrix components in musculoskeletal and adipose tissues respectively, and subjected to a severe thermal stress. The results obtained showed a massive translocation of bone marrow stromal cells through the inserts' membrane toward the &quot;injury&quot; site. Unexpectedly, it emerged that col...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3962267</comments>
            <pubDate>Sun, 05 Sep 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3962267</guid>        </item>
        <item>
            <title>Extracellular matrix-derived products modulate endothelial and progenitor cell migration and proliferation in vitro and stimulate regenerative healing in vivo.</title>
            <link>http://www.medworm.com/index.php?rid=3915699&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20797438%26dopt%3DAbstract</link>
            <description>Authors: Vorotnikova E, McIntosh D, Dewilde A, Zhang J, Reing JE, Zhang L, Cordero K, Bedelbaeva K, Gourevitch D, Heber-Katz E, Badylak SF, Braunhut SJ
    Most adult mammals heal without restorative replacement of lost tissue and instead form scar tissue at an injury site. One exception is the adult MRL/MpJ mouse that can regenerate ear and cardiac tissue after wounding with little evidence of scar tissue formation. Following production of a MRL mouse ear hole, 2mm in diameter, a structure rapidly forms at the injury site that resembles the amphibian blastema at a limb amputation site during limb regeneration. We have isolated MRL blastemal cells (MRL-B) from this structure and adapted them to culture. We demonstrate by RT-PCR that even after continuous culturing of these cells they maint...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3915699</comments>
            <pubDate>Sun, 22 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3915699</guid>        </item>
        <item>
            <title>An experimental model for studying the biomechanics of embryonic tendon: Evidence that the development of mechanical properties depends on the actinomyosin machinery.</title>
            <link>http://www.medworm.com/index.php?rid=3915701&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20736063%26dopt%3DAbstract</link>
            <description>In conclusion, the mechanical properties per se of the tendon constructs are attributable to the ECM generated by the cells but the improvement of mechanical properties during time in culture was dependent on non-muscle myosin II-derived forces.
    PMID: 20736063 [PubMed - as supplied by publisher] (Source: Matrix Biology)</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3915701</comments>
            <pubDate>Fri, 20 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3915701</guid>        </item>
        <item>
            <title>Synthesis of embryonic tendon-like tissue by human marrow stromal/mesenchymal stem cells requires a three-dimensional environment and transforming growth factor ss3.</title>
            <link>http://www.medworm.com/index.php?rid=3915700&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20736064%26dopt%3DAbstract</link>
            <description>In conclusion, MSCs that self-generate TGFbeta signaling or the addition of TGFbeta3 protein to BM-MNCs in fixed-length fibrin gels spontaneously make embryonic tendon-like tissue in vitro within 7days.
    PMID: 20736064 [PubMed - as supplied by publisher] (Source: Matrix Biology)</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3915700</comments>
            <pubDate>Fri, 20 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3915700</guid>        </item>
        <item>
            <title>Nanofibers in a hyaluronan-based pericellular matrix.</title>
            <link>http://www.medworm.com/index.php?rid=3900158&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20732419%26dopt%3DAbstract</link>
            <description>Authors: Gerlach D, Kaminski T, PÃ©rez-Willard F, Kirfel G, Gieselmann V, Kappler J
    The extracellular matrix of the brain is a highly organized hyaluronan-based supramolecular assembly that is involved in neuronal pathfinding, cell migration, synaptogenesis and neuronal plasticity. Here, we analyze the structure of the hyaluronan-rich pericellular matrix of an oligodendroglial precursor cell line using helium ion beam scanning microscopy at a subnanometer resolution. We find that thin nanofibers are the ultimate building elements of this oligodendroglial pericellular matrix. These structures may participate in the regulation of oligodendroglial maturation and motility.
    PMID: 20732419 [PubMed - as supplied by publisher] (Source: Matrix Biology)</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3900158</comments>
            <pubDate>Thu, 19 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3900158</guid>        </item>
        <item>
            <title>Interaction between the extracellular matrix and lymphatics - consequences for lymphangiogenesis and lymphatic function.</title>
            <link>http://www.medworm.com/index.php?rid=3900159&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20727409%26dopt%3DAbstract</link>
            <description>Authors: Wiig H, Keskin D, Kalluri R
    The lymphatic system is important for body fluid balance as well as immunological surveillance. Due to the identification of new molecular markers during the last decade, there has been a recent dramatic increase in our knowledge on the molecular mechanisms involved in lymphatic vessel growth (lymphangiogenesis) and lymphatic function. Here we review data showing that although it is often overlooked, the extracellular matrix plays an important role in the generation of new lymphatic vessels as a response to physiological and pathological stimuli. Extracellular matrix-lymphatic interactions as well as biophysical characteristics of the stroma have consequences for tumor formation, growth and metastasis. During the recent years, anti-lymphangiogenesis...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3900159</comments>
            <pubDate>Mon, 16 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3900159</guid>        </item>
        <item>
            <title>Cryptic domains of tenascin-C differentially control fibronectin fibrillogenesis.</title>
            <link>http://www.medworm.com/index.php?rid=3882281&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20708078%26dopt%3DAbstract</link>
            <description>Authors: To WS, Midwood KS
    The three-dimensional organization of the ubiquitous extracellular matrix glycoprotein fibronectin regulates cell fate and morphogenesis during development; in particular tubule formation that constitutes the vasculature, lung and kidney. Tenascin-C is a matrix protein with a restricted expression pattern; it is specifically up-regulated at sites of fibronectin fibril assembly during development and in remodeling adult tissues. Here we demonstrate that specific domains of tenascin-C inhibit fibronectin matrix assembly whereas full-length tenascin-C does not. These domains act via distinct mechanisms: TNfn1-8 blocks fibrillogenesis by binding to fibronectin fibrils and preventing intermolecular fibronectin interactions whilst FBG acts independently of binding ...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3882281</comments>
            <pubDate>Mon, 09 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3882281</guid>        </item>
        <item>
            <title>Expression in SPARC-null mice of collagen type I lacking the globular domain of the alpha1(I) N-propeptide results in abdominal hernias and loss of dermal collagen.</title>
            <link>http://www.medworm.com/index.php?rid=3882280&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20708079%26dopt%3DAbstract</link>
            <description>Authors: Card L, Henderson N, Zhang Y, Bornstein P, Bradshaw AD
    The sequence encoding the N-propeptide of collagen I is characterized by significant conservation of amino acids across species; however, the function of the N-propeptide remains poorly defined. Studies in vitro have suggested that one activity of this propeptide might be to act as a feedback inhibitor of collagen I synthesis. To determine whether the N-propeptide contributed to decreased collagen content in SPARC-null mice, mice carrying a deletion of exon 2, which encodes the globular domain of the N-propeptide of collagen I, were crossed to SPARC-null animals. Mice lacking SPARC and expressing collagen I without the globular domain of the N-propeptide were viable and fertile. However, a significant number of animals dev...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3882280</comments>
            <pubDate>Mon, 09 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3882280</guid>        </item>
        <item>
            <title>Nano-structure of the laminin gamma-1 short arm reveals an extended and curved multidomain assembly.</title>
            <link>http://www.medworm.com/index.php?rid=3833679&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20688161%26dopt%3DAbstract</link>
            <description>Authors: Patel TR, Morris GA, Zwolanek D, Keene DR, Li J, Harding SE, Koch M, Stetefeld J
    Laminins are multidomain glycoproteins that play important roles in development and maintenance of the extracellular matrix via their numerous interactions with other proteins. Several receptors for the laminin short arms revealed their importance in network formation and intercellular signaling. However, both the detailed structure of the laminin gamma-1 short arm and its organization within the complexes is poorly understood due to the complexity of the molecule and the lack of a high-resolution structure. The presented data provide the first subatomic resolution structure for the laminin gamma-1 short arm in solution. This was achieved using an integrated approach that combined a number of comp...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3833679</comments>
            <pubDate>Sun, 01 Aug 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3833679</guid>        </item>
        <item>
            <title>Fibroblast growth factor - 2 binding to the endothelial basement membrane peaks at a physiologically relevant shear stress.</title>
            <link>http://www.medworm.com/index.php?rid=3824110&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20678572%26dopt%3DAbstract</link>
            <description>Authors: Reisig K, Clyne AM
    Fibroblast growth factor-2 (FGF2) is produced and released by endothelial cells and binds to heparan sulfate proteoglycans in the endothelial basement membrane (BM), an important FGF2 storage reservoir. Experimental and computational models of FGF2 binding kinetics to both cells and BM under static conditions are well established in the literature but remain largely unexplored under flow. We now examine BM-FGF2 binding kinetics in fluid flow conditions. We hypothesized that FGF2 binding to the endothelial BM would decrease as fluid shear stress increased. To investigate this, BM-FGF2 equilibrium, associative, and dissociative binding were measured at various shear stresses. Surprisingly, FGF2 binding increased up to a physiological arterial shear stress of 2...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3824110</comments>
            <pubDate>Thu, 29 Jul 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3824110</guid>        </item>
        <item>
            <title>Zebrafish type XVII collagen: Gene structures, expression profiles, and morpholino &quot;knock-down&quot; phenotypes.</title>
            <link>http://www.medworm.com/index.php?rid=3824111&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20670682%26dopt%3DAbstract</link>
            <description>Zebrafish type XVII collagen: Gene structures, expression profiles, and morpholino &quot;knock-down&quot; phenotypes.
    Matrix Biol. 2010 Jul 26;
    Authors: Kim SH, Choi HY, So JH, Kim CH, Ho SY, Frank M, Li Q, Uitto J
    The human COL17A1 gene encodes type XVII collagen (also known as the 180-kDa bullous pemphigoid antigen), an integral component of hemidesmosomes, attachment complexes providing integrity to the dermal-epidermal junction. Zebrafish, a facile model system to study skin development, displays fully developed hemidesmosomes at approximately 5days post-fertilization (dpf). We have identified two COL17A1 orthologues in the zebrafish genome, col17a1a and col17a1b, which are expressed in the skin and the neural system, respectively. The proteins coded by these genes have structural mo...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3824111</comments>
            <pubDate>Sun, 25 Jul 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3824111</guid>        </item>
        <item>
            <title>Periostin is a collagen associated bone matrix protein regulated by parathyroid hormone.</title>
            <link>http://www.medworm.com/index.php?rid=3795094&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20654714%26dopt%3DAbstract</link>
            <description>In conclusion, the present study provides novel observations related to the expression, distribution and regulation of periostin in bone cells and extracellular matrix.
