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        <title>Journal of Cell Communication and Signaling 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 'Journal of Cell Communication and Signaling' source.</description>
        <link><![CDATA[http://www.medworm.com/rss/search.php?qu=Journal+of+Cell+Communication+and+Signaling&t=Journal+of+Cell+Communication+and+Signaling&s=Search&f=source]]></link>
        <lastBuildDate>Thu, 09 Feb 2012 16:56:44 +0100</lastBuildDate>
        <item>
            <title>Analysis of the MMP-dependent and independent functions of tissue inhibitor of metalloproteinase-2 on the invasiveness of breast cancer cells.</title>
            <link>http://www.medworm.com/index.php?rid=5596612&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22227894%26dopt%3DAbstract</link>
            <description>Authors: Walsh LA, Cepeda MA, Damjanovski S
    Abstract
    Matrix metalloproteinases (MMPs) are secreted endopeptidases that play an essential role in remodeling the extracellular matrix (ECM). MMPs are primarily active during development, when the majority of ECM remodeling events occurs. In adults, elevated MMP activity has been observed in many pathological conditions such as cancer and osteoarthritis. The proteolytic activity of MMPs is controlled by their natural inhibitors - the tissue inhibitor of metalloproteinases (TIMPs). In addition to blocking MMP-mediated proteolysis, TIMPs have a number of MMP-independent functions including binding to cell surface proteins thereby stimulating signaling cascades. TIMP-2, the most studied member of the family, can both inhibit and activate M...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5596612</comments>
            <pubDate>Sun, 08 Jan 2012 05:00:00 +0100</pubDate>
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        <item>
            <title>Endoglin in liver fibrosis.</title>
            <link>http://www.medworm.com/index.php?rid=5473509&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22131199%26dopt%3DAbstract</link>
            <description>Authors: Finnson KW, Philip A
    Abstract
    Liver fibrosis occurs in most types of chronic liver diseases and is characterized by excessive accumulation of extracellular matrix proteins, leading to disruption of tissue function and eventually organ failure. Transforming growth factor (TGF)-Î² represents an important pro-fibrogenic factor and aberrant TGF-Î² action has been implicated in many disease processes of the liver. Endoglin is a TGF-Î² co-receptor expressed mainly in endothelial cells that has been shown to differentially regulates TGF-Î² signal transduction by inhibiting ALK5-Smad2/3 signalling and augmenting ALK1-Smad1/5 signalling. Recent reports demonstrating upregulation of endoglin expression in pro-fibrogenic cell types such as scleroderma fibroblasts and hepatic stellate...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5473509</comments>
            <pubDate>Thu, 01 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5473509</guid>        </item>
        <item>
            <title>MEK/ERK inhibitors: proof-of-concept studies in lung fibrosis.</title>
            <link>http://www.medworm.com/index.php?rid=5473508&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22131200%26dopt%3DAbstract</link>
            <description>Authors: Leask A
    Abstract
    There is no therapy for chronic fibroproliferative diseases, in spite of the fact that current health statistics suggest that these (which include cardiovascular disease, pulmonary fibrosis, diabetic nephropathy, liver cirrhosis and systemic sclerosis) have been estimated to cause approximately 45% of the deaths in the developed world. Recently, many studies have shown that mitogen activated protein kinases (MAPKs) are activated in response to fibrogenic agents and contribute to the formation and function of the myofibroblast, the critical cell type responsible for excessive scarring. A recent report by Madala and colleagues (Am J Respir Cell Mol Biol, 2011) has provided a proof-of-concept study showing that the specific MEK inhibitor ARRY-142886 (ARRY) ca...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5473508</comments>
            <pubDate>Thu, 01 Dec 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5473508</guid>        </item>
        <item>
            <title>ICCNS-sponsored meetings.</title>
            <link>http://www.medworm.com/index.php?rid=5473510&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22127505%26dopt%3DAbstract</link>
            <description>Authors: Perbal B
    PMID: 22127505 [PubMed - as supplied by publisher] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5473510</comments>
            <pubDate>Wed, 30 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5473510</guid>        </item>
        <item>
            <title>Meeting report: novel targets for cancer and connective tissues diseases.</title>
            <link>http://www.medworm.com/index.php?rid=5416053&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D22083621%26dopt%3DAbstract</link>
            <description>Authors: Leask A
    PMID: 22083621 [PubMed - as supplied by publisher] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5416053</comments>
            <pubDate>Tue, 15 Nov 2011 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">5416053</guid>        </item>
        <item>
            <title>Salivary proteins as predictors and controls for oral health.</title>
            <link>http://www.medworm.com/index.php?rid=5243942&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21927991%26dopt%3DAbstract</link>
            <description>Authors: Vukosavljevic D, Custodio W, Siqueira WL
    Abstract
    We will provide a translational view of using the recent technological advances in dental research for predicting, monitoring, and preventing the development of oral diseases by investigating the diagnostic and therapeutic role of salivary proteins. New analytical state-of-the-art technologies such as mass spectrometry and atomic force microscopy have revolutionized the field of oral biology. These novel technologies open avenues for a comprehensive characterization of the salivary proteins followed by the evaluation of the physiological functions which could make possible in a near future the development of a new series of synthetic protein for therapeutic propose able to prevent global oral diseases such as periodontal di...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5243942</comments>
            <pubDate>Sun, 18 Sep 2011 04:00:00 +0100</pubDate>
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        <item>
            <title>Task of the introns, cell communication explained by field physics.</title>
            <link>http://www.medworm.com/index.php?rid=5243934&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21928077%26dopt%3DAbstract</link>
            <description>Authors: Meyl K
    Abstract
    The evolution of genes is achieved via cellular communication based on the principles of resonance. Resonance between the DNA of cells requires not only the appropriate frequency and phase but also mirrored modulation of the transmitter and receiver using identical information. If the receiver is missing information that still needs to be transported, no interference or suppression of the resonance is allowed. In nature creating a predominance of non-coded DNA regions, which maintains and completes the resonance required in reading and writing of genetic information, solves this problem.
    PMID: 21928077 [PubMed - as supplied by publisher] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5243934</comments>
            <pubDate>Sun, 18 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5243934</guid>        </item>
        <item>
            <title>Novel targets for cancer and connective tissues diseases: A meeting sponsored by the International CCN Society : Coast Coal Harbour Hotel, Vancouver, BC, Canada (September 24-27, 2011).</title>
            <link>http://www.medworm.com/index.php?rid=5216272&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21904831%26dopt%3DAbstract</link>
            <description>Authors: 
    PMID: 21904831 [PubMed - as supplied by publisher] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5216272</comments>
            <pubDate>Fri, 09 Sep 2011 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">5216272</guid>        </item>
        <item>
            <title>On how CCN6 suppresses breast cancer growth and invasion.</title>
            <link>http://www.medworm.com/index.php?rid=5140458&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21842227%26dopt%3DAbstract</link>
            <description>Authors: Huang W, Pal A, Kleer CG
    Abstract
    Living cells communicate with their microenvironment and exchange information through signaling pathways in order to carry out most biological processes. The CCN family of proteins has the ability to coordinate the extracellular and intracellular signaling pathways and epithelial-stromal cross-talks. CCN proteins have been shown to play roles in multiple processes including cancer, either as tumor suppressors or oncogenes. Particularly, loss of CCN6 expression has been reported in highly aggressive breast cancer types, especially in inflammatory breast cancer and breast cancer with axillary lymph node metastasis. Recent findings can better explain the biological relevance of CCN6 as a tumor suppressor protein in breast tumorigenesis. CCN6 ...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5140458</comments>
            <pubDate>Fri, 12 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5140458</guid>        </item>
        <item>
            <title>Sp1king out cancer (....and fibrosis?).</title>
            <link>http://www.medworm.com/index.php?rid=5140459&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21822787%26dopt%3DAbstract</link>
            <description>Authors: Leask A
    Abstract
    It is becoming increasingly apparent that many of the basic mechanisms underlying cancers also underlie fibrotic diseases. For example, the Sp1 family of transcription factors plays an essential role in controlling the gene expression of proteins that promote both oncogenesis and fibrogenesis. The drug mithramycin, which prevents Sp1 binding to DNA, has been in use clinically for some cancers, but has side-effects. However, other drugs exist that affect Sp1 activity through promoting Sp1 protein degradation. Evidence has emerged that low levels of mithramycin can be combined with these drugs to result in potent antitumorigenic effects without resulting in obvious toxicity (Gao et al. Cancer Res 2011 Jun 20; Jia et al. Cancer Res 70:1111-1119, 2010). Given ...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5140459</comments>
            <pubDate>Fri, 05 Aug 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5140459</guid>        </item>
        <item>
            <title>Tryptase activates isolated adult cardiac fibroblasts via protease activated receptor-2 (PAR-2).</title>
            <link>http://www.medworm.com/index.php?rid=5094894&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21786087%26dopt%3DAbstract</link>
            <description>Authors: Murray DB, McLarty-Williams J, Nagalla KT, Janicki JS
    Protease activated receptor-2 (PAR-2) derived cycloxygenase-2 (COX-2) was recently implicated in a cardiac mast cell and fibroblast cross-talk signaling cascade mediating myocardial remodeling secondary to mechanical stress. We designed this study to investigate in vitro assays of isolated adult cardiac fibroblasts to determine whether binding of tryptase to the PAR-2 receptor on cardiac fibroblasts will lead to increased expression of COX-2 and subsequent formation of the arachodonic acid metabolite 15-d-Prostaglandin J(2) (15-d-PGJ(2)). The effects of tryptase (100Â mU) and co-incubation with PAR-2 inhibitor peptide sequence FSLLRY-NH(2) (10(-6)M) on proliferation, hydroxyproline concentration, 15-d-PGJ(2) formation and P...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5094894</comments>
            <pubDate>Fri, 22 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5094894</guid>        </item>
        <item>
            <title>CCN3 suppresses mitogenic signalling and reinstates growth control mechanisms in Chronic Myeloid Leukaemia.</title>
            <link>http://www.medworm.com/index.php?rid=5042521&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21773872%26dopt%3DAbstract</link>
            <description>Authors: McCallum L, Lu W, Price S, Lazar N, Perbal B, Irvine AE
    CCN3, a tumour suppressor gene, is down-regulated as a result of BCR-ABL tyrosine kinase activity in Chronic Myeloid Leukaemia (CML). We have established a stable CCN3 expression model in the human K562 CML cell line and have further validated the role for CCN3 in the leukaemogenic process. K562 cells stably transfected with CCN3 (K562/CCN3; 2.25â€‰Ã—â€‰10(6) copies per 50Â ng cDNA) demonstrated over 50% reduction in cell growth in comparison to cells stably transfected with empty vector (K562/control; pâ€‰=â€‰0.005). K562/CCN3 cells had reduced colony formation capacity (reduced by 29.7%, pâ€‰=â€‰0.03) and reduced mitogenic signalling in comparison to K562/control cells (reduced by 29.5% (pâ€‰=â€‰0.002) and 37.4% (pâ€‰=â...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5042521</comments>
            <pubDate>Tue, 19 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5042521</guid>        </item>
        <item>
            <title>Elevated CCN2 expression in scleroderma: a putative role for the TGFÎ² accessory receptors TGFÎ²RIII and endoglin.</title>
            <link>http://www.medworm.com/index.php?rid=5042522&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21769684%26dopt%3DAbstract</link>
            <description>Authors: Holmes AM, Ponticos M, Shi-Wen X, Denton CP, Abraham DJ
    The ability of TGFÎ²1 to act as a potent pro-fibrotic mediator is well established, potently inducing the expression of fibrogenic genes including type I collagen (COL1A2) and CCN2. Previously we have shown elevated expression of the TGFÎ² accessory receptor, endoglin on Systemic Sclerosis (SSc) dermal fibroblasts. Here we sought to assess the cell surface expression of the TGFÎ² receptor complex on SSc dermal fibroblasts (SDF), and investigate their role in maintaining the elevated expression of CCN2. SDF exhibited elevated expression of the TGFÎ² accessory receptors betaglycan/TGFÎ²RIII and endoglin, but not type I or type II receptors. To determine the effect of altered receptor repertoire on TGFÎ² responses, we invest...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5042522</comments>
            <pubDate>Mon, 18 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5042522</guid>        </item>
        <item>
            <title>Eureka! Ets a target for fibrosis!</title>
            <link>http://www.medworm.com/index.php?rid=5042524&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21748431%26dopt%3DAbstract</link>
            <description>Authors: Leask A
    The oncogenic Ets family of transcription factors is now recognized to play a key role in fibroblasts as it controls the expression of a variety of pro-fibrotic genes, including the induction of CCN2 by transforming growth factor Î². A recent report (Baran et al., Am J Respir Cell Mol Biol. 2011 May 11) shows that mice containing a version of ets2 that is incapable of being phosphorylated are resistant to bleomycin-induced lung fibrosis. This latter paper is the subject of this commentary.