    PMID: 20654714 [PubMed - as supplied by publisher] (Source: Matrix Biology)</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3795094</comments>
            <pubDate>Mon, 19 Jul 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3795094</guid>        </item>
        <item>
            <title>Modulatory effect of interleukin-1alpha on expression of structural matrix proteins, MMPs and TIMPs in human cardiac myofibroblasts: Role of p38 MAP kinase.</title>
            <link>http://www.medworm.com/index.php?rid=3759168&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20619343%26dopt%3DAbstract</link>
            <description>Authors: Turner NA, Warburton P, O'Regan DJ, Ball SG, Porter KE
    The proinflammatory cytokine interleukin-1 (IL-1) elicits catabolic effects on the myocardial extracellular matrix (ECM) early after myocardial infarction but there is little understanding of its direct effects on cardiac myofibroblasts (CMF), or the role of p38 mitogen-activated protein kinase (MAPK). We used a focused RT-PCR microarray to investigate the effects of IL-1alpha on expression of 41 ECM genes in CMF cultured from different patients, and explored regulation by p38 MAPK. IL-1alpha (10ng/ml, 6h) had minimal effect on mRNA expression of structural ECM proteins, including collagens, laminins, fibronectin and vitronectin. However, it induced marked increases in expression of specific ECM proteases, including matrix...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3759168</comments>
            <pubDate>Tue, 06 Jul 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3759168</guid>        </item>
        <item>
            <title>Skeletal muscle weakness in osteogeneis imperfecta mice.</title>
            <link>http://www.medworm.com/index.php?rid=3759167&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20619344%26dopt%3DAbstract</link>
            <description>In this study we examined the soleus (S), plantaris (P), gastrocnemius (G), tibialis anterior (TA) and quadricep (Q) muscles of mice expressing mild (+/oim) and moderately severe (oim/oim) OI for evidence of inherent muscle pathology. In particular, muscle weight, fiber cross-sectional area (CSA), fiber type, fiber histomorphology, fibrillar collagen content, absolute, relative and specific peak tetanic force (P(o,) P(o)/mg and P(o)/CSA respectively) of individual muscles were evaluated. Oim/oim mouse muscles were generally smaller, contained less fibrillar collagen, had decreased P(o) and an inability to sustain P(o) for the 300-ms testing duration for specific muscles; +/oim mice had a similar but milder skeletal muscle phenotype. +/oim mice had mild weakness of specific muscles but were...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3759167</comments>
            <pubDate>Mon, 05 Jul 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3759167</guid>        </item>
        <item>
            <title>Mechanisms of Emphysema in Autosomal Dominant Cutis Laxa.</title>
            <link>http://www.medworm.com/index.php?rid=3733986&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20600892%26dopt%3DAbstract</link>
            <description>Authors: Hu Q, Shifren A, Sens C, Choi J, Szabo Z, Starcher BC, Knutsen RH, Shipley JM, Davis EC, Mecham RP, Urban Z
    Heterozygous elastin gene mutations cause autosomal dominant cutis laxa associated with emphysema and aortic aneurysms. To investigate the molecular mechanisms leading to cutis laxa in vivo, we generated transgenic mice by pronuclear injection of minigenes encoding normal human tropoelastin (WT) or tropoelastin with a cutis laxa mutation (CL). Three independent founder lines of CL mice showed emphysematous pulmonary airspace enlargement. No consistent dermatological or cardiovascular pathologies were observed. One CL and one WT line were selected for detailed studies. Both mutant and control transgenic animals showed elastin deposition into pulmonary elastic fibers, indi...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3733986</comments>
            <pubDate>Sun, 27 Jun 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3733986</guid>        </item>
        <item>
            <title>T-lymphocytes mediate left ventricular fibrillar collagen crosslinking and diastolic dysfunction in mice.</title>
            <link>http://www.medworm.com/index.php?rid=3733984&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20600894%26dopt%3DAbstract</link>
            <description>Authors: Yu Q, Vazquez R, Zabadi S, Watson RR, Larson DF
    Aberrant concentrations of cardiac extracellular matrix (ECM) fibrillar collagen crosslinking have been proposed to be an underlying cause of cardiac diastolic dysfunction however the role of the adaptive immune system in this process has yet to be investigated. Fibrillar collagen crosslinking is a product of the enzymatic activities of lysyl oxidase (LOX and LOXL-3) released by the cardiac fibroblast and possibly cardiac myocytes. Our hypothesis is that stimulation of the TH1 lymphocytes activates lysyl oxidase mediated ECM crosslinking and thereby alter left ventricular function. Three-month old C57BL/J female mice were treated with selective TH1 lymphocyte inducers - T-cell receptor Vbeta peptides (TCR). After 6weeks, candidat...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3733984</comments>
            <pubDate>Thu, 24 Jun 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3733984</guid>        </item>
        <item>
            <title>Inducible macropinocytosis of hyaluronan in B16-F10 melanoma cells.</title>
            <link>http://www.medworm.com/index.php?rid=3733985&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20600893%26dopt%3DAbstract</link>
            <description>Authors: Greyner HJ, Wiraszka T, Zhang LS, Petroll WM, Mummert ME
    Hyaluronan (HA) is a glycosaminoglycan composed of N-acetylglucosamine and glucuronic acid subunits. Endocytosis is thought to play an essential role in the catabolism of HA due to the intracellular compartmentalization of the HA degrading hyaluronidase enzymes. Previous investigations have shown that keratinocytes, chondrocytes and breast tumor cell lines endocytose HA via the cell surface glycoprotein, CD44. However, other cell types endocytose HA using a CD44-independent mechanism that remains to be defined. The purpose of this study was to investigate HA endocytosis in B16-F10 melanoma cells. We found that B16-F10 melanoma cells expressed CD44 on their surfaces. Unexpectedly, CD44 did not play a role in the endocytos...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3733985</comments>
            <pubDate>Tue, 22 Jun 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3733985</guid>        </item>
        <item>
            <title>The cell biology of suturing tendons.</title>
            <link>http://www.medworm.com/index.php?rid=3733983&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20600895%26dopt%3DAbstract</link>
            <description>In conclusion, the suture repair of injured tendons produces acellular zones, which may potentially cause early tendon failure.
    PMID: 20600895 [PubMed - as supplied by publisher] (Source: Matrix Biology)</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3733983</comments>
            <pubDate>Sun, 20 Jun 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3733983</guid>        </item>
        <item>
            <title>Perlecan deficiency causes muscle hypertrophy, a decrease in myostatin expression, and changes in muscle fiber composition.</title>
            <link>http://www.medworm.com/index.php?rid=3659748&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20541011%26dopt%3DAbstract</link>
            <description>Authors: Xu Z, Ichikawa N, Kosaki K, Yamada Y, Sasaki T, Sakai LY, Kurosawa H, Hattori N, Arikawa-Hirasawa E
    Perlecan is a component of the basement membrane that surrounds skeletal muscle. The aim of the present study is to identify the role of perlecan in skeletal muscle hypertrophy and myostatin signaling, with and without mechanical stress, using a mouse model (Hspg2(-/-)-Tg) deficient in skeletal muscle perlecan. We found that myosin heavy chain (MHC) type IIb fibers in the tibialis anterior (TA) muscle of Hspg2(-/-)-Tg mice had a significantly increased fiber cross-sectional area (CSA) compared to control (WT-Tg) mice. Hspg2(-/-)-Tg mice also had an increased number of type IIx fibers in the TA muscle. Myostatin and its type I receptor (ALK4) expression was substantially decrease...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3659748</comments>
            <pubDate>Mon, 07 Jun 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3659748</guid>        </item>
        <item>
            <title>Defective proteoglycan sulfation of the growth plate zones causes reduced chondrocyte proliferation via an altered Indian hedgehog signalling.</title>
            <link>http://www.medworm.com/index.php?rid=3581995&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20470884%26dopt%3DAbstract</link>
            <description>Authors: Gualeni B, Facchini M, De Leonardis F, Tenni R, Cetta G, Viola M, Passi A, Superti-Furga A, Forlino A, Rossi A
    Mutations in the sulfate transporter gene, SCL26A2, lead to cartilage proteoglycan undersulfation resulting in chondrodysplasia in humans; the phenotype is mirrored in the diastrophic dysplasia (dtd) mouse. It remains unclear whether bone shortening and deformities are caused solely by changes in the cartilage matrix, or whether chondroitin sulfate proteoglycan undersulfation affects also signalling pathways involved in cell proliferation and differentiation. Therefore we studied macromolecular sulfation in the different zones of the dtd mouse growth plate and these data were related to growth plate histomorphometry and proliferation analysis. A 2-fold increase of non...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3581995</comments>
            <pubDate>Mon, 10 May 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3581995</guid>        </item>
        <item>
            <title>HDAC-mediated control of ERK- and PI3K-dependent TGF-beta-induced extracellular matrix-regulating genes.</title>
            <link>http://www.medworm.com/index.php?rid=3581994&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20470885%26dopt%3DAbstract</link>
            <description>Authors: Barter MJ, Pybus L, Litherland GJ, Rowan AD, Clark IM, Edwards DR, Cawston TE, Young DA
    Histone deacetylases (HDACs) regulate the acetylation of histones in the control of gene expression. Many non-histone proteins are also targeted for acetylation, including TGF-beta signalling pathway components such as Smad2, Smad3 and Smad7. Our studies in mouse C3H10T1/2 fibroblasts suggested that a number of TGF-beta-induced genes that regulate matrix turnover are selectively regulated by HDACs. Blockade of HDAC activity with trichostatin A (TSA) abrogated the induction of a disintegrin and metalloproteinase 12 (Adam12) and tissue inhibitor of metalloproteinases-1 (Timp-1) genes by TGF-beta, whereas plasminogen activator inhibitor-1 (Pai-1) expression was unaffected. Analysis of the acti...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3581994</comments>
            <pubDate>Mon, 10 May 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3581994</guid>        </item>
        <item>
            <title>Methylglyoxal-Modified Collagen Promotes Myofibroblast Differentiation.</title>
            <link>http://www.medworm.com/index.php?rid=3515573&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20423729%26dopt%3DAbstract</link>
            <description>Authors: Yuen A, Laschinger C, Talior I, Lee W, Chan M, Birek J, Young EW, Sivagurunathan K, Won E, Simmons CA, McCulloch CA
    Fibrosis is a frequent complication of diabetes mellitus in many organs and tissues but the mechanism of how diabetes-induced glycation of extracellular matrix proteins impacts the formation of fibrotic lesions is not defined. As fibrosis is mediated by myofibroblasts, we investigated the effect of collagen glycation on the conversion of human cardiac fibroblasts to myofibroblasts. Collagen glycation was modeled by the glucose metabolite, methylglyoxal (MGO). Cells cultured on MGO-treated collagen exhibited increased activity of the alpha-smooth muscle actin promoter and enhanced expression of alpha-smooth muscle actin, ED-A fibronectin and cadherin, which are ma...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3515573</comments>
            <pubDate>Fri, 23 Apr 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3515573</guid>        </item>
        <item>
            <title>Secreted phosphoprotein 1 binds integrins to initiate multiple cell signaling pathways, including FRAP1/mTOR, to support attachment and force-generated migration of trophectoderm cells.</title>
            <link>http://www.medworm.com/index.php?rid=3467486&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20385232%26dopt%3DAbstract</link>
            <description>Authors: Kim J, Erikson DW, Burghardt RC, Spencer TE, Wu G, Bayless KJ, Johnson GA, Bazer FW
    Attachment and migration of trophectoderm (Tr) cells, hallmarks of blastocyst implantation in mammals, are unique uterine events. Secreted phosphoprotein 1 (SPP1) in the uterus binds integrins on conceptus Tr and uterine luminal epithelium (LE), affecting cell-cell and cell-matrix interactions. The signal transduction pathways activated by SPP1 and integrins in conceptuses have not been elucidated. Results of this study demonstrate that SPP1 binds alphavbeta3 and alpha5beta1 integrins to induce focal adhesion assembly, a prerequisite for adhesion and migration of Tr, through activation of: 1) P70S6K via crosstalk between FRAP1/mTOR and MAPK pathways; 2) mTOR, PI3K, MAPK3/MAPK1 (Erk1/2) and MAPK...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3467486</comments>
            <pubDate>Thu, 08 Apr 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3467486</guid>        </item>
        <item>
            <title>LTBP-2 has multiple heparin/heparan sulfate binding sites.</title>
            <link>http://www.medworm.com/index.php?rid=3467487&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20382221%26dopt%3DAbstract</link>
            <description>In this study we investigated the molecular interactions of LTBP-2 with heparin and heparan sulfate proteoglycans (HSPGs) since unidentified cell surface HSPGs are critical for normal fiber assembly. In solid phase assays, heparin conjugated to albumin (HAC) bound strongly to recombinant full length human LTBP-2. This interaction was completely blocked by addition of excess heparin, but not chondroitin sulfate, confirming specificity. Analysis of binding to LTBP-2 fragments showed that HAC bound strongly to N-terminal fragment LTBP-2 NT(H) and more weakly to central fragment LTBP-2 C(H). No binding was detected to C-terminal fragment LTBP-2 CT(H). Kds for heparin binding were calculated for full-length LTBP-2, LTBP-2 NT(H) and LTBP-2 C(H) as 0.9 nM, 0.7 nM and 80 nM respectively. HAC inter...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3467487</comments>
            <pubDate>Wed, 07 Apr 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3467487</guid>        </item>
        <item>
            <title>Syndecan-4 and beta1 integrin are regulated by electrical activity in skeletal muscle: Implications for cell adhesion.</title>
            <link>http://www.medworm.com/index.php?rid=3449914&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20362053%26dopt%3DAbstract</link>
            <description>Authors: Ugarte G, Santander C, Brandan E
    Syndecan-4 and integrins are involved in the cell migration and adhesion processes in several cell types. Syndecan-4, a transmembrane heparan sulfate proteoglycan, is associated to focal adhesions in adherent cells and has been described as a marker of satellite cells in skeletal muscle. In this tissue, beta1 integrin forms heterodimers with alpha5 and alpha6 during myoblast differentiation and with alpha7 in adult muscle. Here, we show that the levels of these two cell surface membrane molecules are regulated by spontaneous electrical activity during the differentiation of rat primary myoblasts. Syndecan-4 and beta1 integrin protein levels decrease after the inhibition of electrical activity using tetrodotoxin (TTX). Syndecan-4 also decreases ...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3449914</comments>
            <pubDate>Mon, 29 Mar 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3449914</guid>        </item>
        <item>
            <title>Age-dependent changes in the structure, composition and biophysical properties of a human basement membrane.</title>
            <link>http://www.medworm.com/index.php?rid=3449913&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20362054%26dopt%3DAbstract</link>
            <description>Authors: Candiello J, Cole GJ, Halfter W
    Basement membranes (BMs) are considered to be uniform, approximately 100nm-thin extracellular matrix sheets that serve as a substrate for epithelial cells, endothelial cells and myotubes. To find out whether BMs maintain their ultrastructure, protein composition and biophysical properties throughout life the natural aging history of the human inner limiting membranes (ILM) was investigated. The ILM is a BM at the vitreal surface of the retina that connects the retina with the vitreous. Transmission electron microscopy (TEM) showed that the ILM steadily increases in thickness from 70nm at fetal stages to several microns at age 90. By the age of 20, the ILM loses its laminated structure to become an amorphous and very irregular extracellular matri...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3449913</comments>
            <pubDate>Mon, 29 Mar 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3449913</guid>        </item>
        <item>
            <title>Loss of collagen-receptor DDR1 delays renal fibrosis in hereditary type IV collagen disease.</title>
            <link>http://www.medworm.com/index.php?rid=3399745&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20307660%26dopt%3DAbstract</link>
            <description>Authors: Gross O, Girgert R, Beirowki B, Kretzler M, Kang HG, Kruegel J, Miosge N, Busse AC, Segerer S, Vogel WF, M&amp;#xFC;ller GA, Weber M
    Alport syndrome is a hereditary type IV collagen disease leading progressive renal fibrosis, hearing loss and ocular changes. End stage renal failure usually develops during adolescence. COL4A3 -/- mice serve as an animal model for progressive renal scarring in Alport syndrome. The present study evaluates the role of Discoidin Domain Receptor 1 (DDR1) in cell-matrix-interaction involved in pathogenesis of Alport syndrome including renal inflammation and fibrosis. DDR1/COL4A3 double-knockouts were compared to COL4A3 -/- mice with 50% or 100% expression of DDR1, wildtype controls and to DDR1-/- COL4A3 +/+ controls for over 6 years. Double-knockouts liv...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3399745</comments>
            <pubDate>Fri, 19 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3399745</guid>        </item>
        <item>
            <title>Ameloblast differentiation in the human developing tooth: Effects of extracellular matrices.</title>
            <link>http://www.medworm.com/index.php?rid=3354876&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20211728%26dopt%3DAbstract</link>
            <description>In this study we have characterized ameloblast differentiation in human developing incisors, and have further investigated the role of extracellular matrix proteins on ameloblast differentiation. Histological and immunohistochemical analyses showed that in the human tooth, the basement membrane separating the early developing dental epithelium and mesenchyme was lost shortly before dentin deposition was initiated, prior to enamel matrix secretion. Presecretary ameloblasts elongated as they came into contact with the dentin matrix, and then shortened to become secretory ameloblasts. In situ hybridization showed that at the presecretory stage of odontoblasts expressed type I collagen mRNA, and also briefly expressed amelogenin mRNA. This was followed by upregulation of amelogenin mRNA expres...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3354876</comments>
            <pubDate>Thu, 04 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3354876</guid>        </item>
        <item>
            <title>From the Editor's Desk Osteoporosis and hot flashes - a molecular connection?</title>
            <link>http://www.medworm.com/index.php?rid=3303127&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20171555%26dopt%3DAbstract</link>
            <description>Authors: 
    
    PMID: 20171555 [PubMed - in process] (Source: Matrix Biology)</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3303127</comments>
            <pubDate>Thu, 25 Feb 2010 00:18:05 +0100</pubDate>
            <guid isPermaLink="false">3303127</guid>        </item>
        <item>
            <title>Pl-nectin, a discoidin family member, is a ligand for betaC integrins in the sea urchin embryo.</title>
            <link>http://www.medworm.com/index.php?rid=3284742&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20159038%26dopt%3DAbstract</link>
            <description>Authors: Zito F, Burke RD, Matranga V
    Pl-nectin is a component of the extracellular matrix that surrounds embryos of the sea urchin Paracentrotus lividus. Pl-nectin mediates adhesion of dissociated embryonic cells to substrates and interfering with ectodermic cells contacting Pl-nectin results in defects in skeleton growth and morphogenesis. Recently, we reported that Pl-nectin is a new member of the discoidin family, in agreement with the notion that many discoidin-containing proteins are involved in cell adhesion processes as integrin ligands. To better understand the molecular basis for the interaction of Pl-nectin with ectoderm, we investigated the hypothesis that Pl-nectin is an integrin ligand in sea urchin embryos. We show that in P. lividus embryos, betaC-containing integrins l...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3284742</comments>
            <pubDate>Sat, 13 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3284742</guid>        </item>
        <item>
            <title>Matrix Metalloproteinase-3 In Articular Cartilage Is Upregulated By Joint Immobilization And Suppressed By Passive Joint Motion.</title>
            <link>http://www.medworm.com/index.php?rid=3276924&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20153826%26dopt%3DAbstract</link>
            <description>Authors: Leong DJ, Gu XI, Li Y, Lee JY, Laudier DM, Majeska RJ, Schaffler MB, Cardoso L, Sun HB
    Both underloading and overloading of joints can lead to articular cartilage degradation, a process mediated in part by matrix metalloproteinases (MMPs). Here we examine the effects of reduced loading of rat hindlimbs on articular cartilage expression of MMP-3, which not only digests matrix components but also activates other proteolytic enzymes. We show that hindlimb immobilization resulted in elevated mRNA expression at 6 hours that was sustained throughout the 21day immobilization period. MMP-3 upregulation was higher in the medial condyle than the lateral, and was greatest in the superficial cartilage zone, followed by middle and deep zones. These areas also showed decreases in safranin O...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276924</comments>
            <pubDate>Thu, 11 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276924</guid>        </item>
        <item>
            <title>Adult equine bone-marrow stromal cells produce a cartilage-like ECM mechanically superior to animal-matched adult chondrocytes.</title>
            <link>http://www.medworm.com/index.php?rid=3276923&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20153827%26dopt%3DAbstract</link>
            <description>Authors: Kopesky PW, Lee HY, Vanderploeg EJ, Kisiday JD, Frisbie DD, Plaas AH, Ortiz C, Grodzinsky AJ
    Our objective was to evaluate the age-dependent mechanical phenotype of bone marrow stromal cell- (BMSC-) and chondrocyte-produced cartilage-like neotissue and to elucidate the matrix-associated mechanisms which generate this phenotype. Cells from both immature (2-4 month-old foals) and skeletally-mature (2-5 year-old adults) mixed-breed horses were isolated from animal-matched bone marrow and cartilage tissue, encapsulated in self-assembling-peptide hydrogels, and cultured with and without TGF-beta1 supplementation. BMSCs and chondrocytes from both donor ages were encapsulated with high viability. BMSCs from both ages produced neo-tissue with higher mechanical stiffness than that prod...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3276923</comments>
            <pubDate>Thu, 11 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3276923</guid>        </item>
        <item>
            <title>Tissue section AFM: In situ ultrastructural imaging of native biomolecules.</title>
            <link>http://www.medworm.com/index.php?rid=3263151&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20144712%26dopt%3DAbstract</link>
            <description>Authors: Graham HK, Hodson NW, Hoyland JA, Millward-Sadler SJ, Garrod D, Scothern A, Griffiths CE, Watson RE, Cox TR, Erler JT, Trafford AW, Sherratt MJ
    Conventional approaches for ultrastructural high resolution imaging of biological specimens induce profound changes in bio-molecular structures. By combining tissue cryo-sectioning with non-destructive atomic force microscopy (AFM) imaging we have developed a methodology that may be applied by the non-specialist to both preserve and visualize biomolecular structures (in particular extracellular matrix assemblies) in situ. This tissue section AFM technique is capable of: i) resolving nm-microm scale features of intra- and extra-cellular structures in tissue cryosections; ii) imaging the same tissue region before and after experimental i...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3263151</comments>
            <pubDate>Fri, 05 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3263151</guid>        </item>
        <item>
            <title>Interaction between cartilage oligomeric matrix protein and extracellular matrix protein 1 mediates endochondral bone growth.</title>
            <link>http://www.medworm.com/index.php?rid=3255265&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20138147%26dopt%3DAbstract</link>