    PMID: 21748431 [PubMed - as supplied by publisher] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5042524</comments>
            <pubDate>Mon, 11 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5042524</guid>        </item>
        <item>
            <title>CCN3/NOV small interfering RNA enhances fibrogenic gene expression in primary hepatic stellate cells and cirrhotic fat storing cell line CFSC.</title>
            <link>http://www.medworm.com/index.php?rid=5042523&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21748432%26dopt%3DAbstract</link>
            <description>In this study we showed ccn3/nov mRNA to increase dramatically following hepatic stellate cell activation, reaching peak levels in fully transdifferentiated myofibroblasts. In models of experimental hepatic fibrosis, CCN3/NOV increased significantly at the mRNA and protein levels. CCN3/NOV was found mainly in non-parenchymal cells along the areas of tissue damage and repair. In the bile-duct ligation model, CCN3/NOV was localized mainly along portal tracts, while the repeated application of carbon tetrachloride resulted in CCN3/NOV expression mainly in the centrilobular areas. In contrast to CCN2/CTGF, the profibrotic cytokines platelet-derived growth factor-B and -D as well as transforming growth factor-Î² suppressed CCN3/NOV expression. In vitro, CCN3/NOV siRNA attenuated migration in th...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=5042523</comments>
            <pubDate>Mon, 04 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">5042523</guid>        </item>
        <item>
            <title>Regulation of cytochrome P4501A by protein kinase C: the role of heat shock protein70.</title>
            <link>http://www.medworm.com/index.php?rid=4998718&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21725659%26dopt%3DAbstract</link>
            <description>Authors: Ghosh MC, Ray AK
    Carbofuran is a pesticide, which is used throughout the world as a nematicide and an acaricide. This pesticide integrates into living organisms through aquatic ecosystem. In earlier report, we had demonstrated that cytochrome P4501A was induced in cultured catfish hepatocytes in response to carbofuran, which might be responsible for the detoxification of this pesticide. As the underlying signaling mechanism associated with induction and regulation of cytochrome P4501A has not yet been well defined, we therefore in the present study have investigated to identify the regulatory network of cytochrome P4501A in catfish liver or cultured hepatocytes by targeting several key signaling molecules such as phosphatidyl inositol (PI) or protein kinase C (PKC), which are ...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4998718</comments>
            <pubDate>Fri, 01 Jul 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4998718</guid>        </item>
        <item>
            <title>CCN1 contributes to skin connective tissue aging by inducing age-associated secretory phenotype in human skin dermal fibroblasts.</title>
            <link>http://www.medworm.com/index.php?rid=4998726&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21720918%26dopt%3DAbstract</link>
            <description>Authors: Quan T, Qin Z, Robichaud P, Voorhees JJ, Fisher GJ
    Dermal connective tissue collagen is the major structural protein in skin. Fibroblasts within the dermis are largely responsible for collagen production and turnover. We have previously reported that dermal fibroblasts, in aged human skin in vivo, express elevated levels of CCN1, and that CCN1 negatively regulates collagen homeostasis by suppressing collagen synthesis and increasing collagen degradation (Quan et al. Am J Pathol 169:482-90, 2006, J Invest Dermatol 130:1697-706, 2010). In further investigations of CCN1 actions, we find that CCN1 alters collagen homeostasis by promoting expression of specific secreted proteins, which include matrix metalloproteinases and proinflammatory cytokines. We also find that CCN1-induced s...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4998726</comments>
            <pubDate>Thu, 30 Jun 2011 23:00:00 +0100</pubDate>
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        <item>
            <title>Pomegranate sensitizes Tamoxifen action in ER-Î± positive breast cancer cells.</title>
            <link>http://www.medworm.com/index.php?rid=4998735&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21706446%26dopt%3DAbstract</link>
            <description>The objective of the study was to determine whether PFEs may able to enhance/sensitize the TAM's effect in ER-positive MCF-7 breast cancer cells. To test the hypothesis, we determined the effect of PFEs on sensitive and TAM-resistant-MCF-7 cell viability and cell death in the presence or absence of TAM under estrogenic or non-estrogenic culture environment. The present studies demonstrated that PFEs enhance the TAM action in both sensitive and TAM-resistant MCF-7 cells through the inhibition of cell viability (regular or estrogen-induced) by inducing cell-death machinery. Collectively, the results showed for the first time that pomegranate combined with TAM may represent a novel and a powerful approach to enhance and sensitize TAM action.
    PMID: 21706446 [PubMed - as supplied by publish...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4998735</comments>
            <pubDate>Sun, 26 Jun 2011 23:00:00 +0100</pubDate>
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        <item>
            <title>CCN2 expression and localization in melanoma cells.</title>
            <link>http://www.medworm.com/index.php?rid=4951213&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21667293%26dopt%3DAbstract</link>
            <description>Authors: Sha W, Leask A
    The matricellular protein connective tissue growth factor (CTGF, CCN2) is overexpressed in several forms of cancer and may represent a novel target in anti-cancer therapy. However, whether CCN2 is expressed in melanoma cells is unknown. The highly metastatic murine melanoma cell line B16(F10) was used for our studies. Real time polymerase chain reaction analysis was used to detect mRNA expression of CCN1, CCN2, CCN3 and CCN4 in Western blot and immunofluorescence analyses were used to detect CCN2 protein. Inhibitors of signal transduction cascades were used to probe the mechanism underlying CCN2 expression in B16(F10) cells. CCN2 was expressed in B16(F10) cells, and was reduced by the FAK/src inhibitor PP2 and the MEK/ERK inhibitor U0126 indicating that CCN2 act...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4951213</comments>
            <pubDate>Sat, 11 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4951213</guid>        </item>
        <item>
            <title>Calcium and copper transport ATPases: analogies and diversities in transduction and signaling mechanisms.</title>
            <link>http://www.medworm.com/index.php?rid=4951214&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21656155%26dopt%3DAbstract</link>
            <description>Authors: Inesi G
    The calcium transport ATPase and the copper transport ATPase are members of the P-ATPase family and retain an analogous catalytic mechanism for ATP utilization, including intermediate phosphoryl transfer to a conserved aspartyl residue, vectorial displacement of bound cation, and final hydrolytic cleavage of Pi. Both ATPases undergo protein conformational changes concomitant with catalytic events. Yet, the two ATPases are prototypes of different features with regard to transduction and signaling mechanisms. The calcium ATPase resides stably on membranes delimiting cellular compartments, acquires free Ca(2+) with high affinity on one side of the membrane, and releases the bound Ca(2+) on the other side of the membrane to yield a high free Ca(2+) gradient. These features...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4951214</comments>
            <pubDate>Wed, 08 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4951214</guid>        </item>
        <item>
            <title>MicroRNAs 130a/b are regulated by BCR-ABL and downregulate expression of CCN3 in CML.</title>
            <link>http://www.medworm.com/index.php?rid=4903068&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21638198%26dopt%3DAbstract</link>
            <description>This study shows that miRNAs modulate CCN3 expression. Deregulated miRNA expression initiated by BCR-ABL may be one mechanism of downregulating CCN3 whereby leukaemic cells evade negative growth regulation.
    PMID: 21638198 [PubMed - as supplied by publisher] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4903068</comments>
            <pubDate>Thu, 02 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4903068</guid>        </item>
        <item>
            <title>CCN-2 is up-regulated by and mediates effects of matrix bound advanced glycated end-products in human renal mesangial cells.</title>
            <link>http://www.medworm.com/index.php?rid=4903069&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21630131%26dopt%3DAbstract</link>
            <description>In conclusion, CCN-2 is induced by non-enzymatically glycated matrix and it mediates downstream fibronectin and TIMP-1 increases, thus through this mechanism potentially contributing to ECM accumulation in the renal glomerulus in diabetes.
    PMID: 21630131 [PubMed - as supplied by publisher] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4903069</comments>
            <pubDate>Wed, 01 Jun 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4903069</guid>        </item>
        <item>
            <title>Pre- and post-translational regulation of osteopontin in cancer.</title>
            <link>http://www.medworm.com/index.php?rid=4800672&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21516514%26dopt%3DAbstract</link>
            <description>Authors: Anborgh PH, Mutrie JC, Tuck AB, Chambers AF
    Osteopontin (OPN) is a matricellular protein that binds to a number of cell surface receptors including integrins and CD44. It is expressed in many tissues and secreted into body fluids including blood, milk and urine. OPN plays important physiological roles in bone remodeling, immune response and inflammation. It is also a tumour-associated protein, and elevated OPN levels are associated with tumour formation, progression and metastasis. Research has revealed a promising role for OPN as a cancer biomarker. OPN is subject to alternative splicing, as well as post-translational modifications such as phosphorylation, glycosylation and proteolytic cleavage. Functional differences have been revealed for different isoforms and post-transla...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4800672</comments>
            <pubDate>Mon, 09 May 2011 18:45:49 +0100</pubDate>
            <guid isPermaLink="false">4800672</guid>        </item>
        <item>
            <title>CCN2/decorin interactions: a novel approach to combating fibrosis?</title>
            <link>http://www.medworm.com/index.php?rid=4800671&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21533889%26dopt%3DAbstract</link>
            <description>Authors: Leask A
    CCN2 (connective tissue growth factor, CTGF), a member of the CCN family is overexpressed in fibrotic disease and is essential for the development of experimental fibrosis. Drugs targeting CCN2 action may therefore prove to be useful anti-fibrotic approaches. CCN2 acts via integrins and heparan sulfate-containing proteoglycans (HSPGs). In a recent study, Vial and colleagues (2011) show that decorin can bind CCN2. A peptide corresponding to the leucine rich repeats peptide 12 region of decorin can neutralize CCN2-mediated activity on C2C12 cells in vitro. Thus it is conceivable that this peptide could be used in the future as a novel antifibrotic approach.
    PMID: 21533889 [PubMed - as supplied by publisher] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4800671</comments>
            <pubDate>Sat, 30 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4800671</guid>        </item>
        <item>
            <title>CCN2 is not required for skin development.</title>
            <link>http://www.medworm.com/index.php?rid=4800670&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21533890%26dopt%3DAbstract</link>
            <description>Authors: Liu S, Leask A
    Mice lacking the pro-adhesive matricellular protein connective tissue growth factor (CTGF/CCN2) display an embryonic lethal phenotype due to defects in bone and cartilage. However, the specific role of CCN2 in skin development is unknown. Here, we generated mice deleted for CCN2 in the entire body (using a cre/lox system in which CCN2 is deleted in the entire body due to the presence of a constitutively expressed cre recombinase). We found that CCN2 was not required for the development of skin as defined by skin thickness measurements, trichrome staining and immunostaining with anti-CD31 (to detect endothelial cells) and anti-Î±-SMA (to detect smooth muscle cells and pericytes) antibodies. Thus, although recently we have shown that CCN2 is required for fibrogene...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4800670</comments>
            <pubDate>Sat, 30 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4800670</guid>        </item>
        <item>
            <title>Deconstructing fibrosis research: do pro-fibrotic signals point the way for chronic dermal wound regeneration?</title>
            <link>http://www.medworm.com/index.php?rid=4747819&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21503732%26dopt%3DAbstract</link>
            <description>Authors: Elliott CG, Hamilton DW
    Chronic wounds are characterized by inadequate matrix synthesis, no re-epithelialization, infection and ultimately no wound resolution. In contrast, fibrosis is characterized by overproduction of matrix and excess matrix contraction. As research in the fields of chronic wounds and fibrosis surges forward, important parallels can now be drawn between the dysfunctions in fibrotic diseases and the needs of chronic wounds. These parallels exist at both the macroscopic level and at the molecular level. Thus in finding the individual factors responsible for the progression of fibrotic diseases, we may identify new therapeutic targets for the resolution of chronic wounds. The aim of this review is to discuss how recent advances in fibrosis research have found ...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4747819</comments>
            <pubDate>Mon, 18 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4747819</guid>        </item>
        <item>
            <title>Association of the metastatic phenotype with CCN family members among breast and oral cancer cells.</title>
            <link>http://www.medworm.com/index.php?rid=4747820&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21499980%26dopt%3DAbstract</link>
            <description>In this study, we comprehensively analyzed the roles of all six CCN family members in cell growth, migration and invasion of breast cancer cells in vitro and in vivo. As a result, we found the CCN2/CCN3 ratio to be a parameter that is associated with the metastatic phenotype of breast cancer cells that are highly metastatic to the bone. The same analysis with cell lines from oral squamous carcinomas that are not metastatic to the bone further supported our notion. These results suggest the functional significance of the interplay between CCN family members in regulating the phenotype of cancer cells.
    PMID: 21499980 [PubMed - as supplied by publisher] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4747820</comments>
            <pubDate>Sun, 17 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4747820</guid>        </item>
        <item>
            <title>3D tumour models: novel in vitro approaches to cancer studies.</title>
            <link>http://www.medworm.com/index.php?rid=4747821&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21499821%26dopt%3DAbstract</link>
            <description>This article aims to overview current 3D in vitro models of cancer and review strategies employed by researchers to tackle these aspects with special reference to recent promising developments, as well as the current limitations of 2D cultures and in vivo models. 3D in vitro models provide an important alternative to both complex in vivo whole organism approaches, and 2D culture with its spatial limitations. Here we review current strategies in the field of modelling cancer, with special reference to advances in complex 3D in vitro models.
    PMID: 21499821 [PubMed - as supplied by publisher] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4747821</comments>
            <pubDate>Fri, 15 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4747821</guid>        </item>
        <item>
            <title>CCN1: a novel target for pancreatic cancer.</title>
            <link>http://www.medworm.com/index.php?rid=4747854&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21484184%26dopt%3DAbstract</link>
            <description>Authors: Leask A
    Members of CCN family of matricellular proteins are being increasingly recognized by the translational research community as representing excellent targets for drug intervention. Although much effort has been expended in outlining the mechanisms involved in pancreatic carcinogenesis, the precise molecular pathways involved remain incompletely understood, and appropriate targets for drug intervention remain elusive. A recent exciting report by Haque and colleagues (Mol Cancer. 2011 Jan 13;10:8) provides strong evidence that CCN1 (cyr61) is a potential therapeutic target in pancreatic cancer.
    PMID: 21484184 [PubMed - as supplied by publisher] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4747854</comments>
            <pubDate>Mon, 04 Apr 2011 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">4747854</guid>        </item>
        <item>
            <title>Purification and characterization of native human insulin-like growth factor binding protein-6.</title>
            <link>http://www.medworm.com/index.php?rid=4747853&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21484185%26dopt%3DAbstract</link>
            <description>Authors: Taferner A, Micutkova L, Hermann M, Jansen-DÃ¼rr P, Pircher H
    Insulin-like growth factor binding proteins (IGFBPs) are key regulators of insulin-like growth factor (IGF) mediated signal transduction and thereby can profoundly influence cellular phenotypes and cell fate. Whereas IGFBPs are extracellular proteins, intracellular activities were described for several IGFBP family members, such as IGFBP-3, which can be reinternalized by endocytosis and reaches the nucleus through routes that remain to be fully established. Within the family of IGFBPs, IGFBP-6 is unique for its specific binding to IGF-II. IGFBP-6 was described to possess additional IGF-independent activities, which have in part been attributed to its translocation to the nucleus; however, cellular uptake of IGFBP-6 ...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4747853</comments>
            <pubDate>Wed, 23 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4747853</guid>        </item>
        <item>
            <title>CCN2: a bona fide target for anti-fibrotic drug intervention.</title>
            <link>http://www.medworm.com/index.php?rid=4747852&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21484186%26dopt%3DAbstract</link>
            <description>Authors: Leask A
    CCN2 (formerly known as connective tissue growth factor) was identified by several different laboratories approximately 20Â years ago. Almost since its identification as a factor induced in normal fibroblasts by transforming growth factor Î² and overexpressed in fibrotic disease, CCN2 has been hypothesized to be not only a marker but also a central mediator of fibrosis in vivo. Finally, in vivo data are emerging to validate this key hypothesis. For example, a neutralizing anti-CCN2 antibody was found to attenuate fibrogenesis in three separate animal models (Wang et al. in Fibrogenesis Tissue Repair 4:1-4, 2011). This commentary addresses recent data indicating that CCN2 appears to represent a key central mediator of fibrosis and a good target for anti-fibrotic drug in...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4747852</comments>
            <pubDate>Sun, 06 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4747852</guid>        </item>
        <item>
            <title>Integrin-linked kinase: a Scaffold protein unique among its ilk.</title>
            <link>http://www.medworm.com/index.php?rid=4747851&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21484187%26dopt%3DAbstract</link>
            <description>Authors: Dagnino L
    Integrin-linked kinase (ILK) is a scaffolding protein with central roles in tissue development and homeostasis. Much debate has focused on whether ILK is a bona fide or a pseudo- kinase. This aspect of ILK function has been complicated by the large volumes of conflicting observations obtained from a wide variety of experimental approaches, from in vitro models, to analyses in invertebrates and in mammals. Key findings in support or against the notion that ILK is catalytically active are summarized. The importance of ILK as an adaptor protein is well established, and defining its role as a signaling hub will be the next key step to understand its distinct biological roles across tissues and species.