            <description>Authors: Kong L, Tian Q, Guo F, Mucignat MT, Perris R, Sercu S, Merregaert J, Di Cesare PE, Liu CJ
    In an effort to define the biological functions of COMP, a functional genetic screen was performed. This led to the identification of extracellular matrix protein 1 (ECM1) as a novel COMP-associated partner. COMP directly binds to ECM1 both in vitro and in vivo. The EGF domain of COMP and the C-terminus of ECM1 mediate the interaction between them. COMP and ECM1 Colocalize in the Growth Plates in Vivo. ECM1 inhibits chondrocyte hypertrophy, matrix mineralization, and endochondral bone formation, and COMP overcomes the inhibition by ECM1. In addition, COMP-mediated neutralization of ECM1 inhibition depends on their interaction, since COMP largely fails to overcome the ECM1 inhibition in th...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3255265</comments>
            <pubDate>Tue, 02 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3255265</guid>        </item>
        <item>
            <title>Characterization of the Six Zebrafish Clade B Fibrillar Procollagen Genes, with Evidence for Evolutionarily Conserved Alternative Splicing within the pro-alpha1(V) C-propeptide.</title>
            <link>http://www.medworm.com/index.php?rid=3220882&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20102740%26dopt%3DAbstract</link>
            <description>Authors: Hoffman GG, Branam AM, Huang G, Pelegri F, Cole WG, Wenstrup RM, Greenspan DS
    Genes for tetrapod fibrillar procollagen chains can be divided into two clades, A and B, based on sequence homologies and differences in protein domain and gene structures. Although the major fibrillar collagen types I-III comprise only clade A chains, the minor fibrillar collagen types V and XI comprise both clade A chains and the clade B chains pro-alpha1(V), pro-alpha3(V), pro-alpha1(XI) and pro-alpha2(XI), in which defects can underlie various genetic connective tissue disorders. Here we characterize the clade B procollagen chains of zebrafish. We demonstrate that in contrast to the four tetrapod clade B chains, zebrafish have six clade B chains, designated here as pro-alpha1(V), pro-alpha3(V)a a...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3220882</comments>
            <pubDate>Sat, 23 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3220882</guid>        </item>
        <item>
            <title>Reduced versican cleavage due to Adamts9 haploinsufficiency is associated with cardiac and aortic anomalies.</title>
            <link>http://www.medworm.com/index.php?rid=3213053&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20096780%26dopt%3DAbstract</link>
            <description>Authors: Kern CB, Wessels A, McGarity J, Dixon LJ, Alston E, Argraves WS, Geeting D, Nelson CM, Menick DR, Ape SS
    Here, we demonstrate that ADAMTS9, a highly conserved versican-degrading protease, is required for correct cardiovascular development and adult homeostasis. Analysis of Adamts9(+/LacZ) heterozygous adult mice revealed anomalies in the aortic wall, valvulosinus and valve leaflets. Abnormal myocardial projections and 'spongy' myocardium consistent with non-compaction of the left ventricle were also found in Adamts9(+/LacZ) mice. During development, Adamts9 was expressed in derivatives of the Secondary Heart Field, vascular smooth muscle cells (VSMC) in the arterial wall, mesenchymal cells of the valves, and non-myocardial cells of the ventricular myocardium but expression als...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3213053</comments>
            <pubDate>Wed, 20 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3213053</guid>        </item>
        <item>
            <title>The role of small leucine-rich proteoglycans in collagen fibrillogenesis.</title>
            <link>http://www.medworm.com/index.php?rid=3186361&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20080181%26dopt%3DAbstract</link>
            <description>Authors: Kalamajski S, Oldberg A
    Small leucine-rich proteoglycans/proteins (SLRPs) are associated with collagen fibril formation, and therefore important for the proper formation of extracellular matrices. SLRPs are differentially expressed in tissues and during pathological conditions, contributing to the development of connective tissue properties. The binding of SLRPs to collagens have recently been characterized, and may give some clues to the significance of these interactions. In this minireview, we summarize published work in this field, and propose several mechanisms for how SLRPs can control collagen matrix structure and function. SLRPs appear to influence collagen cross-linking patterns. We also propose that the SLRP-collagen interactions can assist in the process of juxtapos...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3186361</comments>
            <pubDate>Thu, 14 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3186361</guid>        </item>
        <item>
            <title>Matrix Biology meets Toxinology.</title>
            <link>http://www.medworm.com/index.php?rid=3186364&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20079834%26dopt%3DAbstract</link>
            <description>Authors: Eble JA
    Venoms are cocktails containing pharmacologically active compounds, which drastically affect essential functions of the neuromuscular and cardiovascular system, as well as of blood, kidney and other organs. As the extracellular matrix and its contacts with cells are responsible for maintaining the integrity and functionality of these organs and tissues, it is not surprising that several venom components target matrix molecules and their respective cellular receptors. Many venom components, such as matrix-degrading enzymes, disintegrins, and C-type lectin-like proteins, have been identified and have helped to found the frontier research field of matrix toxinology. Interestingly, many toxins consist of domains which are structurally homologous to modules and domains of m...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3186364</comments>
            <pubDate>Wed, 13 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3186364</guid>        </item>
        <item>
            <title>Degradation of hydroxyapatite in vivo and in vitro requires osteoclastic sodium-bicarbonate co-transporter NBCn1.</title>
            <link>http://www.medworm.com/index.php?rid=3186363&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20079835%26dopt%3DAbstract</link>
            <description>Authors: Riihonen R, Nielsen S, V&amp;#xE4;&amp;#xE4;n&amp;#xE4;nen HK, Laitala-Leinonen T, Kwon TH
    Dissolution of the inorganic bone matrix releases not only calcium and phosphate ions, but also bicarbonate. Electroneutral sodium-bicarbonate co-transporter (NBCn1) is expressed in inactive osteoclasts, but its physiological role in bone resorption has remained unknown. We show here that NBCn1, encoded by the SLC4A7 gene, is directly involved in bone resorption. NBCn1 protein was specifically found at the bone-facing ruffled border areas, and metabolic acidosis increased NBCn1 expression in rats in vivo. In human hematopoietic stem cell cultures, NBCn1 mRNA expression was observed only after formation of resorbing osteoclasts. To further confirm the critical role of NBCn1 during bone resorption, hu...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3186363</comments>
            <pubDate>Wed, 13 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3186363</guid>        </item>
        <item>
            <title>Dentin sialophosphoprotein (DSPP) is cleaved into its two natural dentin matrix products by three isoforms of bone morphogenetic protein-1 (BMP1).</title>
            <link>http://www.medworm.com/index.php?rid=3186362&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20079836%26dopt%3DAbstract</link>
            <description>In this study, full-length recombinant mouse DSPP was made for the first time in furin-deficient mammalian LoVo cells and used to test the ability of three different isoforms of one candidate protease, bone morphogenetic protein-1 (BMP1) to cleave DSPP at the appropriate site. Furthermore, two reported enhancers of BMP1/mTLD activity (procollagen C-endopeptidase enhancer-1, PCPE-1, and secreted frizzled-related protein-2, sFRP2) were tested for their abilities to modulate BMP1-mediated processing of both DSPP and another SIBLING family member with a similar cleavage motif, dentin matrix protein-1 (DMP1). Three splice variants of BMP1 (classic BMP1, the full-length mTolloid (mTLD), and the shorter isoform lacking the CUB3 domain, BMP1-5) were all shown to cleave the recombinant DSPP in vitr...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3186362</comments>
            <pubDate>Wed, 13 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3186362</guid>        </item>
        <item>
            <title>pH effects on the hyaluronan hydrolysis catalysed by hyaluronidase in the presence of proteins : Part I. Dual aspect of the pH-dependence.</title>
            <link>http://www.medworm.com/index.php?rid=3137687&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20043995%26dopt%3DAbstract</link>
            <description>Authors: Lenormand H, Deschrevel B, Vincent JC
    Hyaluronan (HA) hydrolysis catalysed by hyaluronidase (HAase) is strongly inhibited when performed at a low ratio of HAase to HA concentrations and at low ionic strength. This is because long HA chains can form non-active complexes with HAase. Bovine serum albumin (BSA) is able to compete with HAase to form electrostatic complexes with HA so freeing HAase which then recovers its catalytic activity. This BSA-dependence is characterised by two main domains separated by the optimal BSA concentration: below this concentration the HAase activity increases when the BSA concentration is increased, above this concentration the HAase activity decreases. This occurs provided that HA is negatively charged and BSA positively charged, i.e. in a pH rang...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3137687</comments>
            <pubDate>Mon, 28 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3137687</guid>        </item>
        <item>
            <title>Characterizing molecular diffusion in the lens capsule.</title>
            <link>http://www.medworm.com/index.php?rid=3114046&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20026402%26dopt%3DAbstract</link>
            <description>Authors: Danysh BP, Patel TP, Czymmek KJ, Edwards DA, Wang L, Pande J, Duncan MK
    The lens capsule compartmentalizes the cells of the avascular lens from other ocular tissues. Small molecules required for lens cell metabolism, such as glucose, salts, and waste products, freely pass through the capsule. However, the lens capsule is selectively permeable to proteins such as growth hormones and substrate carriers which are required for proper lens growth and development. We used fluorescence recovery after photobleaching (FRAP) to characterize the diffusional behavior of various sized dextrans (3, 10, 40, 150, and 250kDa) and proteins endogenous to the lens environment (EGF, gammaD-crystallin, BSA, transferrin, ceruloplasmin, and IgG) within the capsules of whole living lenses. We found th...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3114046</comments>
            <pubDate>Fri, 18 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3114046</guid>        </item>
        <item>
            <title>Using human neural crest-derived progenitor cells to investigate osteogenesis: An in vitro study.</title>
            <link>http://www.medworm.com/index.php?rid=3114045&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20026403%26dopt%3DAbstract</link>
            <description>Authors: Degistirici O, Grabellus F, Irsen S, Schmid KW, Thie M
    Human tooth contains a distinct population of neural crest-derived progenitor cells (dNC-PCs) which are known to give rise to specialized daughter cells of an osteogenic lineage. We hypothesised that dNC-PCs could develop into neural crest-derived bone in a self-propagating and extracorporal culture system. Thus, we examined the three-dimensional structure obtained from osteogenic-stimulated dNC-PCs by morphological, biochemical and spectroscopic methods. After the onset of stimulation, cells formed a multilayer with outer cells covering the surface and inner cells secreting a hyaline matrix. With prolonged culture, multilayers contracted and formed a three-dimensional construct which subsequently converted to a calcified ...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3114045</comments>
            <pubDate>Fri, 18 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3114045</guid>        </item>
        <item>
            <title>Effect of activation of viral receptors on the gelatinases MMP-2 and MMP-9 in human mesothelial cells.</title>
            <link>http://www.medworm.com/index.php?rid=3114044&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20026404%26dopt%3DAbstract</link>
            <description>CONCLUSIONS: With these results we provide evidence for a mechanism by which infectious agents can mediate processes of the final common path of inflammation as fibrosis via regulation of MMP and TIMP.