    PMID: 21484187 [PubMed - as supplied by publisher] (Source: Journ...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4747851</comments>
            <pubDate>Thu, 03 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4747851</guid>        </item>
        <item>
            <title>Report on the 6th international workshop of the CCN family of genes.</title>
            <link>http://www.medworm.com/index.php?rid=4747842&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21484584%26dopt%3DAbstract</link>
            <description>Authors: Twigg SM, Irvine S, Leask A, Perbal B
    
    PMID: 21484584 [PubMed - in process] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4747842</comments>
            <pubDate>Tue, 01 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4747842</guid>        </item>
        <item>
            <title>Abstracts of the 6th International Workshop on the CCN Family of Genes : Held at the Slieve Donnard Hotel, Newcastle, Northern Ireland 20-24 October 2010.</title>
            <link>http://www.medworm.com/index.php?rid=4747837&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21484585%26dopt%3DAbstract</link>
            <description>Authors: 
    
    PMID: 21484585 [PubMed - in process] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4747837</comments>
            <pubDate>Tue, 01 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4747837</guid>        </item>
        <item>
            <title>Hormesis provides a generalized quantitative estimate of biological plasticity.</title>
            <link>http://www.medworm.com/index.php?rid=4747836&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21484586%26dopt%3DAbstract</link>
            <description>This article provides the first quantitative estimate of biological plasticity that may be generalized across plant, microbial, animal systems, and across all levels of biological organization. The quantitative features of plasticity are described by the hormesis dose response model. These findings have important biological, biomedical and evolutionary implications.
    PMID: 21484586 [PubMed - in process] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4747836</comments>
            <pubDate>Tue, 01 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4747836</guid>        </item>
        <item>
            <title>Exploiting notochord cells for stem cell-based regeneration of the intervertebral disc.</title>
            <link>http://www.medworm.com/index.php?rid=4747834&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21484587%26dopt%3DAbstract</link>
            <description>Authors: McCann MR, Bacher CA, SÃ©guin CA
    The nucleus pulposus is an avascular and aneural tissue that has significant influence on the homeostasis and overall function of the intervertebral disc. The nucleus pulposus is comprised of a heterogeneous population of cells including large notochord cells and smaller chondrocyte-like cells. Loss of notochord cells has been correlated with the pathogenesis of disc degeneration and consequently, it has been hypothesized that regeneration of the disc could be mediated by notochord cells. Attempts to grow and expand notochord cells in vitro have thus far been limited by cell availability and ineffective culturing methodologies. As a result, co-culturing techniques have been developed in order to exploit notochord-derived signals for the differe...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4747834</comments>
            <pubDate>Tue, 01 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4747834</guid>        </item>
        <item>
            <title>Further evidence for a role of endothelin-1 (ET-1) in critical limb ischaemia.</title>
            <link>http://www.medworm.com/index.php?rid=4747832&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21484588%26dopt%3DAbstract</link>
            <description>Authors: Dashwood MR, Tsui JC
    Critical limb ischaemia (CLI), due to atherosclerotic arterial occlusion, affects over 20,000 people per year in the United Kingdom with many facing lower limb amputation and early death. A role for endothelin-1 (ET-1) in atherosclerosis is well-established and increased circulating and tissue levels of this peptide have been detected in patients with CLI. ET-1 and its receptors were identified in atherosclerotic popliteal arteries obtained from CLI patients undergoing lower limb amputation. In addition, plasma ET-1 levels were compared with those of non-ischaemic controls. ET-1 was associated with regions of atherosclerotic plaque, particularly in regions with high macrophage content. This peptide was also associated with endothelial cells lining the main...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4747832</comments>
            <pubDate>Tue, 01 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4747832</guid>        </item>
        <item>
            <title>Will o' the wisp: CCN4 as a novel molecular target in osteoarthritis.</title>
            <link>http://www.medworm.com/index.php?rid=4747830&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21484589%26dopt%3DAbstract</link>
            <description>Authors: Leask A
    Osteoarthritis (OA), or degenerative arthritis, is characterized by mechanical stress-induced changes in cartilage and bone. OA is a leading cause of chronic disability in North America and Europe. A recent study written by Blom and colleagues (Arthritis and Rheumatism 2009; 60:501-12) showed that elevated wnt signaling was observed in experimental OA as well as in patient samples. The authors found that the known wnt target WISP-1 (CCN4) was also overexpressed; CCN4 was sufficient to recapitulate an OA phenotype in vitro and in vivo, suggesting that CCN4 may be a novel target for drug intervention in OA. This commentary summarizes these exciting findings.
    PMID: 21484589 [PubMed - in process] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4747830</comments>
            <pubDate>Tue, 01 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4747830</guid>        </item>
        <item>
            <title>The gap junction as a &quot;Biological Rosetta Stone&quot;: implications of evolution, stem cells to homeostatic regulation of health and disease in the Barker hypothesis.</title>
            <link>http://www.medworm.com/index.php?rid=4747829&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21484590%26dopt%3DAbstract</link>
            <description>The gap junction as a &quot;Biological Rosetta Stone&quot;: implications of evolution, stem cells to homeostatic regulation of health and disease in the Barker hypothesis.
    J Cell Commun Signal. 2011 Mar;5(1):53-66
    Authors: Trosko JE
    The discovery of the gap junction structure, its functions and the family of the &quot;connexin&quot; genes, has been basically ignored by the major biological disciplines. These connexin genes code for proteins that organize to form membrane-associated hemi-channels, &quot;connexons&quot;, co-join with the connexons of neighboring cells to form gap junctions. Gap junctions appeared in the early evolution of the metazoan. Their fundamental functions, (e.g., to synchronize electrotonic and metabolic functions of societies of cells, and to regulate cell proliferation, cell differe...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4747829</comments>
            <pubDate>Tue, 01 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4747829</guid>        </item>
        <item>
            <title>When there's smoke there'sâ€¦scleroderma: evidence that patients with scleroderma should stop smoking.</title>
            <link>http://www.medworm.com/index.php?rid=4747823&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21484591%26dopt%3DAbstract</link>
            <description>Authors: Leask A
    There is no treatment for the autoimmune disease scleroderma (systemic sclerosis, SSc), a multisystem disorder characterized by vascular damage and fibrosis. In particular, SSc can severely affect the lung, resulting in pulmonary arterial hypertension and fibrosis. Smoking is well-known to affect pulmonary health, and a recent report (Hudson et al., Arthritis Rheum, in press Oct 8) provides convincing evidence that stopping smoking improves disease outcome in SSc patients. This commentary discusses this recent publication which suggests that physicians should encourage SSc patients to stop smoking immediately.
    PMID: 21484591 [PubMed - in process] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4747823</comments>
            <pubDate>Tue, 01 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4747823</guid>        </item>
        <item>
            <title>Spatial-temporal modulation of CCN proteins during wound healing in human skin in vivo.</title>
            <link>http://www.medworm.com/index.php?rid=4747822&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21484592%26dopt%3DAbstract</link>
            <description>In this study, we examined the localization and expression of the six CCN family members in normal adult human skin and during wound healing in vivo. Transcript and protein expression were studied by laser-capture microdissection-coupled real-time PCR and immunohistochemistry, respectively. Our results demonstrate that CCN1, CCN4, and CCN6 are expressed at relatively low levels in normal human skin. CCN2, CCN3, and CCN5 are the most highly expressed transcripts in the epidermis. CCN3 and CCN5 proteins are prominent in epidermal keratinocytes, whereas CCN2 is primarily expressed in melanocytes. Differential expression within epidermal layers suggests that CCN3 and CCN5 are linked with keratinocyte differentiation. CCN2, CCN3 and CCN5, are the three most highly expressed transcripts in the d...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4747822</comments>
            <pubDate>Tue, 01 Mar 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4747822</guid>        </item>
        <item>
            <title>The role of CCN2 in cartilage and bone development.</title>
            <link>http://www.medworm.com/index.php?rid=4747850&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21484188%26dopt%3DAbstract</link>
            <description>Authors: Kubota S, Takigawa M
    CCN2, a classical member of the CCN family of matricellular proteins, is a key molecule that conducts cartilage development in a harmonized manner through novel molecular actions. During vertebrate development, all cartilage is primarily formed by a process of mesenchymal condensation, while CCN2 is induced to promote this process. Afterwards, cartilage develops into several subtypes with different fates and missions, in which CCN2 plays its proper roles according to the corresponding microenvironments. The history of CCN2 in cartilage and bone began with its re-discovery in the growth cartilage in long bones, which determines the skeletal size through the process of endochondral ossification. CCN2 promotes physiological developmental processes not only in...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4747850</comments>
            <pubDate>Mon, 14 Feb 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4747850</guid>        </item>
        <item>
            <title>Proteasome inhibitors in cancer therapy.</title>
            <link>http://www.medworm.com/index.php?rid=4747848&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21484190%26dopt%3DAbstract</link>
            <description>Authors: Crawford LJ, Walker B, Irvine AE
    The ubiquitin proteasome pathway plays a critical role in regulating many processes in the cell which are important for tumour cell growth and survival. Inhibition of proteasome function has emerged as a powerful strategy for anti-cancer therapy. Clinical validation of the proteasome as a therapeutic target was achieved with bortezomib and has prompted the development of a second generation of proteasome inhibitors with improved pharmacological properties. This review summarises the main mechanisms of action of proteasome inhibitors in cancer, the development of proteasome inhibitors as therapeutic agents and the properties and progress of next generation proteasome inhibitors in the clinic.
    PMID: 21484190 [PubMed - as supplied by publisher...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4747848</comments>
            <pubDate>Mon, 31 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4747848</guid>        </item>
        <item>
            <title>Possible strategies for anti-fibrotic drug intervention in scleroderma.</title>
            <link>http://www.medworm.com/index.php?rid=4747849&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21484189%26dopt%3DAbstract</link>
            <description>Authors: Leask A
    There are no approved drugs for treating the fibrosis in scleroderma (systemic sclerosis, SSc). Myfibroblasts within connective tissue express the highly contractile protein Î±-smooth muscle actin (Î±-SMA) and are responsible for the excessive synthesis and remodeling of extracellular matrix (ECM) characterizing SSc. Drugs targeting myofibroblast differentiation, recruitment and activity are currently under consideration as anti-fibrotic treatments in SSc but thus far have principally focused on the transforming growth factor Î² (TGFÎ²), endothelin-1 (ET-1), connective tissue growth factor (CCN2/CTGF) and platelet derived growth factor (PDGF) pathways, which display substantial signaling crosstalk. Moreover, peroxisome proliferator-activated receptor (PPAR)Î³ also appe...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4747849</comments>
            <pubDate>Sat, 29 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4747849</guid>        </item>
        <item>
            <title>Breast cancer at bone metastatic sites: recent discoveries and treatment targets.</title>
            <link>http://www.medworm.com/index.php?rid=4747847&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21484191%26dopt%3DAbstract</link>
            <description>Authors: Hussein O, Komarova SV
    Breast carcinoma is the most common cancer of women. Bones are often involved with breast carcinoma metastases with the resulting morbidity and reduced quality of life. Breast cancer cells arriving at bone tissues mount supportive microenvironment by recruiting and modulating the activity of several host tissue cell types including the specialized bone cells osteoblasts and osteoclasts. Pathologically activated osteoclasts produce osteolytic lesions associated with bone pain, pathological fractures, cord compression and other complications of metastatic breast carcinoma at bone. Over the last decade there has been enormous growth of knowledge in the field of osteoclasts biology both in the physiological state and in the tumor microenvironment. This knowl...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4747847</comments>
            <pubDate>Wed, 19 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4747847</guid>        </item>
        <item>
            <title>Autophagy and ATP-induced anti-apoptosis in antigen presenting cells (APC) follows the cytokine storm in patients after major trauma.</title>
            <link>http://www.medworm.com/index.php?rid=4747846&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21484192%26dopt%3DAbstract</link>
            <description>Authors: Schneider EM, Flacke S, Liu F, Lorenz MR, Schilling P, Nass ME, Foehr KJ, Huber-Lang M, Weiss ME
    Severe trauma and the systemic inflammatory response syndrome (SIRS) occur as a result of a cytokine storm which is in part due to ATP released from damaged tissue. This pathology also leads to increased numbers of immature antigen presenting cells (APC) sharing properties of dendritic cells (DC) or macrophages (MÎ¦). The occurrence of immature APC appears to coincide with the reactivation of herpes virus infections such as Epstein Barr virus (EBV). The aim of this study was the comparative analysis of the ultrastructural and functional characteristics of such immature APC. In addition, we investigated EBV infection/ reactivation and whether immature APC might be targets for natura...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4747846</comments>
            <pubDate>Thu, 13 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4747846</guid>        </item>
        <item>
            <title>Phagocytosis and digestion of pH-sensitive fluorescent dye (Eos-FP) transfected E. coli in whole blood assays from patients with severe sepsis and septic shock.</title>
            <link>http://www.medworm.com/index.php?rid=4747845&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21484193%26dopt%3DAbstract</link>
            <description>Authors: Schreiner L, Huber-Lang M, Weiss ME, Hohmann H, Schmolz M, Schneider EM
    The function of phagocytic and antigen presenting cells is of crucial importance to sustain immune competence against infectious agents as well as malignancies. We here describe a reproducible procedure for the quantification of phagocytosis by leukocytes in whole blood. For this, a pH-sensitive green-fluorescent protein- (GFP) like dye (Eos-FP) is transfected into infectious microroganisms. After UV-irradiation, the transfected bacteria emit green (â‰ˆ5160Â nm) and red (â‰ˆ581Â nm) fluorescent light at 490Â nm excitation. Since the red fluorescent light is sensitive to acidic pH, the phagocytosed bacteria stop emitting red fluorescent light as soon as the phagosomes fuse with lysosomes. The green fluoresc...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4747845</comments>
            <pubDate>Wed, 12 Jan 2011 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4747845</guid>        </item>
        <item>
            <title>Decrypting the labyrinth of inflammatory cell signaling pathways: Editorial to the meeting &quot;Inflammation 2010&quot;.</title>
            <link>http://www.medworm.com/index.php?rid=4464877&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21234120%26dopt%3DAbstract</link>
            <description>Decrypting the labyrinth of inflammatory cell signaling pathways: Editorial to the meeting &quot;Inflammation 2010&quot;.
    J Cell Commun Signal. 2010 Dec;4(4):159-60
    Authors: Kelkel M, Orlikova B, Diederich M
    
    PMID: 21234120 [PubMed - in process] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4464877</comments>
            <pubDate>Wed, 01 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4464877</guid>        </item>
        <item>
            <title>Steroid signaling activation and intracellular localization of sex steroid receptors.</title>
            <link>http://www.medworm.com/index.php?rid=4464876&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21234121%26dopt%3DAbstract</link>
            <description>Authors: Giraldi T, Giovannelli P, Di Donato M, Castoria G, Migliaccio A, Auricchio F
    In addition to stimulating gene transcription, sex steroids trigger rapid, non-genomic responses in the extra-nuclear compartment of target cells. These events take place within seconds or minutes after hormone administration and do not require transcriptional activity of sex steroid receptors. Depending on cell systems, activation of extra-nuclear signaling pathways by sex steroids fosters cell cycle progression, prevents apoptosis, leads to epigenetic modifications and increases cell migration through cytoskeleton changes. These findings have raised the question of intracellular localization of sex steroid receptors mediating these responses. During the past years, increasing evidence has shown that...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4464876</comments>
            <pubDate>Wed, 01 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4464876</guid>        </item>
        <item>
            <title>Selective regulation of nuclear orphan receptors 4A by adenosine receptor subtypes in human mast cells.</title>
            <link>http://www.medworm.com/index.php?rid=4464875&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21234122%26dopt%3DAbstract</link>
            <description>Authors: Zhang L, Paine C, Dip R
    Nuclear orphan receptors 4A (NR4A) are early responsive genes that belong to the superfamily of hormone receptors and comprise NR4A1, NR4A2 and NR4A3. They have been associated to transcriptional activation of multiple genes involved in inflammation, apoptosis and cell cycle control. Here, we establish a link between NR4As and adenosine, a paradoxical inflammatory molecule that can contribute to persistence of inflammation or mediate inflammatory shutdown. Transcriptomics screening of the human mast cell-line HMC-1 revealed a sharp induction of transcriptionally active NR4A2 and NR4A3 by the adenosine analogue NECA. The concomitant treatment of NECA and the adenosine receptor A(2A) (A(2A)AR) selective antagonist SCH-58261 exaggerated this effect, sugges...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4464875</comments>
            <pubDate>Wed, 01 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4464875</guid>        </item>
        <item>
            <title>TSP-1 in lung fibrosis.</title>
            <link>http://www.medworm.com/index.php?rid=4464874&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21234123%26dopt%3DAbstract</link>
            <description>Authors: Di Guglielmo GM
    Lung fibrosis is often treated with corticosteroids to reduce the inflammatory response, however, no effective treatment options exist for the underlying disease. An important player in the fibrotic cascade is the cytokine, transforming growth factor beta (TGFÎ²). TGFÎ² is converted from an inactive procytokine complex to active TGFÎ² by enzymes such as thrombospondin-1 (TSP-1). It is therefore presumed that TSP-1 deficient mice would fare better to bleomycin-induced pulmonary fibrosis because TGFÎ² would not be efficiently converted to the active form. Interestingly, a recent article by Ezzie and colleagues shows that TSP-1 deficiency does not protect mice from systemic bleomycin challenge. Indeed, they find the opposite, as TSP-1-null mice appear to exhibit g...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4464874</comments>
            <pubDate>Wed, 01 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4464874</guid>        </item>
        <item>
            <title>Commentary on a recent article-&quot;A prostacyclin analogue, Iloprost, protects from bleomycin-induced fibrosis in mice&quot; Zhu Y et al. Respir Res. 2010 Mar 20;11(1):34.</title>
            <link>http://www.medworm.com/index.php?rid=4464873&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21234124%26dopt%3DAbstract</link>
            <description>Commentary on a recent article-&quot;A prostacyclin analogue, Iloprost, protects from bleomycin-induced fibrosis in mice&quot; Zhu Y et al. Respir Res. 2010 Mar 20;11(1):34.
    J Cell Commun Signal. 2010 Dec;4(4):187-8
    Authors: Stratton R, Newton F
    Data from our laboratory show that in vitro fibroblasts are exquisitely responsive to prostacyclin and the prostacyclin derivative Iloprost, which block their activation by TGFÎ². A recent article by Zhu Y et al confirm these effects in vivo showing that Iloprost, given as a single intraperitoneal injection, blocks lung fibrosis in the bleomycin model of lung injury and fibrosis. These results are important because at present no effective clinical treatments are available to treat idiopathic lung fibrosis, which progresses and leads to respirator...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4464873</comments>
            <pubDate>Wed, 01 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4464873</guid>        </item>
        <item>
            <title>Mastering a mediator: blockade of CCN-2 shows early promise in human diabetic kidney disease.</title>
            <link>http://www.medworm.com/index.php?rid=4464872&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21234125%26dopt%3DAbstract</link>
            <description>Authors: Twigg SM
    In diabetes complications, CCN-2 (known originally as CTGF) has been implicated in diabetic nephropathy both as a marker and a mediator of disease. This commentary addresses CCN-2 in diabetic nephropathy, in the context of the recent publication of the first human study to inhibit CCN-2 bioactivity in diabetic kidney disease.
    PMID: 21234125 [PubMed - in process] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4464872</comments>
            <pubDate>Wed, 01 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4464872</guid>        </item>
        <item>
            <title>Targeting the jagged/notch pathway: a new treatment for fibrosis?</title>
            <link>http://www.medworm.com/index.php?rid=4464871&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21234126%26dopt%3DAbstract</link>
            <description>Authors: Leask A
    There is no treatment for fibrotic disease. TGFÎ² is known to promote fibrogenesis in vivo and in vitro, however, development of anti-fibrotic strategies targeting the TGFÎ² axis is problematic owing to the pleitropic nature of TGFÎ² action. Two recent papers (Kavian et al. 2010; Nyhan et al. 2010) suggest that the jagged/Notch pathway may selectively mediate fibrogenic properties of TGFÎ² and thus may represent a novel therapeutic approach to fibrosis for scleroderma and kidney fibrosis; these papers are the subject of this commentary.
    PMID: 21234126 [PubMed - in process] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4464871</comments>
            <pubDate>Wed, 01 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4464871</guid>        </item>
        <item>
            <title>CCN6 (WISP3): a new anti-cancer therapy?</title>
            <link>http://www.medworm.com/index.php?rid=4464870&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21234127%26dopt%3DAbstract</link>
            <description>Authors: Leask A
    The CCN family of matricellular proteins are dysregulated in cancers, and may strategies targeting them may represent novel approaches to treating these diseases. A recent study from Huang and colleagues (Cancer Res. 70: 3340-50, 2010) suggests that CCN6 (WISP3) is downregulated in aggressive breast cancers, and this phenomenon may result in the promotion of tumor survival. CCN6 may represent a novel therapeutic approach to breast cancer.
    PMID: 21234127 [PubMed - in process] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4464870</comments>
            <pubDate>Wed, 01 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4464870</guid>        </item>
        <item>
            <title>B cell block: is rituximab a new possible treatment for systemic sclerosis?</title>
            <link>http://www.medworm.com/index.php?rid=4464869&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21234128%26dopt%3DAbstract</link>
            <description>This report is one of a series of recent studies suggesting that rituximab may be a possible treatment for SSc. This commentary summarizes these observations.
    PMID: 21234128 [PubMed - in process] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4464869</comments>
            <pubDate>Wed, 01 Dec 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4464869</guid>        </item>
        <item>
            <title>JCCS-A journal for translational research.</title>
            <link>http://www.medworm.com/index.php?rid=4165220&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21063500%26dopt%3DAbstract</link>
            <description>Authors: Leask A, Perbal B
    
    PMID: 21063500 [PubMed - in process] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4165220</comments>
            <pubDate>Fri, 01 Oct 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4165220</guid>        </item>
        <item>
            <title>Signalling in the genomic era.</title>
            <link>http://www.medworm.com/index.php?rid=4165219&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21063501%26dopt%3DAbstract</link>
            <description>Authors: Lo Vasco VR
    For a complex organism, short range signalling is not sufficient to coordinate the behaviour of all cells composing itself. The response to stimuli is the reprogramming of cell activity (resulting in differentiation, proliferation, stand by or apoptosis depending on the set of signals). Cells own elaborate and complex systems of proteins that enable them to communicate, including both secreted signalling molecules and related factors, deriving from relic mechanisms. The intra and intercellular signalling are actively studied not only to comprehend the basic mechanisms that allowed the evolution of mammals species on earth, but also because the alteration of one or more of these pathways is recognized to be involved in a crescent number of human diseases, both degen...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4165219</comments>
            <pubDate>Fri, 01 Oct 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4165219</guid>        </item>
        <item>
            <title>CCN5: biology and pathophysiology.</title>
            <link>http://www.medworm.com/index.php?rid=4165218&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21063502%26dopt%3DAbstract</link>
            <description>Authors: Russo JW, Castellot JJ
    CCN5 is one of six proteins in the CCN family. This family of proteins has been shown to play important roles in many processes, including proliferation, migration, adhesion, extracellular matrix regulation, angiogenesis, tumorigenesis, fibrosis, and implantation. In this review, we focus on the biological and putative pathophysiological roles of CCN5. This intriguing protein is structurally unique among the CCN family members, and has a unique biological activity profile as well.
    PMID: 21063502 [PubMed - in process] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4165218</comments>
            <pubDate>Fri, 01 Oct 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4165218</guid>        </item>
        <item>
            <title>The contribution of adhesion signaling to lactogenesis.</title>
            <link>http://www.medworm.com/index.php?rid=4165217&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21063503%26dopt%3DAbstract</link>
            <description>Authors: Morrison B, Cutler ML
    The mammary gland undergoes hormonally controlled cycles of pubertal maturation, pregnancy, lactation, and involution, and these processes rely on complex signaling mechanisms, many of which are controlled by cell-cell and cell-matrix adhesion. The adhesion of epithelial cells to the extracellular matrix initiates signaling mechanisms that have an impact on cell proliferation, survival, and differentiation throughout lactation. The control of integrin expression on the mammary epithelial cells, the composition of the extracellular matrix and the presence of secreted matricellular proteins all contribute to essential adhesion signaling during lactogenesis. In vitro and in vivo studies, including the results from genetically engineered mice, have shed light...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4165217</comments>
            <pubDate>Fri, 01 Oct 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4165217</guid>        </item>
        <item>
            <title>A novel role of CCN3 in regulating endothelial inflammation.</title>
            <link>http://www.medworm.com/index.php?rid=4165216&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21063504%26dopt%3DAbstract</link>
            <description>This study identifies CCN3 as a novel regulator of endothelial proinflammatory activation.
    PMID: 21063504 [PubMed - in process] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4165216</comments>
            <pubDate>Fri, 01 Oct 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4165216</guid>        </item>
        <item>
            <title>Yin and Yang Part Deux: CCN5 inhibits the pro-fibrotic effects of CCN2.</title>
            <link>http://www.medworm.com/index.php?rid=4165215&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21063505%26dopt%3DAbstract</link>
            <description>Authors: Leask A
    There is no treatment for fibrotic disease is a significant cause of mortality. CCN2 Members of the CCN family of matricellular proteins have a characteristic four domain structure. CCN2 (connective tissue growth factor) is believed to play an essential role in fibrogenesis. In a recent paper, data are provided that CCN5 (wisp2), which lacks the carboxy-terminal heparin-binding domain shared by the other CCN proteins, may act as a dominant-negative protein to suppress CCN2-mediated fibrogenesis. These data are consistent with the notion that different CCN proteins may enhance or suppress each other's action and also suggest that CCN5, may be used as a novel anti-fibrotic therapy.
    PMID: 21063505 [PubMed - in process] (Source: Journal of Cell Communication and Signal...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4165215</comments>
            <pubDate>Fri, 01 Oct 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4165215</guid>        </item>
        <item>
            <title>When there's smoke there's.....CCN2.</title>
            <link>http://www.medworm.com/index.php?rid=4165214&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21063506%26dopt%3DAbstract</link>
            <description>Authors: Leask A
    Smoking causes oral fibrosis. In a recent report, Takeuchi and colleagues (J Dent Res 89:34-9, 2010) evaluate whether nicotine can directly elevate collagen production in gingival fibroblasts. They show that CCN2 (connective tissue growth factor, CTGF) is elevated in response to nicotine and that a neutralizing CCN2 antibody reduces the ability of nicotine to promote collagen production. These data suggest that nicotine from smoking may promote periodontal fibrosis via CCN2. This commentary summarizes these findings.
    PMID: 21063506 [PubMed - in process] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4165214</comments>
            <pubDate>Fri, 01 Oct 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">4165214</guid>        </item>
        <item>
            <title>Role of prostaglandins in fibroblast activation and fibrosis.</title>
            <link>http://www.medworm.com/index.php?rid=3653307&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20531982%26dopt%3DAbstract</link>
            <description>Authors: Stratton R, Shiwen X
    Fibroblasts release prostaglandins and express a range of prostanoid receptors. However the importance of prostaglandins in fibroblast biology have not been fully explored. Our studies showed that the prostaglandin metabolite PGI(2) blocks the activation of fibroblasts, antagonising the induction of Ras/MEK/ERK signalling by TGFbeta. Endogenous PGI(2) acts so as to limit the activation of fibroblasts following tissue injury. By contrast PGE(2) induced in injured tissues or disease states may promote recruitment of inflammatory cells and lead to secondary activation of fibroblasts. The effects of PGI(2) on cell signaling could be manipulated to inhibit fibrosis in patients.