    PMID: 20026404 [PubMed - as supplied by publisher] (Source: Matrix Biology)</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3114044</comments>
            <pubDate>Fri, 18 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3114044</guid>        </item>
        <item>
            <title>Type I collagen promotes epithelial-mesenchymal transition through ILK-dependent activation of NF-kappaB and LEF-1.</title>
            <link>http://www.medworm.com/index.php?rid=3105564&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20018240%26dopt%3DAbstract</link>
            <description>Authors: Medici D, Nawshad A
    Collagen I has been shown to promote epithelial-mesenchymal transition (EMT), a critical process of embryonic development and disease progression. However, little is known about the signaling mechanisms by which collagen I induces this cellular transformation. Here we show that collagen I causes ILK-dependent phosphorylation of IkappaB and subsequent nuclear translocation of active NF-kappaB, which in turn promotes increased expression of the Snail and LEF-1 transcription factors. ILK also causes inhibitory phosphorylation of GSK-3beta, a kinase that prevents functional activation of both Snail and LEF-1. These transcription factors alter expression of epithelial and mesenchymal markers to initiate EMT and stimulate cell migration. These data provide a foun...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3105564</comments>
            <pubDate>Mon, 14 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3105564</guid>        </item>
        <item>
            <title>Imbalance between matrix metalloproteinases and tissue inhibitor of metalloproteinases in hypertensive vascular remodeling.</title>
            <link>http://www.medworm.com/index.php?rid=3075389&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19969080%26dopt%3DAbstract</link>
            <description>Authors: Castro MM, Rizzi E, Prado CM, Rossi MA, Tanus-Santos JE, Gerlach RF
    Structural vascular changes in two-kidney, one-clip (2K-1C) hypertension may result from increased matrix metalloproteinase (MMP)-2 activity. MMP-2 activation is regulated by other MMPs, including transmembrane-MMPs, and by tissue inhibitors of MMPs (TIMPs). We have investigated the localization of MMP-2, -9, -14, and TIMPs 1-4 in hypertensive aortas and measured their levels by zymography/Western blotting and immunohistochemistry. Gelatinolytic activity was assayed in tissues by in situ zymography. Sham-operated and 2K-1C hypertensive rats were treated with doxycycline (or vehicle) for 8weeks, and the systolic blood pressure was monitored weekly. Doxycycline attenuated 2K-1C hypertension (165+/-11.7mmHg versu...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3075389</comments>
            <pubDate>Fri, 04 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3075389</guid>        </item>
        <item>
            <title>Collagen XVI induces formation of focal contacts on intestinal myofibroblasts isolated from the normal and inflamed intestinal tract.</title>
            <link>http://www.medworm.com/index.php?rid=3033828&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19931388%26dopt%3DAbstract</link>
            <description>Authors: Ratzinger S, Eble JA, Pasoldt A, Opolka A, Rogler G, Grifka J, Gr&amp;#xE4;ssel S
    In Crohn's disease (CD) the stress-shield of intestinal subepithelial myofibroblasts (ISEMF) provided by intact tissue is disturbed due to inflammation and thus, cells start with remodelling activities. This is characterized by increased numbers of collagen-producing ISEMF causing an uncontrolled, irreversible wound-healing response to the chronic inflammation of the gastrointestinal tract. Reconstitution of the original ECM leads ISEMF to exit this cycle. In contrast, during fibrosis, ISEMF persist. It is known that ISEMF produce and deposit collagen types I, III, IV and V; however synthesis and the role of fibrillar peripheral molecules like collagen type XVI have not been addressed yet. Here, we h...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3033828</comments>
            <pubDate>Tue, 17 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3033828</guid>        </item>
        <item>
            <title>The human alpha11 integrin promoter drives fibroblast-restricted expression in vivo and is regulated by TGF-beta1 in a Smad- and Sp1-dependent manner.</title>
            <link>http://www.medworm.com/index.php?rid=3000759&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19913614%26dopt%3DAbstract</link>
            <description>Authors: Lu N, Ranta J, Heuchel R, Soininen R, Gullberg D
    Integrin alpha11beta1 is expressed by ectomesenchymally- and mesodermally- derived fibroblasts and is the major collagen receptor on embryonic fibroblasts. We have previously characterized a 3kb human alpha11 promoter region in vitro. In the current study we generated promoter-LacZ reporter transgenic mice to examine the ability of the 3kb alpha11 promoter to drive tissue-specific expression also in vivo. Our data show that the alpha11 promoter region that we have characterized contains most of the regulatory elements that direct ectomesenchymal and mesodermal fibroblast-specific expression. Not much is known about integrin alpha11 regulation by TGF-beta family members and the potential role of alpha11 in TGF-beta1 driven proces...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3000759</comments>
            <pubDate>Wed, 11 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3000759</guid>        </item>
        <item>
            <title>Hyaluronan oligosaccharides promote excisional wound healing through enhanced angiogenesis.</title>
            <link>http://www.medworm.com/index.php?rid=3000758&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19913615%26dopt%3DAbstract</link>
            <description>In this study, we prepared a special slow-releasing gel that contains a mixture of defined size of o-HA and studied the healing effects of o-HA by topical application to an acute wound model. We report that o-HA complex promotes the repair of tissue injury of a murine excisional dermal wound. The therapy by o-HA was compared with high molecular weight HA (HMW-HA) and the known angiogenesis stimulator, VEGF. At days 6 to 8 after treatment, significant differences were seen in wound closure rates between o-HA and control or HMW-HA groups, in which o-HA showed an increased wound recovery. Histological analysis revealed that increased neo-blood and lymph vessels were formed in wounded tissues treated by o-HA. In addition, treatments of wounds with o-HA resulted in more granulation productionco...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3000758</comments>
            <pubDate>Wed, 11 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3000758</guid>        </item>
        <item>
            <title>Platelet Derived Growth Factor B and Epithelial Mesenchymal Transition of Peritoneal Mesothelial Cells.</title>
            <link>http://www.medworm.com/index.php?rid=2985394&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19896531%26dopt%3DAbstract</link>
            <description>Authors: Patel P, West-Mays J, Kolb M, Rodrigues JC, Hoff CM, Margetts PJ
    Platelet derived growth factor (PDGF) is involved in wound healing in various organ systems. Its potential role in the context of peritoneal injury following long term peritoneal dialysis is unclear. We used an adenovirus expressing the B chain of PDGF (AdPDGF-B) to assess its effect on pro-fibrotic pathways in the peritoneal membrane. To assess the transforming growth factor (TGF) beta independent effects of PDGF, we over-expressed PDGF-B in the peritoneum of either wild-type mice (Smad3(+/+)) or those with a deletion of the TGFbeta signaling protein Smad3 (Smad3(-/-)). PDGF-B induced sustained angiogenesis in both Smad3(+/+) and Smad3(-/-) mice. Despite increased collagen gene expression, collagen accumulation ...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2985394</comments>
            <pubDate>Wed, 04 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2985394</guid>        </item>
        <item>
            <title>Transient tropoelastin nanoparticles are early-stage intermediates in the coacervation of human tropoelastin whose aggregation is facilitated by heparan sulfate and heparin decasaccharides.</title>
            <link>http://www.medworm.com/index.php?rid=2985395&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19895887%26dopt%3DAbstract</link>
            <description>We describe novel 200-300nm spherical particles that serve as intermediates in the formation of the coacervate. Their aggregation gives 800nm to 1microm species. This process is facilitated by heparan sulfate and dermatan sulfate interactions which effectively lower the critical concentration to facilitate this transition. This coacervation process was examined using a panel of heparin chains of various lengths and showed greatest efficacy for the decasaccharide, followed by the octasaccharide, while the hexasaccharide displayed the shortest efficacious length. We propose that these oligosaccharide interactions enable the charge-mediated aggregation of positively charged tropoelastin. This biochemistry models glycosaminoglycan interactions on the cell surface during elastogenesis which is ...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2985395</comments>
            <pubDate>Tue, 03 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2985395</guid>        </item>
        <item>
            <title>FAK mediates signal crosstalk between type II collagen and TGF-beta 1 cascades in chondrocytic cells.</title>
            <link>http://www.medworm.com/index.php?rid=2912607&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19840848%26dopt%3DAbstract</link>
            <description>In this study, expression of pSMAD 2, pSMAD 3, pFAK(Y397) and pFAK(Y925) were synergistically increased by co-treatment with type II collagen and TGF-beta1 in articular chondrocytes. The proliferation of porcine articular chondrocytes and GAG secretion in SW1353 cells were synergistically increased by co-stimulation with type II collagen and TGF-beta1. Synergistically increased expression and nuclear translocation of pSMAD 2 and pSMAD 3 and GAG secretion of SW1353 cells were significantly inhibited by siFAK transfection. Therefore, we suggest that FAK-SMAD 2/3 mediates signal crosstalk between type II collagen and TGF-beta1 and regulates GAG secretion in chondrocytic cells.