    PMID: 20531982 [PubMed - in process] (Source: Journal of Cell Communication and ...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3653307</comments>
            <pubDate>Mon, 31 May 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3653307</guid>        </item>
        <item>
            <title>Prostaglandin E(2) is crucial in the response of podocytes to fluid flow shear stress.</title>
            <link>http://www.medworm.com/index.php?rid=3653306&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20531983%26dopt%3DAbstract</link>
            <description>Authors: Srivastava T, McCarthy ET, Sharma R, Cudmore PA, Sharma M, Johnson ML, Bonewald LF
    Podocytes play a key role in maintaining and modulating the filtration barrier of the glomerulus. Because of their location, podocytes are exposed to mechanical strain in the form of fluid flow shear stress (FFSS). Several human diseases are characterized by glomerular hyperfiltration, such as diabetes mellitus and hypertension. The response of podocytes to FFSS at physiological or pathological levels is not known. We exposed cultured podocytes to FFSS, and studied changes in actin cytoskeleton, prostaglandin E(2) (PGE(2)) production and expression of cyclooxygenase-1 and-2 (COX-1, COX-2). FFSS caused a reduction in transversal F-actin stress filaments and the appearance of cortical actin networ...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3653306</comments>
            <pubDate>Mon, 31 May 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3653306</guid>        </item>
        <item>
            <title>CCN5, a secreted protein, localizes to the nucleus.</title>
            <link>http://www.medworm.com/index.php?rid=3653305&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20531984%26dopt%3DAbstract</link>
            <description>Authors: Wiesman KC, Wei L, Baughman C, Russo J, Gray MR, Castellot JJ
    CCN5, a member of the CCN family of growth factors, inhibits the proliferation and migration of smooth muscle cells in cell culture and animal models. Expressed in both embryonic and adult tissues, CCN5 exhibits a matricellular localization pattern characteristic of secreted proteins that are closely associated with the cell surface. In addition to this observed expression pattern, immunohistochemical evidence suggests the presence of nuclear CCN5 in some cells. To determine if CCN5 localizes to the nucleus we performed immunofluorescence, confocal imaging, and cell fractionation to corroborate the immunohistochemical observations. After confirming the presence of nuclear CCN5 using four independent experimental met...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3653305</comments>
            <pubDate>Mon, 31 May 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3653305</guid>        </item>
        <item>
            <title>Spatiotemporal expression of periostin during skin development and incisional wound healing: lessons for human fibrotic scar formation.</title>
            <link>http://www.medworm.com/index.php?rid=3653304&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20531985%26dopt%3DAbstract</link>
            <description>Authors: Zhou HM, Wang J, Elliott C, Wen W, Hamilton DW, Conway SJ
    Differentiation of fibroblasts to myofibroblasts and collagen fibrillogenesis are two processes essential for normal cutaneous development and repair, but their misregulation also underlies skin-associated fibrosis. Periostin is a matricellular protein normally expressed in adult skin, but its role in skin organogenesis, incisional wound healing and skin pathology has yet to be investigated in any depth. Using C57/BL6 mouse skin as model, we first investigated periostin protein and mRNA spatiotemporal expression and distribution during development and after incisional wounding. Secondarily we assessed whether periostin is expressed in human skin pathologies, including keloid and hypertrophic scars, psoriasis and atopic ...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3653304</comments>
            <pubDate>Mon, 31 May 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3653304</guid>        </item>
        <item>
            <title>It's a knockout: CCN3 suppresses neointimal thickening.</title>
            <link>http://www.medworm.com/index.php?rid=3653303&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20531986%26dopt%3DAbstract</link>
            <description>Authors: Leask A
    The role of CCN proteins in vivo is only just becoming understood. A prototypical member of the CCN family, CCN3 suppresses proliferation. In a study in press, Shimoyama and colleagues show that mice lacking CCN3 have a hyperproliferative response to vascular injury. These data, along with other recent observations, suggest that CCN3 may represent a novel therapy for hyperproliferative diseases.
    PMID: 20531986 [PubMed - in process] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3653303</comments>
            <pubDate>Mon, 31 May 2010 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">3653303</guid>        </item>
        <item>
            <title>Regulation of pro-inflammatory and pro-fibrotic factors by CCN2/CTGF in H9c2 cardiomyocytes.</title>
            <link>http://www.medworm.com/index.php?rid=3328098&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20195389%26dopt%3DAbstract</link>
            <description>In this study, cellular mechanisms by which CTGF regulates pathways involved in fibrosis and inflammation were explored. Murine H9c2 cardiomyocytes were treated with recombinant human (rh)CTGF and ECM formation gene expression: fibronectin, collagen type -I and -III and ECM degradation genes: TIMP-1, TIMP-2 and PAI-1 were found to be induced. CTGF treatment also increased pro-inflammatory cytokines TNF-alpha, IL-6, MCP-1 and IL-8. CTGF upregulated TGF-beta1 mRNA and rapidly induced phosphorylation of TrkA. The CTGF-induced pro-fibrotic and pro-inflammatory effects were blocked by anti-TGF-beta neutralizing antibody and Alk 5 inhibitor (SB431542). A specific blocker of TrkA activation, k252a, also abrogated CTGF-induced effects on fibrosis and gene expresison of MCP-1 and IL-8, but not TNF-...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3328098</comments>
            <pubDate>Mon, 01 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3328098</guid>        </item>
        <item>
            <title>The lectin concanavalin-A signals MT1-MMP catalytic independent induction of COX-2 through an IKKgamma/NF-kappaB-dependent pathway.</title>
            <link>http://www.medworm.com/index.php?rid=3328097&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20195390%26dopt%3DAbstract</link>
            <description>Authors: Sina A, Proulx-Bonneau S, Roy A, Poliquin L, Cao J, Annabi B
    The lectin from Canavalia ensiformis (Concanavalin-A, ConA), one of the most abundant lectins known, enables one to mimic biological lectin/carbohydrate interactions that regulate extracellular matrix protein recognition. As such, ConA is known to induce membrane type-1 matrix metalloproteinase (MT1-MMP) which expression is increased in brain cancer. Given that MT1-MMP correlated to high expression of cyclooxygenase (COX)-2 in gliomas with increasing histological grade, we specifically assessed the early proinflammatory cellular signaling processes triggered by ConA in the regulation of COX-2. We found that treatment with ConA or direct overexpression of a recombinant MT1-MMP resulted in the induction of COX-2 expres...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3328097</comments>
            <pubDate>Mon, 01 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3328097</guid>        </item>
        <item>
            <title>CCN3/CCN2 regulation and the fibrosis of diabetic renal disease.</title>
            <link>http://www.medworm.com/index.php?rid=3328096&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20195391%26dopt%3DAbstract</link>
            <description>Authors: Riser BL, Najmabadi F, Perbal B, Rambow JA, Riser ML, Sukowski E, Yeger H, Riser SC, Peterson DR
    Prior work in the CCN field, including our own, suggested to us that there might be co-regulatory activity and function as part of the actions of this family of cysteine rich cytokines. CCN2 is now regarded as a major pro-fibrotic molecule acting both down-stream and independent of TGF-beta1, and appears causal in the disease afflicting multiple organs. Since diabetic renal fibrosis is a common complication of diabetes, and a major cause of end stage renal disease (ESRD), we examined the possibility that CCN3 (NOV), might act as an endogenous negative regulator of CCN2 with the capacity to limit the overproduction of extracellular matrix (ECM), and thus prevent, or ameliorate fibro...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3328096</comments>
            <pubDate>Mon, 01 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3328096</guid>        </item>
        <item>
            <title>Thrombin-induced CCN2 expression as a target for anti-fibrotic therapy in scleroderma.</title>
            <link>http://www.medworm.com/index.php?rid=3057266&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19957054%26dopt%3DAbstract</link>
            <description>Authors: Leask A
    Scleroderma (systemic sclerosis, SSc) is a fibrotic disease for which there is no therapy. CCN2 (connective tissue growth factor, CTGF) is a marker and mediator of fibrosis. Previously, it has been shown that thrombin induces CCN2 expression in fibroblasts. In a recent fascinating report, Bogatkevich et al. (Arthritis Rheum 60:3455-3464, 2009) show that dabigatran, an inhibitor of thrombin action, blocks the overexpression of CCN2 by scleroderma fibroblasts and reverses the contractile phenotype of these cells. These results strongly suggest that dabigatran may be a potential antifibrotic drug for the treatment of fibrosing diseases such as scleroderma.
    PMID: 19957054 [PubMed - as supplied by publisher] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3057266</comments>
            <pubDate>Thu, 03 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3057266</guid>        </item>
        <item>
            <title>Connective tissue growth factor is induced in bleomycin-induced skin scleroderma.</title>
            <link>http://www.medworm.com/index.php?rid=3000683&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19916059%26dopt%3DAbstract</link>
            <description>In this report, we use an antibody recognizing CCN2 to assess the cell types in mouse dermis which express CCN2 in the bleomycin model of skin scleroderma. Control (PBS injected) and fibrotic (bleomycin-injected) dermis was examined for CCN2, alpha-smooth muscle actin (alpha-SMA) (to detect myofibroblasts), and NG2 (to detect pericytes) expression. Consistent with previously published data, CCN2 expression was largely absent in the dermis of control mice. However, upon exposure to bleomycin, CCN2 was observed in the dermis. Cells that expressed CCN2 were alpha-SMA-expressing myofibroblasts. Approximately 85% of myofibroblasts were NG2-positive, CCN2-expressing pericytes, indicating that pericytes significantly contributed to the presence of myofibroblasts in sclerotic dermis. Thus CCN2 is ...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3000683</comments>
            <pubDate>Sun, 15 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3000683</guid>        </item>
        <item>
            <title>The role of astrocyte-secreted matricellular proteins in central nervous system development and function.</title>
            <link>http://www.medworm.com/index.php?rid=2991957&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19904629%26dopt%3DAbstract</link>
            <description>Authors: Eroglu C
    Matricellular proteins, such as thrombospondins (TSPs1-4), SPARC, SPARC-like1 (hevin) and tenascin C are expressed by astrocytes in the central nervous system (CNS) of rodents. The spatial and temporal expression patterns of these proteins suggest that they may be involved in important developmental processes such as cell proliferation and maturation, cell migration, axonal guidance and synapse formation. In addition, upon injury to the nervous system the expression of these proteins is upregulated, suggesting that they play a role in tissue remodeling and repair in the adult CNS. The genes encoding these proteins have been disrupted in mice. Interestingly, none of these proteins are required for survival, and furthermore, there are no evident abnormalities at the gro...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2991957</comments>
            <pubDate>Wed, 11 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2991957</guid>        </item>
        <item>
            <title>Deadly liaisons: fatal attraction between CCN matricellular proteins and the tumor necrosis factor family of cytokines.</title>
            <link>http://www.medworm.com/index.php?rid=2977958&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19898959%26dopt%3DAbstract</link>
            <description>Authors: Chen CC, Lau LF
    Recent studies have revealed an unexpected synergism between two seemingly unrelated protein families: CCN matricellular proteins and the tumor necrosis factor (TNF) family of cytokines. CCN proteins are dynamically expressed at sites of injury repair and inflammation, where TNF cytokines are also expressed. Although TNFalpha is an apoptotic inducer in some cancer cells, it activates NFkappaB to promote survival and proliferation in normal cells, and its cytotoxicity requires inhibition of de novo protein synthesis or NFkappaB signaling. The presence of CCN1, CCN2, or CCN3 overrides this requirement and unmasks the apoptotic potential of TNFalpha, thus converting TNFalpha from a proliferation-promoting protein into an apoptotic inducer. These CCN proteins also ...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2977958</comments>
            <pubDate>Sat, 07 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2977958</guid>        </item>
        <item>
            <title>Thrombospondin-2 and SPARC/osteonectin are critical regulators of bone remodeling.</title>
            <link>http://www.medworm.com/index.php?rid=2944273&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19862642%26dopt%3DAbstract</link>
            <description>Authors: Delany AM, Hankenson KD
    Thrombospondin-2 (TSP2) and osteonectin/BM-40/SPARC are matricellular proteins that are highly expressed by bone cells. Mice deficient in either of these proteins show phenotypic alterations in the skeleton, and these phenotypes are most pronounced under conditions of altered bone remodeling. For example, TSP2-null mice have higher cortical bone volume and are resistant to bone loss associated with ovariectomy, whereas SPARC-null mice have decreased trabecular bone volume and fail to demonstrate an increase in bone mineral density in response to a bone-anabolic parathyroid hormone treatment regimen. In vitro, marrow stromal cell (MSC) osteoprogenitors from TSP2-null mice have increased proliferation but delayed formation of mineralized matrix. Similarly...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2944273</comments>
            <pubDate>Wed, 28 Oct 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2944273</guid>        </item>
        <item>
            <title>Endothelin-1 as a neuropeptide: neurotransmitter or neurovascular effects?</title>
            <link>http://www.medworm.com/index.php?rid=2917095&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19847673%26dopt%3DAbstract</link>
            <description>Authors: Dashwood MR, Loesch A
    Endothelin-1 (ET-1) is an endothelium-derived peptide that also possesses potent mitogenic activity. There is also a suggestion the ET-1 is a neuropeptide, based mainly on its histological identification in both the central and peripheral nervous system in a number of species, including man. A neuropeptide role for ET-1 is supported by studies showing a variety of effects caused following its administration into different regions of the brain and by application to peripheral nerves. In addition there are studies proposing that ET-1 is implicated in a number of neural circuits where its transmitter affects range from a role in pain and temperature control to its action on the hypothalamo-neurosecretory system. While the effect of ET-1 on nerve tissue is be...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2917095</comments>
            <pubDate>Wed, 21 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2917095</guid>        </item>
        <item>
            <title>The role of thrombospondins in wound healing, ischemia, and the foreign body reaction.</title>
            <link>http://www.medworm.com/index.php?rid=2917096&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19844806%26dopt%3DAbstract</link>
            <description>Authors: Kyriakides TR, Maclauchlan S
    Thrombospondin (TSP) 1 and TSP2 have been implicated in the regulation of several processes during tissue repair. Due to their matricellular nature, these proteins are thought to modulate cell-matrix interactions through a variety of mechanisms specific to the spatio-temporal context of their expression. Most notably, TSP1 and TSP2 appear to play distinct, non-overlapping roles in the healing of skin wounds. In contrast, both proteins have been implicated as regulators of ischemia-induced angiogenesis. Moreover, TSP2 has been shown to be a critical regulator of angiogenesis in the foreign body response (FBR). In this review, we discuss the role of TSPs in tissue repair and examine the mechanistic data regarding the ability of the thrombospondins to...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2917096</comments>
            <pubDate>Tue, 20 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2917096</guid>        </item>
        <item>
            <title>The role of tenascin-C in tissue injury and tumorigenesis.</title>
            <link>http://www.medworm.com/index.php?rid=2911039&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19838819%26dopt%3DAbstract</link>
            <description>Authors: Midwood KS, Orend G
    The extracellular matrix molecule tenascin-C is highly expressed during embryonic development, tissue repair and in pathological situations such as chronic inflammation and cancer. Tenascin-C interacts with several other extracellular matrix molecules and cell-surface receptors, thus affecting tissue architecture, tissue resilience and cell responses. Tenascin-C modulates cell migration, proliferation and cellular signaling through induction of pro-inflammatory cytokines and oncogenic signaling molecules amongst other mechanisms. Given the causal role of inflammation in cancer progression, common mechanisms might be controlled by tenascin-C during both events. Drugs targeting the expression or function of tenascin-C or the tenascin-C protein itself are curr...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2911039</comments>
            <pubDate>Fri, 16 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2911039</guid>        </item>
        <item>
            <title>The interaction of Thrombospondins with extracellular matrix proteins.</title>
            <link>http://www.medworm.com/index.php?rid=2902073&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19830595%26dopt%3DAbstract</link>
            <description>Authors: Tan K, Lawler J
    The thrombospondins (TSPs) are a family of five matricellular proteins that appear to function as adapter molecules to guide extracellular matrix synthesis and tissue remodeling in a variety of normal and disease settings. Various TSPs have been shown to bind to fibronectin, laminin, matrilins, collagens and other extracellular matrix (ECM) proteins. The importance of TSP-1 in this context is underscored by the fact that it is rapidly deposited at the sites of tissue damage by platelets. An association of TSPs with collagens has been known for over 25 years. The observation that the disruption of the TSP-2 gene in mice leads to collagen fibril abnormalities provided important in vivo evidence that these interactions are physiologically important. Recent biochem...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2902073</comments>
            <pubDate>Thu, 15 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2902073</guid>        </item>
        <item>
            <title>A sticky situation: CCN1 promotes both proliferation and apoptosis of cancer cells.</title>
            <link>http://www.medworm.com/index.php?rid=2902072&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19834822%26dopt%3DAbstract</link>
            <description>Authors: Leask A
    Members of the CCN family of matricellular signaling regulators promote cell adhesion through integrins and heparan sulfate-containing proteoglycans. A paradox of the CCN field is that, depending on the set of circumstances examined, individual CCN molecules can have quite different, and often opposing, effects. In a recent report, Franzen and colleagues (Mol Cancer Res. 7:1045-1055, 2009) show using siRNA knockdown that CCN1 (cyr61) is essential for the proliferation of prostate cancer cells. Intriguingly, on the other hand, CCN1 also enhances TRAIL-induced apoptosis. Thus the utility of anti-CCN1 therapy in cancer needs to be carefully considered in light of these divergent results. The significance of this paper is discussed.
    PMID: 19834822 [PubMed - as supplied...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2902072</comments>
            <pubDate>Thu, 15 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2902072</guid>        </item>
        <item>
            <title>SPARC: a matricellular regulator of tumorigenesis.</title>
            <link>http://www.medworm.com/index.php?rid=2872114&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19809893%26dopt%3DAbstract</link>
            <description>Authors: Arnold SA, Brekken RA
    Although many clinical studies have found a correlation of SPARC expression with malignant progression and patient survival, the mechanisms for SPARC function in tumorigenesis and metastasis remain elusive. The activity of SPARC is context- and cell-type-dependent, which is highlighted by the fact that SPARC has shown seemingly contradictory effects on tumor progression in both clinical correlative studies and in animal models. The capacity of SPARC to dictate tumorigenic phenotype has been attributed to its effects on the bioavailability and signaling of integrins and growth factors/chemokines. These molecular pathways contribute to many physiological events affecting malignant progression, including extracellular matrix remodeling, angiogenesis, immune ...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2872114</comments>
            <pubDate>Tue, 06 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2872114</guid>        </item>
        <item>
            <title>The matricellular functions of small leucine-rich proteoglycans (SLRPs).</title>
            <link>http://www.medworm.com/index.php?rid=2872113&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19809894%26dopt%3DAbstract</link>
            <description>Authors: Merline R, Schaefer RM, Schaefer L
    The small leucine-rich proteoglycans (SLRPs) are biologically active components of the extracellular matrix (ECM), consisting of a protein core with leucine rich-repeat (LRR) motifs covalently linked to glycosaminoglycan (GAG) side chains. The diversity in composition resulting from the various combinations of protein cores substituted with one or more GAG chains along with their pericellular localization enables SLRPs to interact with a host of different cell surface receptors, cytokines, growth factors, and other ECM components, leading to modulation of cellular functions. SLRPs are capable of binding to: (i) different types of collagens, thereby regulating fibril assembly, organization, and degradation; (ii) Toll-like receptors (TLRs), com...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2872113</comments>
            <pubDate>Thu, 01 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2872113</guid>        </item>
        <item>
            <title>Connective tissue growth factor (CCN2, CTGF) and organ fibrosis: lessons from transgenic animals.</title>
            <link>http://www.medworm.com/index.php?rid=2859191&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19798591%26dopt%3DAbstract</link>
            <description>Authors: Brigstock DR
    In recent months, four different systems have been reported in the literature in which CCN2 transgenes were individually expressed in podocytes, hepatocytes, cardiomyocytes or respiratory epithelial cells to achieve overexpression in, respectively, the kidney, liver, heart, or lung. These transgenic systems have provided valuable information about the contribution of CCN2 to fibrosis in vivo and have begun to reveal the complexities of the underlying mechanisms involved. On the one hand, studies of these animals have revealed that CCN2 overexpression does not necessarily lead directly to fibrotic pathology but may cause severe non-fibrotic tissue damage due to its other effects on cell function (e.g. heart). On the other hand, overexpression of CCN2 in concert wit...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2859191</comments>
            <pubDate>Thu, 01 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2859191</guid>        </item>
        <item>
            <title>Thrombospondins in the heart: potential functions in cardiac remodeling.</title>
            <link>http://www.medworm.com/index.php?rid=2859190&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19798592%26dopt%3DAbstract</link>
            <description>Authors: Schellings MW, van Almen GC, Sage EH, Heymans S
    Cardiac remodeling after myocardial injury involves inflammation, angiogenesis, left ventricular hypertrophy and matrix remodeling. Thrombospondins (TSPs) belong to the group of matricellular proteins, which are non-structural extracellular matrix proteins that modulate cell-matrix interactions and cell function in injured tissues or tumors. They interact with different matrix and membrane-bound proteins due to their diverse functional domains. That the expression of TSPs strongly increases during cardiac stress or injury indicates an important role for them during cardiac remodeling. Recently, the protective properties of TSP expression against heart failure have been acknowledged. The current review will focus on the biological...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2859190</comments>
            <pubDate>Thu, 01 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2859190</guid>        </item>
        <item>
            <title>The role of osteopontin in inflammatory processes.</title>
            <link>http://www.medworm.com/index.php?rid=2859189&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19798593%26dopt%3DAbstract</link>
            <description>Authors: Lund SA, Giachelli CM, Scatena M
    Osteopontin (OPN) is a matricellular protein that mediates diverse biological functions. OPN is involved in normal physiological processes and is implicated in the pathogenesis of a variety of disease states, including atherosclerosis, glomerulonephritis, cancer, and several chronic inflammatory diseases. Through interactions with several integrins, OPN mediates cell migration, adhesion, and survival in many cell types. OPN also functions as a Th1 cytokine, promotes cell-mediated immune responses, and plays a role in chronic inflammatory and autoimmune diseases. Besides its function in inflammation, OPN is also a regulator of biomineralization and a potent inhibitor of vascular calcification.
    PMID: 19798593 [PubMed - as supplied by publishe...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2859189</comments>
            <pubDate>Thu, 01 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2859189</guid>        </item>
        <item>
            <title>Thrombopoietic-mesenchymal interaction that may facilitate both endochondral ossification and platelet maturation via CCN2.</title>
            <link>http://www.medworm.com/index.php?rid=2859188&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19798594%26dopt%3DAbstract</link>
            <description>In this study, we initially pursued the possible origin of the CCN2 in platelets. First, we examined if the CCN2 in platelets was produced by megakaryocyte progenitors during differentiation. Unexpectedly, neither megakaryocytic CMK cells nor megakaryocytes that had differentiated from human haemopoietic stem cells in culture showed any detectable CCN2 gene expression or protein production. Together with the fact that no appreciable CCN2 was detected in megakaryocytes in vivo, these results suggest that megakaryocytes themselves do not produce CCN2. Next, we suspected that mesenchymal cells situated around megakaryocytes in the bone marrow were stimulated by the latter to produce CCN2, which was then taken up by platelets. To evaluate this hypothesis, we cultured human chondrocytic HCS-2/8...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2859188</comments>
            <pubDate>Thu, 01 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2859188</guid>        </item>
        <item>
            <title>Fibulin-5, an integrin-binding matricellular protein: its function in development and disease.</title>
            <link>http://www.medworm.com/index.php?rid=2859187&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19798595%26dopt%3DAbstract</link>
            <description>Authors: Yanagisawa H, Schluterman MK, Brekken RA
    Interactions between the extracellular matrix (ECM) and cells are critical in embryonic development, tissue homeostasis, physiological remodeling, and tumorigenesis. Matricellular proteins, a group of ECM components, mediate cell-ECM interactions. One such molecule, Fibulin-5 is a 66-kDa glycoprotein secreted by various cell types, including vascular smooth muscle cells (SMCs), fibroblasts, and endothelial cells. Fibulin-5 contributes to the formation of elastic fibers by binding to structural components including tropoelastin and fibrillin-1, and to cross-linking enzymes, aiding elastic fiber assembly. Mice deficient in the fibulin-5 gene (Fbln5) exhibit systemic elastic fiber defects with manifestations of loose skin, tortuous aorta, ...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2859187</comments>
            <pubDate>Thu, 01 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2859187</guid>        </item>
        <item>
            <title>SPARC functions as an inhibitor of adipogenesis.</title>
            <link>http://www.medworm.com/index.php?rid=2859186&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19798596%26dopt%3DAbstract</link>
            <description>Authors: Nie J, Sage EH
    Adipogenesis, a key step in the pathogenesis of obesity, involves extensive ECM remodeling, changes in cell-ECM interactions, and cytoskeletal rearrangement. Matricellular proteins regulate cell-cell and cell-ECM interactions. Evidence in vivo and in vitro indicates that the prototypic matricellular protein, SPARC, inhibits adipogenesis and promotes osteoblastogenesis. Herein we discuss mechanisms underlying the inhibitory effect of SPARC on adipogenesis. SPARC enhances the Wnt/beta-catenin signaling pathway and regulates the expression and posttranslational modification of collagen. SPARC might drive preadipocytes away from the status of growth arrest and therefore prevent terminal differentiation. SPARC could also decrease WAT deposition through its negative e...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2859186</comments>
            <pubDate>Thu, 01 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2859186</guid>        </item>
        <item>
            <title>The many facets of the matricelluar protein periostin during cardiac development, remodeling, and pathophysiology.</title>
            <link>http://www.medworm.com/index.php?rid=2859185&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19798597%26dopt%3DAbstract</link>
            <description>Authors: Norris RA, Moreno-Rodriguez R, Hoffman S, Markwald RR
    Periostin is a member of a growing family of matricellular proteins, defined by their ability to interact with components of the extracellular milieu, and with receptors at the cell surface. Through these interactions, periostin has been shown to play a crucial role as a profibrogenic molecule during tissue morphogenesis. Tissues destined to become fibrous structures are dependent on cooperative interactions between periostin and its binding partners, whereas in its absence, these structures either totally or partially fail to become mature fibrous entities. Within the heart, fibrogenic differentiation is required for normal tissue maturation, remodeling and function, as well as in response to a pathological myocardial insu...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2859185</comments>
            <pubDate>Thu, 01 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2859185</guid>        </item>
        <item>
            <title>The role of SPARC in extracellular matrix assembly.</title>
            <link>http://www.medworm.com/index.php?rid=2859184&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19798598%26dopt%3DAbstract</link>
            <description>Authors: Bradshaw AD
    SPARC is a collagen-binding matricellular protein. Expression of SPARC in adult tissues is frequently associated with excessive deposition of collagen and SPARC-null mice fail to generate a robust fibrotic response to a variety of stimuli. This review summarizes recent advancements in the characterization of the binding of SPARC to collagens and describes the results of studies that implicate a function for SPARC in the regulation of the assembly of basal lamina and fibrillar collagen in the ECM. Potential cellular mechanisms that underlie SPARC activity in ECM deposition are also explored.
    PMID: 19798598 [PubMed - as supplied by publisher] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2859184</comments>
            <pubDate>Thu, 01 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2859184</guid>        </item>
        <item>
            <title>Thrombospondins function as regulators of angiogenesis.</title>
            <link>http://www.medworm.com/index.php?rid=2859183&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19798599%26dopt%3DAbstract</link>
            <description>Authors: Bornstein P
    Thrombospondins (TSPs) -1 and -2 were among the first protein inhibitors of angiogenesis to be identified, a property that was subsequently attributed to the interactions of sequences in their type I repeats with endothelial cell-surface receptors. The interactions of TSPs-1 and -2 with cell-surface receptors, proteases, growth factors, and other bioactive molecules, coupled with the absence of direct structural functions that can be attributed to these matrix proteins, qualify them for inclusion in the category of 'matricellular proteins'. The phenotypes of TSP-1, TSP-2, and double TSP-1/2-null mice confirm the roles that these proteins play in the regulation of angiogenesis, and provide clues to some of the other important functions of these multi-domain proteins...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2859183</comments>
            <pubDate>Thu, 01 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2859183</guid>        </item>
        <item>
            <title>Matricellular proteins: an overview.</title>
            <link>http://www.medworm.com/index.php?rid=2834975&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19779848%26dopt%3DAbstract</link>
            <description>Authors: Bornstein P
    
    PMID: 19779848 [PubMed - as supplied by publisher] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2834975</comments>
            <pubDate>Thu, 24 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2834975</guid>        </item>
        <item>
            <title>Getting to the heart of the matter: CCN2 plays a role in cardiomyocyte hypertrophy.</title>
            <link>http://www.medworm.com/index.php?rid=2735117&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19701807%26dopt%3DAbstract</link>
            <description>Authors: Leask A
    Connective tissue growth factor (CTGF/CCN2) is overexpressed in diabetes. Diabetic rats possess myocardial and cardiomyocyte hypertrophy. In a recent report, Wang and colleagues (Am J Physiol Cell Physiol. 2009 Jul 22. [Epub ahead of print]) show that CCN2 directly mediates cardiomyocyte hypertrophy as well as that induced by high glucose and fatty acid. CCN2 acted via the TrkA receptor. These data are the subject of this commentary, and emphasize that CCN2 may be an excellent target for therapy in diabetes.