    PMID: 19840848 [PubMed - as supplied by publisher] (Source: Matrix Biology)</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2912607</comments>
            <pubDate>Thu, 15 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2912607</guid>        </item>
        <item>
            <title>Extracellular matrix assembly and organization during zebrafish gastrulation.</title>
            <link>http://www.medworm.com/index.php?rid=2912606&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19840849%26dopt%3DAbstract</link>
            <description>Authors: Latimer A, Jessen JR
    Zebrafish gastrulation entails morphogenetic cell movements that shape the body plan and give rise to an embryo with defined anterior-posterior and dorsal-ventral axes. Regulating these cell movements are diverse signaling pathways and proteins including Wnts, Src-family tyrosine kinases, cadherins, and matrix metalloproteinases. While our knowledge of how these proteins impact cell polarity and migration has advanced considerably in the last decade, almost no data exist regarding the organization of extracellular matrix (ECM) during zebrafish gastrulation. Here, we describe for the first time the assembly of a fibronectin (FN) and laminin containing ECM in the early zebrafish embryo. This matrix was first detected at early gastrulation (65% epiboly) in th...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2912606</comments>
            <pubDate>Thu, 15 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2912606</guid>        </item>
        <item>
            <title>Leberagin-C, a disintegrin-like/cysteine rich protein from Macrovipera lebetina transmediterranea venom, inhibits alpha-v-beta-3 integrin-mediated cell adhesion.</title>
            <link>http://www.medworm.com/index.php?rid=2872292&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19808093%26dopt%3DAbstract</link>
            <description>Authors: Limam I, Bazaa A, Srairi-Abid N, Taboubi S, Jebali J, Zouari-Kessentini R, Kallech-Ziri O, Mejdoub H, Hammami A, El Ayeb M, Luis J, Marrakchi N
    Leberagin-C, a new member of the disintegrin-like/cysteine-rich (D/C) family, was purified to homogeneity from the venom of Tunisian snake Macrovipera lebetina transmediterranea. It is a monomeric protein with a molecular mass of 25,787Da. Its complete sequence of 205 amino acids residues was established by cDNA cloning. The leberagin-C shows many conserved sequences with other known D/C proteins, like the SECD binding sites and a pattern of 28 cysteines. It is the first purified protein from Macrovipera lebetina transmediterranea with only two disintegrin-like/cysteine-rich domains. Leberagin-C is able to inhibit platelet aggregation ...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2872292</comments>
            <pubDate>Fri, 02 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2872292</guid>        </item>
        <item>
            <title>Two Dicarbonyl compounds, 3-deoxyglucosone and methylglyoxal, differentially modulate dermal fibroblasts.</title>
            <link>http://www.medworm.com/index.php?rid=2864750&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19800404%26dopt%3DAbstract</link>
            <description>Authors: Sassi-Gaha S, Loughlin DT, Kappler F, Schwartz ML, Su B, Tobia AM, Artlett CM
    Advanced glycation endproducts accumulate on long-lived proteins such as collagens as a function of diet and age and mediate the cross-linking of those proteins causing changes in collagen pathophysiology resulting in the disruption of normal collagen matrix remodeling. Two commonly studied advanced glycation endproduct precursors 3-deoxyglucosone and methylglyoxal were investigated for their role in the modification of collagen and on extracellular matrix expression. Fibroblasts cultured on methylglyoxal cross-linked matrices increased the expression of collagen, active TGF-beta1, beta1-integrin, and decreased Smad7; whereas 3-deoxyglucosone decreased collagen, active TGF-beta1, beta1-integrin but i...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2864750</comments>
            <pubDate>Tue, 29 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2864750</guid>        </item>
        <item>
            <title>Identification of alpha-dystroglycan binding sequences in the laminin alpha2 chain LG4-5 module.</title>
            <link>http://www.medworm.com/index.php?rid=2864751&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19800000%26dopt%3DAbstract</link>
            <description>In this study, heparin and alpha-dystroglycan binding sequences were identified using 42 overlapping synthetic peptides from the LG4-5 module and using recombinant LG4-5 protein (rec-alpha2LG4-5). Physiological activities of the active peptides were also examined in explants of submandibular glands. Heparin binding screens showed that the A2G78 peptide (GLLFYMARINHA) bound to heparin and prevented its binding to rec-alpha2LG4-5. Furthermore, alanine substitution of the arginine residue in the A2G78 site on rec-alpha2LG4-5 decreased heparin binding activity. When alpha-dystroglycan binding of the peptides was screened, two peptides, A2G78 and A2G80 (VQLRNGFPYFSY), bound alpha-dystroglycan. A2G78 and A2G80 also inhibited alpha-dystroglycan binding of rec-alpha2LG4-5. A2G78 and A2G80 specific...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2864751</comments>
            <pubDate>Mon, 28 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2864751</guid>        </item>
        <item>
            <title>Myeloperoxidase-derived oxidants selectively disrupt the protein core of the heparan sulfate proteoglycan perlecan.</title>
            <link>http://www.medworm.com/index.php?rid=2856105&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19788922%26dopt%3DAbstract</link>
            <description>Authors: Rees MD, Whitelock JM, Malle E, Chuang CY, Iozzo RV, Nilasaroya A, Davies MJ
    The potent oxidants hypochlorous acid (HOCl) and hypobromous acid (HOBr) are produced extracellularly by myeloperoxidase, following release of this enzyme from activated leukocytes. The subendothelial extracellular matrix is a key site for deposition of myeloperoxidase and damage by myeloperoxidase-derived oxidants, with this damage implicated in the impairment of vascular cell function during acute inflammatory responses and chronic inflammatory diseases such as atherosclerosis. The heparan sulfate proteoglycan perlecan, a key component of the subendothelial extracellular matrix, regulates important cellular processes and is a potential target for HOCl and HOBr. It is shown here that perlecan binds m...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2856105</comments>
            <pubDate>Fri, 25 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2856105</guid>        </item>
        <item>
            <title>Impaired wound healing in mice lacking the basement membrane protein nidogen 1.</title>
            <link>http://www.medworm.com/index.php?rid=2824531&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19766719%26dopt%3DAbstract</link>
            <description>Authors: Baranowsky A, Mokkapati S, Bechtel M, Kr&amp;#xFC;gel J, Miosge N, Wickenhauser C, Smyth N, Nischt R
    Nidogen 1 and 2 are ubiquitous basement membrane (BM) components, whose interactions in particular with laminin, collagen IV and perlecan have been considered important for BM formation. Genetic deletion of either NID gene does not reveal BM alterations suggesting compensatory roles for nidogen 1 and 2. However, neurological deficits in nidogen 1 null mice, not seen in the absence of nidogen 2, also suggest isoform specific functions. To test this further, skin wound healing which requires BM reformation was studied in adult nidogen 1 deficient mice. Although re-epithelization was not altered, the newly formed epidermis showed marked hyperproliferation and a delay in differentiatio...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2824531</comments>
            <pubDate>Wed, 16 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2824531</guid>        </item>
        <item>
            <title>Adult human bone marrow stromal cells regulate expression of their MMPs and TIMPs in differentiation type-specific manner.</title>
            <link>http://www.medworm.com/index.php?rid=2824532&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19765656%26dopt%3DAbstract</link>
            <description>Authors: Mauney J, Volloch V
    Previously, we described a profound impact of structural conformation of collagen matrix on osteogenic and adipogenic differentiation of bone marrow stromal cells. Thus, a marginal p38-independent adipogenesis on native collagen I matrix contrasts with an efficient p38-dependent differentiation on denatured collagen I. An efficient Hsp90-dependent osteogenesis occurs on native collagen I matrix but not on its denatured counterpart where it is insignificant and proceeds in an Hsp90-independent manner. Whereas only marginal osteogenesis and no detectable adipogenesis of bone marrow stromal cells occur on native collagen IV, the same matrix supports a highly efficient adipogenesis in denatured structural state. The present study addresses the opposite directio...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2824532</comments>
            <pubDate>Mon, 14 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2824532</guid>        </item>
        <item>
            <title>Human bone marrow-derived stromal cells show highly efficient thermal stress-resistant adipogenesis on denatured collagen IV matrix but not on its native counterpart.</title>
            <link>http://www.medworm.com/index.php?rid=2810244&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19761844%26dopt%3DAbstract</link>
            <description>Authors: Mauney J, Volloch V
    Collagen IV is the major matrix component associated with differentiating adipocytes in adipose tissues, and the understanding of its contribution in adipogenic differentiation could be important for elucidation of mechanisms and processes driving the obesity. Therefore, in the light of our previous findings of differential effects of structural conformation of collagen I matrix on differentiation of bone marrow stromal cells, we investigated whether similar phenomenon occurs on collagen IV matrix in native and denatured structural states. The results of the present study show that native collagen IV is unsupportive of adipogenic differentiation and very little if any adipogenesis occurs on this matrix in the presence of adipogenic stimuli. In sharp contras...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2810244</comments>
            <pubDate>Sun, 13 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2810244</guid>        </item>
        <item>
            <title>A novel functional role of iduronate-2-sulfatase in zebrafish early development.</title>
            <link>http://www.medworm.com/index.php?rid=2810243&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19761845%26dopt%3DAbstract</link>
            <description>Authors: Moro E, Tomanin R, Friso A, Modena N, Tiso N, Scarpa M, Argenton F
    Sulfated glycosaminoglycan chains of extracellular matrix and cell membrane-tethered proteoglycans exert specific cellular functions by interacting with a broad spectrum of morphogens and growth factors. In humans, a congenital impaired catabolism of sulfated glycosaminoglycans is associated with severe metabolic disorders. Here, we report on the identification and characterization of a zebrafish iduronate sulfatase orthologue. By knocking down its function with antisense morpholino oligos, we demonstrate that iduronate sulfatase plays a critical role during early vertebrate development and its downregulation may be responsible for severe developmental defects, including a misshapen trunk and abnormal craniofac...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2810243</comments>
            <pubDate>Sun, 13 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2810243</guid>        </item>
        <item>
            <title>Specific processing of tenascin-C by the metalloprotease meprinbeta neutralizes its inhibition of cell spreading.</title>
            <link>http://www.medworm.com/index.php?rid=2797530&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19748582%26dopt%3DAbstract</link>
            <description>Authors: Ambort D, Brellier F, Becker-Pauly C, St&amp;#xF6;cker W, Andrejevic-Blant S, Chiquet M, Sterchi EE
    The metalloprotease meprin has been implicated in tissue remodelling due to its capability to degrade extracellular matrix components. Here, we investigated the susceptibility of tenascin-C to cleavage by meprinbeta and the functional properties of its proteolytic fragments. A set of monoclonal antibodies against chicken and human tenascin-C allowed the mapping of proteolytic fragments generated by meprinbeta. In chicken tenascin-C, meprinbeta processed all three major splicing variants by removal of 10kDa N-terminal and 38kDa C-terminal peptides, leaving a large central part of subunits intact. A similar cleavage pattern was found for large human tenascin-C variant where two N-term...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2797530</comments>
            <pubDate>Thu, 10 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2797530</guid>        </item>
        <item>
            <title>A comparison of different purification methods of aggrecan fragments from human articular cartilage and synovial fluid.</title>
            <link>http://www.medworm.com/index.php?rid=2789281&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19744558%26dopt%3DAbstract</link>
            <description>Authors: Struglics A, Larsson S
    In the study of aggrecan fragmentation several methods to extract and purify aggrecan from cartilage and synovial fluid (SF) are used. This work compares and evaluates the effectiveness for purification of aggrecan of the most commonly used methods by the ratio of sulfated glycosaminoglycan (sGAG) to protein and by fragment analysis by Western blot. A novel method for purification of aggrecan fragments from SF by boiling (Boiled SF) is also presented. Of the sGAG extracted from cartilage by guanidinium, 66% was recovered by associative-dissociative cesium chloride density gradient centrifugation (A1D1-D3) with a 9 times higher ratio of sGAG to protein in the A1D1 fraction. Although less enriched in aggrecan, the Western blot aggrecan pattern of the guani...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2789281</comments>
            <pubDate>Sun, 06 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2789281</guid>        </item>
        <item>
            <title>Dynamic loading stimulates chondrocyte biosynthesis when encapsulated in charged hydrogels prepared from poly(ethylene glycol) and chondroitin sulfate.</title>
            <link>http://www.medworm.com/index.php?rid=2759290&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19720146%26dopt%3DAbstract</link>
            <description>In conclusion, extracellular events associated with a charged matrix has a dramatic affect on how chondrocytes respond to mechanical stimulation within these artificial 3D matrices suggesting that streaming potentials and/or dynamic changes in osmolarity may be important regulators of chondrocytes while cell deformation and fluid flow appear to have less of an effect.
    PMID: 19720146 [PubMed - as supplied by publisher] (Source: Matrix Biology)</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2759290</comments>
            <pubDate>Thu, 27 Aug 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2759290</guid>        </item>
        <item>
            <title>LRP1 regulates remodeling of the extracellular matrix by fibroblasts.</title>
            <link>http://www.medworm.com/index.php?rid=2735163&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19699300%26dopt%3DAbstract</link>
            <description>Authors: Gaultier A, Hollister M, Reynolds I, Hsieh EH, Gonias SL
    Low density lipoprotein receptor-related protein (LRP1) is an endocytic receptor for diverse proteases, protease inhibitors, and other plasma membrane proteins, including the urokinase receptor (uPAR). LRP1 also functions in cell-signaling and regulates gene expression. The goal of this study was to determine whether LRP1 regulates remodeling of provisional extracellular matrix (ECM) by fibroblasts. To address this problem, we utilized an in vitro model in which type I collagen was reconstituted and overlaid with fibronectin. Either the collagen or fibronectin was fluorescently-labeled. ECM remodeling by fibroblasts deficient in LRP1, uPAR, or MT1-MMP was studied. MT1-MMP was required for efficient remodeling of the deep...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2735163</comments>
            <pubDate>Tue, 18 Aug 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2735163</guid>        </item>
        <item>
            <title>The alpha 2 chain of collagen type VI sequesters latent proforms of matrix-metalloproteinases and modulates their activation and activity.</title>
            <link>http://www.medworm.com/index.php?rid=2735165&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19698785%26dopt%3DAbstract</link>
            <description>In conclusion, the alpha2(VI) chain modulates MMP availability by sequestering proMMPs in the ECM, blocking proteolytic activity. Therefore, CVI and especially its alpha2(VI) chain might serve as a lead structure for MMP-based therapeutics which modulate the action of these matrix components, e.g. in fibrosis and cancer.
    PMID: 19698785 [PubMed - as supplied by publisher] (Source: Matrix Biology)</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2735165</comments>
            <pubDate>Mon, 17 Aug 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2735165</guid>        </item>
        <item>
            <title>Evidence against proteoglycan mediated collagen fibril load transmission and dynamic viscoelasticity in tendon.</title>
            <link>http://www.medworm.com/index.php?rid=2735164&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19698786%26dopt%3DAbstract</link>
            <description>Authors: Fessel G, Snedeker JG
    The glycosaminoglycan (GAG) dermatan sulphate and chondroitin sulphate side-chains of small leucine-rich proteoglycans have been increasingly posited to act as molecular cross links between adjacent collagen fibrils and to directly contribute to tendon elasticity. GAGs have also been implicated in tendon viscoelasticity, supposedly affecting frictional loss during elongation or fluid flow through the extra cellular matrix. The current study sought to systematically test these theories of tendon structure-function by investigating the mechanical repercussions of enzymatic depletion of GAG complexes by chondroitinase ABC in a reproducible tendon structure-function model (rat tail fascicles). The extent of GAG removal (at least 93%) was verified by relevant ...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2735164</comments>
            <pubDate>Mon, 17 Aug 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2735164</guid>        </item>
        <item>
            <title>Defining the Role of Laminin-332 in Carcinoma.</title>
            <link>http://www.medworm.com/index.php?rid=2713181&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19686849%26dopt%3DAbstract</link>
            <description>Authors: Guess CM, Quaranta V
    The deadly feature of cancer, metastasis, requires invasion of cells through basement membranes (BM), which normally act as a barrier between tissue compartments. In the case of many epithelially-derived cancers (carcinomas), Laminin-332 (Ln-5 332) is a key component of the BM barrier. This review provides a historical examination of Ln-332 from its discovery through identification of its functions in BM and possible role in carcinomas. Current understanding points to distinct roles for the three Ln-332 subunits (alpha3, beta3, gamma2) in cell adhesion, extracellular matrix stability, and cell signaling processes in cancer. Given the large number of studies linking Ln-332 gamma2 subunit with cancer prognosis, particular attention is given to the crucial ro...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2713181</comments>
            <pubDate>Thu, 13 Aug 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2713181</guid>        </item>
        <item>
            <title>ADAM17 Co-purifies with TIMP-3 and Modulates Endothelial Invasion Responses in Three-Dimensional Collagen Matrices.</title>
            <link>http://www.medworm.com/index.php?rid=2691912&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19666115%26dopt%3DAbstract</link>
            <description>In this study, we investigated potential mechanisms through which the known anti-angiogenic factor, tissue inhibitor of metalloproteinase-3 (TIMP-3) blocks angiogenesis. As a strategy to identify TIMP-3 binding proteins, we used tandem affinity purification, employing recombinant adenoviruses constructed to deliver TIMP-3 fused to C-terminal S and His tags (TIMP-3-S-His) or TIMP-1-S-His control to endothelial cells prior to extraction. Western blotting of final eluates revealed robust binding of A Disintegrin and Metalloproteinase (ADAM) 17 and a slight association of ADAM15 to TIMP-3, but not TIMP-1 control. To confirm a functional requirement for ADAM15 and 17 in mediating angiogenic events, a model of endothelial cell invasion was utilized. Silencing of ADAM17, but not ADAM15, expressio...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2691912</comments>
            <pubDate>Thu, 06 Aug 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2691912</guid>        </item>
        <item>
            <title>Mouse AMACO, a kidney and skin basement membrane associated molecule that mediates RGD-dependent cell attachment.</title>
            <link>http://www.medworm.com/index.php?rid=2675224&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19651211%26dopt%3DAbstract</link>
            <description>Authors: Gebauer JM, Keene DR, Olsen BR, Sorokin LM, Paulsson M, Wagener R
    The VWA domain-containing extracellular matrix protein AMACO has not been extensively characterized and its function remains unknown. It has been proposed as a potential cancer marker and carries a rare O-glucosylation and O-fucosylation on its first EGF-like domain. AMACO is a basement membrane associated protein, however its exact localization has not been determined. Here we show by immunogold electron microscopy of mouse kidney and skin that AMACO does not occur within the basement membrane but rather subjacent to the basement membrane at its stromal surface. In skin, AMACO often colocalizes with triple-helical domains of collagen-VII-containing anchoring fibrils as they emerge from the basal lamina. However...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2675224</comments>
            <pubDate>Thu, 30 Jul 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2675224</guid>        </item>
        <item>
            <title>The C-terminal domains of ADAMTS-4 and ADAMTS-5 promote association with N-TIMP-3.</title>
            <link>http://www.medworm.com/index.php?rid=2662998&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19643179%26dopt%3DAbstract</link>
            <description>Authors: Troeberg L, Fushimi K, Scilabra SD, Nakamura H, Dive V, Th&amp;#xF8;gersen IB, Enghild JJ, Nagase H