    PMID: 19701807 [PubMed - as supplied by publisher] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2735117</comments>
            <pubDate>Sun, 23 Aug 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2735117</guid>        </item>
        <item>
            <title>CCN3 and bone marrow cells.</title>
            <link>http://www.medworm.com/index.php?rid=2640113&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19626464%26dopt%3DAbstract</link>
            <description>Authors: Katsube KI, Ichikawa S, Katsuki Y, Kihara T, Terai M, Lau LF, Tamamura Y, Takeda S, Umezawa A, Sakamoto K, Yamaguchi A
    CCN3 expression was observed in a broad variety of tissues from the early stage of development. However, a kind of loss of function in mice (CCN3 del VWC domain -/-) demonstrated mild abnormality, which indicates that CCN3 may not be critical for the normal embryogenesis as a single gene. The importance of CCN3 in bone marrow environment becomes to be recognized by the studies of hematopoietic stem cells and Chronic Myeloid Leukemia cells. CCN3 expression in bone marrow has been denied by several investigations, but we found CCN3 positive stromal and hematopoietic cells at bone extremities with a new antibody although they are a very few populations. We invest...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2640113</comments>
            <pubDate>Wed, 22 Jul 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2640113</guid>        </item>
        <item>
            <title>CCN3: a key growth regulator in Chronic Myeloid Leukaemia.</title>
            <link>http://www.medworm.com/index.php?rid=2635056&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19623482%26dopt%3DAbstract</link>
            <description>This study shows that CCN3 is an important growth regulator in haematopoiesis, abrogation of CCN3 expression enhances BCR-ABL dependent leukaemogenesis. CCN3 restores growth regulation, regains sensitivity to the induction of apoptosis and enhances imatinib cell kill in CML cells. CCN3 may provide an additional therapeutic strategy in the management of CML.
    PMID: 19623482 [PubMed - as supplied by publisher] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2635056</comments>
            <pubDate>Tue, 21 Jul 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2635056</guid>        </item>
        <item>
            <title>Periostin localizes to cells in normal skin, but is associated with the extracellular matrix during wound repair.</title>
            <link>http://www.medworm.com/index.php?rid=2548451&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19543815%26dopt%3DAbstract</link>
            <description>Authors: Jackson-Boeters L, Wen W, Hamilton DW
    Epidermal tissue repair represents a complex series of temporal and dynamic events resulting in wound closure. Matricellular proteins, not normally expressed in quiescent adult tissues, play a pivotal role in wound repair and associated extracellular matrix remodeling by modulating the adhesion, migration, intracellular signaling, and gene expression of inflammatory cells, pericytes, fibroblasts and keratinocytes. Several matricellular proteins show temporal expression during dermal wound repair, but the expression pattern of the recently identified matricellular protein, periostin, has not yet been characterized. The primary aim of this study was to assess whether periostin protein is present in healthy human skin or in pathological remod...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2548451</comments>
            <pubDate>Thu, 18 Jun 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2548451</guid>        </item>
        <item>
            <title>Yin and Yang: CCN3 inhibits the pro-fibrotic effects of CCN2.</title>
            <link>http://www.medworm.com/index.php?rid=2548452&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19475498%26dopt%3DAbstract</link>
            <description>Authors: Leask A
    Fibrotic disease is a significant cause of mortality. CCN2 (connective tissue growth factor [CTGF]), a member of the CCN family of matricellular proteins, plays a significant role in driving the fibrogenic effects of cytokines such as transforming growth factor beta (TGFbeta). It has been proposed that other members of the CCN family can either promote or antagonize the action of CCN2, depending on the context. A recent elegant study published by Bruce Riser and colleagues (Am J Pathol. 174:1725-34, 2009) illustrates that CCN3 (nov) antagonizes the fibrogenic effects of CCN2. This paper, the subject of this commentary, raises the intriguing possibility that CCN3 may be used as a novel anti-fibrotic therapy.
    PMID: 19475498 [PubMed - as supplied by publisher] (Source...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2548452</comments>
            <pubDate>Thu, 28 May 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2548452</guid>        </item>
        <item>
            <title>Normal growth and development in mice over-expressing the CCN family member WISP3.</title>
            <link>http://www.medworm.com/index.php?rid=2548453&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19401829%26dopt%3DAbstract</link>
            <description>Authors: Nakamura Y, Cui Y, Fernando C, Kutz WE, Warman ML
    Loss-of-function mutations in the gene WISP3 cause the autosomal recessive human skeletal disease Progressive Pseudorheumatoid Dysplasia, whereas mice with knockout mutations of Wisp3 have no phenotype. The lack of a phenotype in the Wisp3 knockout mice has constrained studies of the protein's in vivo function. Over-expression experiments in zebrafish indicated that WISP3 may function as a BMP and Wnt signaling modulator. To determine whether these biologic activities are retained in mice, we created two strains of transgenic mice that over-express WISP3 in a broad array of tissues. Despite strong and persistent protein over-expression, the transgenic mice remained phenotypically indistinguishable from their non-transgenic litt...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2548453</comments>
            <pubDate>Tue, 28 Apr 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2548453</guid>        </item>
        <item>
            <title>Alternative splicing of CCN mRNAs .... it has been upon us.</title>
            <link>http://www.medworm.com/index.php?rid=2548454&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19399643%26dopt%3DAbstract</link>
            <description>Authors: Perbal B
    Variant CCN proteins have been identified over the past decade in several normal and pathological situations. The production of CCN truncated proteins have been reported in the case of CCN2(ctgf), CCN3(nov), CCN4(wisp-1) and CCN6(wisp-3). Furthermore, the natural CCN5 is known to miss the C-terminal domain that is present in all other members of the CCN family of proteins. In spite of compelling evidence that assign important biological activities to these truncated CCN variants, their potential regulatory functions have only recently begun to be widely accepted. The report of CCN1(cyr61) intron 3 retention in breast cancer cells now confirms that, in addition to well documented post-translational processing of full length CCN proteins, alternative splicing is to be r...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2548454</comments>
            <pubDate>Mon, 27 Apr 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2548454</guid>        </item>
        <item>
            <title>What's in an intron? CCN1 mRNA splicing in cancer.</title>
            <link>http://www.medworm.com/index.php?rid=2548455&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19381874%26dopt%3DAbstract</link>
            <description>Authors: Leask A
    The CCN family of matricellular signaling regulators shares a common domain structure. Variants of individual CCN proteins exist, which contain different combinations of these domains. Although mRNA splicing is likely to play a key role on CCN biology, this hypothesis has not been thoroughly tested. In a recent report, Hirschfeld and colleagues (Cancer Res 69:2082-90, 2009), show that CCN1 (cyr61) mRNA is normally present in a form in which intron 3 is retained. In cancers, or upon hypoxia, intron 3 is removed resulting in the appearance of CCN1 protein. The significance of this paper is discussed.
    PMID: 19381874 [PubMed - as supplied by publisher] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2548455</comments>
            <pubDate>Mon, 20 Apr 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2548455</guid>        </item>
        <item>
            <title>A rapid and sensitive method for measuring cell adhesion.</title>
            <link>http://www.medworm.com/index.php?rid=2548456&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19370401%26dopt%3DAbstract</link>
            <description>Authors: Lu W, McCallum L, Irvine AE
    We have adapted the CyQuant(R) assay to provide a simple, rapid, sensitive and highly reproducible method for measuring cell adhesion. The modified CyQuant(R) assay eliminates the requirement for labour intensive fluorescent labelling protocols prior to experimentation and has the sensitivity to measure small numbers (&amp;gt;1000) of adherent cells.
    PMID: 19370401 [PubMed - as supplied by publisher] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2548456</comments>
            <pubDate>Wed, 15 Apr 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2548456</guid>        </item>
        <item>
            <title>Wnt 10b activates the CCN2 promoter in NIH 3T3 fibroblasts through the Smad response element.</title>
            <link>http://www.medworm.com/index.php?rid=2326977&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19353303%26dopt%3DAbstract</link>
            <description>In this report, we map the Wnt10b response element in the CCN2 minimal promoter to the previously identified Smad response element. These results suggest that Wnts may cross-talk with the Smad signaling pathway to induce fibrotic responses in fibroblasts.
    PMID: 19353303 [PubMed - as supplied by publisher] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2326977</comments>
            <pubDate>Wed, 08 Apr 2009 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">2326977</guid>        </item>
        <item>
            <title>Global expression profiling reveals regulation of CTGF/CCN2 during lactogenic differentiation.</title>
            <link>http://www.medworm.com/index.php?rid=2326973&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19353304%26dopt%3DAbstract</link>
            <description>Authors: Wang W, Jose C, Kenney N, Morrison B, Cutler ML
    Mammary epithelial cells go through a series of developmental changes during pregnancy and lactation including proliferation, differentiation, secretion and apoptosis. HC11 mouse mammary epithelial cells, which undergo lactogen-induced differentiation in cell culture, were used to follow the changes in gene expression during this process. The expression profiles of over 20,000 genes were compared in HC11 cells undergoing lactogenic differentiation to non-differentiated cells using DNA microarray analysis. Greater than two fold changes were detected in 998 genes in the differentiated cells versus growth controls. Several genes including CTGF/CCN2 exhibited greater than five-fold increase. Validation of the gene expression pattern ...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2326973</comments>
            <pubDate>Wed, 08 Apr 2009 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">2326973</guid>        </item>
        <item>
            <title>Expression of CCN family of genes in human skin in vivo and alterations by solar-simulated ultraviolet irradiation.</title>
            <link>http://www.medworm.com/index.php?rid=2295464&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19319669%26dopt%3DAbstract</link>
            <description>Authors: Quan T, Shin S, Qin Z, Fisher GJ
    The CCN family of proteins is involved in diverse biological functions such as cell growth, adhesion, migration, angiogenesis, and regulation of extracellular matrix. We have investigated expression of CCN family genes and alternations induced by solar-simulated ultraviolet irradiation in human skin in vivo. Transcripts of all six CCN genes were expressed in human skin in vivo. CCN5 was most abundantly expressed followed by CCN2&amp;gt;CCN3&amp;gt;CCN1&amp;gt;CCN4&amp;gt;CCN6. Solar-simulated ultraviolet irradiation increased mRNA expression of CCN1 and CCN2. In contrast, mRNA levels of CCN3, CCN4, CCN5, and CCN6, were reduced. Knowledge gained from this study provides the foundation to explore the functional roles of CCN gene products in cutaneous biology and...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2295464</comments>
            <pubDate>Wed, 25 Mar 2009 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">2295464</guid>        </item>
        <item>
            <title>Strategies for blocking the fibrogenic actions of connective tissue growth factor (CCN2): From pharmacological inhibition in vitro to targeted siRNA therapy in vivo.</title>
            <link>http://www.medworm.com/index.php?rid=2283521&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19294531%26dopt%3DAbstract</link>
            <description>Authors: Brigstock DR
    Connective tissue growth factor (CCN2) is a major pro-fibrotic factor that frequently acts downstream of transforming growth factor beta (TGF-beta)-mediated fibrogenic pathways. Much of our knowledge of CCN2 in fibrosis has come from studies in which its production or activity have been experimentally attenuated. These studies, performed both in vitro and in animal models, have demonstrated the utility of pharmacological inhibitors (e.g. tumor necrosis factor alpha (TNF-alpha), prostaglandins, peroxisome proliferator-activated receptor-gamma (PPAR-gamma) agonists, statins, kinase inhibitors), neutralizing antibodies, antisense oligonucleotides, or small interfering RNA (siRNA) to probe the role of CCN2 in fibrogenic pathways. These investigations have allowed the ...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2283521</comments>
            <pubDate>Wed, 18 Mar 2009 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">2283521</guid>        </item>
        <item>
            <title>Death of a tumor: targeting CCN in pancreatic cancer.</title>
            <link>http://www.medworm.com/index.php?rid=2258266&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19267221%26dopt%3DAbstract</link>
            <description>This report briefly summarizes these findings.
    PMID: 19267221 [PubMed - as supplied by publisher] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2258266</comments>
            <pubDate>Sun, 08 Mar 2009 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2258266</guid>        </item>
        <item>
            <title>Trial by CCN2: a standardized test for fibroproliferative disease?</title>
            <link>http://www.medworm.com/index.php?rid=2242337&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19266315%26dopt%3DAbstract</link>
            <description>Authors: Leask A
    A major issue concerning clinical trials is the availability of standardized assays to evaluate drug efficacy. Ideally, such assays should test the effect of a putative drug on the expression of a biomarker in biological fluids. In a recent study by Kuiper et al. (PLOS One, 3(7): e2675). The relative levels of vascular endothelial growth factor (VEGF) and CCN2 (connective tissue growth factor [CTGF]) were examined in proliferative diabetic retinopathy (PDR). This paper is the subject of this commentary.
    PMID: 19266315 [PubMed - as supplied by publisher] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2242337</comments>
            <pubDate>Sat, 07 Mar 2009 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2242337</guid>        </item>
        <item>
            <title>Connective tissue growth factor(CCN2), a pathogenic factor in diabetic nephropathy. What does it do? How does it do it?</title>
            <link>http://www.medworm.com/index.php?rid=2188575&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19214781%26dopt%3DAbstract</link>
            <description>Authors: Mason RM
    Connective tissue growth factor (CTGF/CCN2) is a member of the CCN family of matricellular proteins. Its expression is induced by a number of factors including TGF-beta. It has been associated with fibrosis in various tissues including the kidney. Diabetic nephropathy (DN) develops in about 30% of patients with diabetes and is characterized by thickening of renal basement membranes, fibrosis in the glomerulus (glomerulosclerosis), tubular atrophy and interstitial fibrosis, all of which compromise kidney function. This review examines changes in CTGF expression in the kidney in DN, the effects they have on glomerular mesangial and podocyte cells and the tubulointerstitium, and how these contribute to driving fibrotic changes in the disease. CTGF can bind to several oth...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2188575</comments>
            <pubDate>Sat, 14 Feb 2009 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2188575</guid>        </item>
        <item>
            <title>Connective tissue growth factor (CTGF, CCN2) gene regulation: a potent clinical bio-marker of fibroproliferative disease?</title>
            <link>http://www.medworm.com/index.php?rid=2122620&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19156539%26dopt%3DAbstract</link>
            <description>Authors: Leask A, Parapuram SK, Shi-Wen X, Abraham DJ
    The CCN (cyr61, ctgf, nov) family of modular proteins regulate diverse biological affects including cell adhesion, matrix production, tissue remodelling, proliferation and differentiation. Recent targeted gene disruption studies have demonstrated the CCN family to be developmentally essential for chondrogenesis, osteogenesis and angiogenesis. CCN2 is induced by agents such as angiotensin II, endothelin-1, glucocorticoids, HGF, TGFbeta, and VEGF, and by hypoxia and biomechanical and shear stress. Dysregulated expression of CCN2 has also been widely documented in many fibroproliferative diseases. This mini-review will focus on CCN2, and the recent progress in understanding CCN2 gene regulation in health and disease. That CCN2 should b...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2122620</comments>
            <pubDate>Wed, 21 Jan 2009 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2122620</guid>        </item>
        <item>
            <title>Report on the fifth international workshop on the CCN family of genes.</title>
            <link>http://www.medworm.com/index.php?rid=2122619&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19156540%26dopt%3DAbstract</link>
            <description>Authors: Irvine AE, Perbal B, Yeger H
    The Fifth International Workshop on the CCN Family of Genes was held in Toronto October 18-22, 2008. This bi-annual workshop provides a unique opportunity for the presentation and discussion of cutting edge research in the CCN field. The CCN family members have emerged as extracellular matrix associated proteins which play a crucial role in cardiovascular and skeletal development, fibrosis and cancer. Significant progress has been made in the development of model systems to tease apart the CCN signalling pathways in these systems. Results presented at the conference suggest that targeting these pathways now shows real promise as a therapeutic strategy.