    We investigated whether the affinity of tissue inhibitor of metalloproteinases (TIMP)-3 for adamalysins with thrombospondin motifs (ADAMTS)-4 and ADAMTS-5 is affected by the non-catalytic ancillary domains of the enzymes. For this purpose, we first established a novel method of purifying recombinant FLAG-tagged TIMP-3 and its inhibitory N-terminal domain (N-TIMP-3) by treating transfected HEK293 cells with sodium chlorate to prevent heparan sulfate proteoglycan-mediated TIMP-3 internalization. TIMP-3 and N-TIMP-3 affinity for selected matrix metalloproteinases and forms of ADAMTS-4 and -5 lacking sequential C-terminal domains was determined. TIMP-3 and N-TIMP-3 displayed similar aff...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2662998</comments>
            <pubDate>Sun, 26 Jul 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2662998</guid>        </item>
        <item>
            <title>Characterization of an unusual tropoelastin with truncated C-Terminus in the frog.</title>
            <link>http://www.medworm.com/index.php?rid=2654220&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19638308%26dopt%3DAbstract</link>
            <description>Authors: Miao M, Stahl RJ, Petersen LF, Reintsch WE, Davis EC, Keeley FW
    Tropoelastin is the monomeric form of elastin, a major polymeric protein of the extracellular elastic matrix of vertebrate tissues with properties of extensibility and elastic recoil. Mammalian and avian species contain a single gene for tropoelastin. A tropoelastin gene has also previously been identified in amphibians. In contrast, two tropoelastin genes with different tissue expression patterns have been described in teleosts. While general characteristics of tropoelastins, such as alternating arrangements of hydrophobic and crosslinking domains, are conserved across a wide phylogenetic range, sequences of these domains are highly variable, particularly when amphibian and teleost tropoelastins are included. For...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2654220</comments>
            <pubDate>Fri, 24 Jul 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2654220</guid>        </item>
        <item>
            <title>Craniofacial cartilage morphogenesis requires zebrafish col11a1 activity.</title>
            <link>http://www.medworm.com/index.php?rid=2654219&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19638309%26dopt%3DAbstract</link>
            <description>Authors: Baas D, Malbouyres M, Haftek-Terreau Z, Le Guellec D, Ruggiero F
    The zebrafish ortholog of the human COL11A1 gene encoding the cartilage collagen XI proalpha1 chain was characterized to explore its function in developing zebrafish using the morpholino-based knockdown strategy. We showed that its expression in zebrafish is developmentally regulated. A low expression level was detected by real-time PCR during the early stages of development. At 24 hpf, a sharp peak of expression was observed. At that stage, in situ hybridization indicated that col11a1 transcripts are restricted to notochord. At 48 hpf, they were exclusively detected in the craniofacial skeleton, endoskeleton of pectoral fins and in otic vesicles. Collagen XI alpha1-deficient zebafish embryos developed defects in...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2654219</comments>
            <pubDate>Fri, 24 Jul 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2654219</guid>        </item>
        <item>
            <title>Characterization and regulation of ADAMTS-16.</title>
            <link>http://www.medworm.com/index.php?rid=2654222&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19635554%26dopt%3DAbstract</link>
            <description>In this study, we ascertained that the full length ADAMTS16 mRNA was expressed in chondrocytes and cloned the appropriate cDNA. Stable over-expression of ADAMTS16 in chondrosarcoma cells led to a decrease in cell proliferation and migration, though not adhesion, as well as a decrease in the expression of matrix metalloproteinase-13 (MMP13). The transcription start point of the human ADAMTS16 gene was experimentally identified as 138bp upstream of the translation start ATG and the basal promoter was mapped out to -1802bp. Overexpression of Egr1 induced ADAMTS16 promoter constructs of -157/+138 or longer whilst Sp1 induced all ADAMTS16 promoter constructs. Transforming growth factor beta (TGFbeta) stimulated expression of endogenous ADAMTS16 gene expression in chondrocyte cell lines.
    PMI...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2654222</comments>
            <pubDate>Thu, 23 Jul 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2654222</guid>        </item>
        <item>
            <title>Hyaluronan synthases and hyaluronidases in the kidney during changes in hydration status.</title>
            <link>http://www.medworm.com/index.php?rid=2654221&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19635555%26dopt%3DAbstract</link>
            <description>In conclusion, HAS 2 appears a major contributor to the baseline levels of hyaluronan. Reduced HAS 2 gene expression and increased excreted urinary hyaluronidase activity during dehydration contribute to the reduced amount of hyaluronan and to antidiuretic response.
    PMID: 19635555 [PubMed - as supplied by publisher] (Source: Matrix Biology)</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2654221</comments>
            <pubDate>Thu, 23 Jul 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2654221</guid>        </item>
        <item>
            <title>The internal mechanical functioning of intervertebral discs and articular cartilage, and its relevance to matrix biology.</title>
            <link>http://www.medworm.com/index.php?rid=2592215&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19586615%26dopt%3DAbstract</link>
            <description>Authors: Adams MA, Dolan P, McNally DS
    Degeneration of intervertebral discs and articular cartilage can cause pain and disability. Risk factors include genetic inheritance and age, but mechanical loading also is important. Its influence has been investigated using miniature pressure transducers to measure the distribution of compressive stress (force per unit area) within loaded tissue. The technique quantifies stress concentrations, and detects regions that behave in a fluid-like manner. Intervertebral discs demonstrate a central fluid-like region which normally extends beyond the anatomical nucleus pulposus so that the whole disc functions like a &quot;water bed&quot;. With increasing age, the fluid region shrinks and pressure within it falls. Stress concentrations appear in the surrounding an...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2592215</comments>
            <pubDate>Sat, 04 Jul 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2592215</guid>        </item>
        <item>
            <title>Site controlled transgenic mice validating increased expression from human matrix metalloproteinase (MMP-1) promoter due to a naturally occurring SNP.</title>
            <link>http://www.medworm.com/index.php?rid=2580416&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19577645%26dopt%3DAbstract</link>
            <description>Authors: Coon CI, Fiering S, Gaudet J, Wyatt CA, Brinckerhoff CE
    Matrix Metalloproteinases (MMPs) comprise a family of more than 20 members, each with the ability to degrade components of the extracellular matrix. The interstitial collagenases have the unique capacity to degrade the stromal collagens, types I, II and III, the body's most abundant proteins. These collagenases include MMP-1, MMP-8, MMP-13 and MMP-14. MMP-1, with a very broad expression pattern, has major roles in mediating matrix destruction in many diseases. We have described a single nucleotide polymorphism (SNP) in the MMP-1 promoter that augments transcription. This SNP is the presence or absence of an extra guanine (G) at -1607 bp, which creates the sequence 5'-GGAA-3'(2G allele), which is a ETS binding site. Compar...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2580416</comments>
            <pubDate>Wed, 01 Jul 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2580416</guid>        </item>
        <item>
            <title>Transport of a hyaluronan-binding protein in brain tissue.</title>
            <link>http://www.medworm.com/index.php?rid=2580417&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19576282%26dopt%3DAbstract</link>
            <description>Authors: Kappler J, Hegener O, Baader SL, Franken S, Gieselmann V, H&amp;#xE4;berlein H, Rauch U
    Hyaluronan is an unsulfated linear glycosaminoglycan with the ability to nucleate extracellular matrices by the formation of aggregates with lecticans. These matrices are essential during development of the central nervous system. In the prospective white matter of the developing brain hyaluronan is organized into fiber-like structures according to confocal microscopy of fixed slices which may guide the migration of neural precursor cells (Baier et al. 2007). By using plasmon surface resonance, microinjection into brain slices and fluorescence correlation spectroscopy, we show that the brain-specific lecticans bind to, but also dissociate rather rapidly from hyaluronan. After microinjection int...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2580417</comments>
            <pubDate>Mon, 29 Jun 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2580417</guid>        </item>
        <item>
            <title>Lack of fibulin-3 alters regenerative tissue responses in the primary olfactory pathway.</title>
            <link>http://www.medworm.com/index.php?rid=2549036&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19520159%26dopt%3DAbstract</link>
            <description>Authors: Vukovic J, Marmorstein LY, McLaughlin PJ, Sasaki T, Plant GW, Harvey AR, Ruitenberg MJ
    The adult olfactory epithelium has maintained the ability to reconstitute its olfactory sensory neurons (OSNs) from a basal progenitor cell compartment. This allows for life-long turnover and replacement of receptor components as well as repair of the primary olfactory pathway in response to injury and environmental insults. The present study investigated whether fibulin-3, a glycoprotein in the extracellular matrix and binding partner of tissue inhibitor of metalloproteinases-3 (TIMP-3), plays a role in ongoing plasticity and regenerative events in the primary adult olfactory pathway. In wild-type control mice, fibulin-3 protein was detected on IB4(+)CD31(+) blood vessels, nerve fascicles a...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2549036</comments>
            <pubDate>Mon, 08 Jun 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2549036</guid>        </item>
        <item>
            <title>Cyclic AMP regulates extracellular matrix gene expression and metabolism in cultured primary rat chondrocytes.</title>
            <link>http://www.medworm.com/index.php?rid=2472062&amp;cid=s_36817_67_f&amp;fid=36817&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19505573%26dopt%3DAbstract</link>
            <description>In this report, we assess the effect of the cell-permeable cAMP analog adenosine 8-(4-chloro-phenylthio)-3',5'-cyclic monophosphate (CPT-cAMP) and PGE(2) on mRNA expression in primary neonatal rat chondrocytes. CPT-cAMP decreased type II collagen, link protein, parathyroid hormone/parathyroid hormone-related peptide receptor and alkaline phosphatase, increased glyceraldehyde-3-phosphate dehydrogenase mRNA and lactate efflux, but did not alter type X collagen or aggrecan mRNA. The effect of CPT-cAMP on type II collagen and link protein mRNAs and chondrocyte metabolism were attenuated by the transcriptional inhibitor actinomycin D, indicating that the ability of CPT-cAMP to suppress mRNA expression was not due to alterations in mRNA stability, but were instead likely due to transcriptional m...</description>
            <author>Matrix Biology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2472062</comments>
            <pubDate>Fri, 05 Jun 2009 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">2472062</guid>        </item>
    </channel>
</rss>