    PMID: 19156540 [PubMed - as supplied by publisher] (Source: Journal of Cell Communication and...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2122619</comments>
            <pubDate>Wed, 21 Jan 2009 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2122619</guid>        </item>
        <item>
            <title>Fifth International Workshop on the CCN Family of Genes: Abstracts and Posters October 18-22, 2008.</title>
            <link>http://www.medworm.com/index.php?rid=2117050&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19152120%26dopt%3DAbstract</link>
            <description>Authors: 
    
    PMID: 19152120 [PubMed - as supplied by publisher] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2117050</comments>
            <pubDate>Mon, 19 Jan 2009 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2117050</guid>        </item>
        <item>
            <title>Using Caenorhabditis elegans as a model organism for evaluating extracellular signal-regulated kinase docking domain inhibitors.</title>
            <link>http://www.medworm.com/index.php?rid=2062579&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19105050%26dopt%3DAbstract</link>
            <description>Authors: Chen F, Mackerell AD, Luo Y, Shapiro P
    We have recently identified several novel ATP-independent inhibitors that target the extracellular signal-regulated kinase-2 (ERK2) protein and inhibit substrate phosphorylation. To further characterize these compounds, we describe the use of C. elegans as a model organism. C. elegans is recognized as a versatile and cost effective model for use in drug development. These studies take advantage of the well characterized process of vulva development and egg laying, which requires MPK-1, the homolog to human ERK2. It is shown that treatment of C. elegans eggs or larvae prior to vulva formation with a previously identified lead compound (76) caused up to 50% reduction in the number of eggs produced from the adult worm. In contrast, compound ...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2062579</comments>
            <pubDate>Tue, 23 Dec 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2062579</guid>        </item>
        <item>
            <title>Matricellular CCN proteins.</title>
            <link>http://www.medworm.com/index.php?rid=2028942&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19067237%26dopt%3DAbstract</link>
            <description>Authors: Perbal B
    We kindly invite you to consider the Journal of Cell Communication and Signaling (JCCS) as a media for publication of your research and participate in promoting JCCS as an important platform for disseminating new results in the fields of cell signaling.
    PMID: 19067237 [PubMed - as supplied by publisher] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2028942</comments>
            <pubDate>Tue, 09 Dec 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2028942</guid>        </item>
        <item>
            <title>Expression and function of alphabeta1 integrins in pancretic beta (INS-1) cells.</title>
            <link>http://www.medworm.com/index.php?rid=1981852&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19023675%26dopt%3DAbstract</link>
            <description>Authors: Krishnamurthy M, Li J, Al-Masri M, Wang R
    Integrin-extracellular matrix interactions are important determinants of beta cell behaviours. The beta1 integrin is a well-known regulator of beta cell activities; however, little is known of its associated alpha subunits. In the present study, alphabeta1 integrin expression was examined in the rat insulinoma cell line (INS-1) to identify their role in beta cell survival and function. Seven alpha subunits associated with beta1 integrin were identified, including alpha1-6 and alphaV. Among these heterodimers, alpha3beta1 was most highly expressed. Common ligands for the alpha3beta1 integrin, including fibronectin, laminin, collagen I and collagen IV were tested to identify the most suitable matrix for INS-1 cell proliferation and funct...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1981852</comments>
            <pubDate>Fri, 21 Nov 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1981852</guid>        </item>
        <item>
            <title>The Notochord, Notochordal cell and CTGF/CCN-2: ongoing activity from development through maturation.</title>
            <link>http://www.medworm.com/index.php?rid=1956093&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19003520%26dopt%3DAbstract</link>
            <description>Authors: Erwin WM
    The growth regulating factor CTGF/CCN-2 is an integral factor in growth and development, connective tissue maintenance, wound repair and cell cycle regulation. It has recently been reported that CTGF/CCN-2 is involved in very early development having been detected in early notochord formation in zebrafish using CTGF/CCN-2 promoter-driven green fluorescent protein (GFP) plasmids. In these studies fluorescence was detected early in the developing embryos, a finding of considerable significance in that CTGF/CCN-2 deficient mutant mice die early after birth due to severe cartilage and skeletal dysplasia and respiratory failure. Such findings confirm the importance of CTGF/CCN-2 in development and of the necessary and sufficient role of this molecule in formation of the sk...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1956093</comments>
            <pubDate>Wed, 12 Nov 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1956093</guid>        </item>
        <item>
            <title>The skinny on CCN2.</title>
            <link>http://www.medworm.com/index.php?rid=1953170&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18991022%26dopt%3DAbstract</link>
            <description>Authors: Leask A
    The CCN family of matricellular proteins directly or indirectly affects development and differentiation. A recent report written by Tan and colleagues (Am J Physiol Cell Physiol 295: C740-C751 2008) shows that CCN2 inhibits adipocyte differentiation. This commentary summarizes these observations.
    PMID: 18991022 [PubMed - as supplied by publisher] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1953170</comments>
            <pubDate>Sat, 08 Nov 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1953170</guid>        </item>
        <item>
            <title>Regulation of CCN2 mRNA expression and promoter activity in activated hepatic stellate cells.</title>
            <link>http://www.medworm.com/index.php?rid=1803441&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18798011%26dopt%3DAbstract</link>
            <description>Authors: Leask A, Chen S, Pala D, Brigstock DR
    The matricellular protein connective tissue growth factor (CCN2) is considered a faithful marker of fibroblast activation in wound healing and in fibrosis. CCN2 is induced during activation of hepatic stellate cells (HSC). Here, we investigate the molecular basis of CCN2 gene expression in HSC. Fluoroscence activated cell sorting was used to investigate CCN2 expression in HSC in vivo in mice treated with CCl(4). CCN2 and TGF-beta mRNA expression were assessed by polymerase chain reaction as a function of culture-induced activation of HSC. CCN2 promoter/reporter constructs were used to map cis-acting elements required for basal and TGFbeta-induced CCN2 promoter activity. Real-time polymerase chain reaction analysis was used to further clari...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1803441</comments>
            <pubDate>Wed, 17 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1803441</guid>        </item>
        <item>
            <title>CCN3: Doctor Jekyll and Mister Hyde.</title>
            <link>http://www.medworm.com/index.php?rid=1786576&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18784988%26dopt%3DAbstract</link>
            <description>Authors: Perbal B
    CCN proteins are key regulators of signaling pathways that are essential for the control of normal life, from birth to death. As such, they make use of their unique mosaic structure to interact with several other regulatory proteins and ligands that control the fate of living cells. The various functions attributed to the CCN proteins may sometimes appear contradictory, but this situation reflects the complexity of the multimolecular scaffolds in which CCN proteins are engaged and the critical impact of the microenvironment that dictates the bioavailability of the elementary building blocks. CCN3 is one of the best examples of a CCN protein showing biological properties which may at first glance appear opposite or contradictory. Indeed, CCN3 acts both as a tumor suppr...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1786576</comments>
            <pubDate>Fri, 12 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1786576</guid>        </item>
        <item>
            <title>CCN2 YAPs at cancer.</title>
            <link>http://www.medworm.com/index.php?rid=1760781&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18766468%26dopt%3DAbstract</link>
            <description>This report briefly summarizes these findings.
    PMID: 18766468 [PubMed - as supplied by publisher] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1760781</comments>
            <pubDate>Wed, 03 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1760781</guid>        </item>
        <item>
            <title>Enzymes used in molecular biology: a useful guide.</title>
            <link>http://www.medworm.com/index.php?rid=1760780&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18766469%26dopt%3DAbstract</link>
            <description>Authors: Ritti&amp;#xE9; L, Perbal B
    Since molecular cloning has become routine laboratory technique, manufacturers offer countless sources of enzymes to generate and manipulate nucleic acids. Thus, selecting the appropriate enzyme for a specific task may seem difficult to the novice. This review aims at providing the readers with some cues for understanding the function and specificities of the different sources of polymerases, ligases, nucleases, phosphatases, methylases, and topoisomerases used for molecular cloning. We provide a description of the most commonly used enzymes of each group, and explain their properties and mechanism of action. By pointing out key requirements for each enzymatic activity and clarifying their limitations, we aim at guiding the reader in selecting appropria...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1760780</comments>
            <pubDate>Wed, 03 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1760780</guid>        </item>
        <item>
            <title>The Starbuck stops here: it's a Smad world.</title>
            <link>http://www.medworm.com/index.php?rid=1649927&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18649015%26dopt%3DAbstract</link>
            <description>Authors: Leask A
    A recent study by Gressner and colleagues suggested caffeine may block CCN2 expression in hepatic cells. This commentary briefly summarizes these observations.
    PMID: 18649015 [PubMed - as supplied by publisher] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1649927</comments>
            <pubDate>Wed, 23 Jul 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1649927</guid>        </item>
        <item>
            <title>Ceramide inhibits CCN2 expression in fibroblasts.</title>
            <link>http://www.medworm.com/index.php?rid=1649926&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18649016%26dopt%3DAbstract</link>
            <description>In this report, we show that C2 ceramide reduced the ability of TGFbeta to induce CCN2 protein, mRNA and promoter activity in fibroblasts. C2 ceramide reduced the ability of TGFbeta to induce the generic Smad responsive promoter/reporter construct SBE-luciferase. These results suggest that C2 ceramide reduces the action of TGFbeta in fibroblasts via Smad antagonism.
    PMID: 18649016 [PubMed - as supplied by publisher] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1649926</comments>
            <pubDate>Wed, 23 Jul 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1649926</guid>        </item>
        <item>
            <title>Functional role of periostin in development and wound repair: implications for connective tissue disease.</title>
            <link>http://www.medworm.com/index.php?rid=1643271&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18642132%26dopt%3DAbstract</link>
            <description>Authors: Hamilton DW
    Integrity of the extracellular matrix (ECM) is essential for maintaining the normal structure and function of connective tissues. ECM is secreted locally by cells and organized into a complex meshwork providing physical support to cells, tissues, and organs. Initially thought to act only as a scaffold, the ECM is now known to provide a myriad of signals to cells regulating all aspects of their phenotype from morphology to differentiation. Matricellular proteins are a class of ECM related molecules defined through their ability to modulate cell-matrix interactions. Matricellular proteins are expressed at high levels during development, but typically only appear in postnatal tissue in wound repair or disease, where their levels increase substantially. Members of the ...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1643271</comments>
            <pubDate>Sun, 20 Jul 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1643271</guid>        </item>
        <item>
            <title>The CCN family of genes: a perspective on CCN biology and therapeutic potential.</title>
            <link>http://www.medworm.com/index.php?rid=1567660&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18568428%26dopt%3DAbstract</link>
            <description>Authors: Yeger H, Perbal B
    The CCN family of genes currently comprises six secreted proteins (designated CCN1-6 after Cyr61/CCN1; ctgf/CCN2; Nov/CCN3; WISP1/CCN4; WISP2/CCN5, WISP3/CCN6) with a similar mosaic primary structure. It is now well accepted that CCN proteins are not growth factors but matricellular proteins that modify signaling of other molecules, in particular those associated with the extracellular matrix. CCN proteins are involved in mitosis, adhesion, apoptosis, extracellular matrix production, growth arrest and migration of multiple cell types. Since their first identification as matricellular factors, the CCN proteins now figure prominently in a variety of major diseases and are now considered valid candidates for therapeutic targeting. Dissection of the molecular mec...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1567660</comments>
            <pubDate>Sat, 21 Jun 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1567660</guid>        </item>
        <item>
            <title>Effect of nitric oxide donor and gamma irradiation on modifications of ERK and JNK in murine peritoneal macrophages.</title>
            <link>http://www.medworm.com/index.php?rid=1567662&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18523870%26dopt%3DAbstract</link>
            <description>This study indicates that ERK and JNK may be under regulation by different type of modifications in macrophages.
    PMID: 18523870 [PubMed - as supplied by publisher] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1567662</comments>
            <pubDate>Wed, 04 Jun 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1567662</guid>        </item>
        <item>
            <title>CCN3-mutant mice are distinct from CCN3-null mice.</title>
            <link>http://www.medworm.com/index.php?rid=1567661&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18523871%26dopt%3DAbstract</link>
            <description>Authors: Perbal B
    A recent manuscript reported phenotypic alterations associated to the expression of a CCN3 protein deleted for the Von Willebrand type C repeat that is common to the various members of the CCN family of proteins. In this comment, the biological significance of these alterations is briefly discussed.
    PMID: 18523871 [PubMed - as supplied by publisher] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1567661</comments>
            <pubDate>Wed, 04 Jun 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1567661</guid>        </item>
        <item>
            <title>CCN3: A novel function in vivo.</title>
            <link>http://www.medworm.com/index.php?rid=1567663&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18506600%26dopt%3DAbstract</link>
            <description>Authors: Leask A
    
    PMID: 18506600 [PubMed - as supplied by publisher] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1567663</comments>
            <pubDate>Wed, 28 May 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1567663</guid>        </item>
        <item>
            <title>Analysis of CCN2 promoter activity in PANC-1 cells: regulation by ras/MEK/ERK.</title>
            <link>http://www.medworm.com/index.php?rid=1567676&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18481199%26dopt%3DAbstract</link>
            <description>Authors: Pickles M, Leask A
    Connective tissue growth factor (CTGF, CCN2) is overexpressed in pancreatic cancer. We mapped the minimal CCN2 promoter active in PANC-1 cells, a human pancreatic cancer cell line. Within this region, Sp1, BCE-1 and Ets elements were important for the activity of the CCN2 promoter. Constitutive hyperactivated ras is a hallmark of cancers, including that of the pancreas. Treatment of PANC-1 cells with the MEK inhibitor U0126 or the Sp1 inhibitor mithramycin reduced CCN2 mRNA and promoter activity. Mutation of the BCE-1, but not Sp1 or Ets, site abolished the responsiveness of the CCN2 promoter to U0126. Overexpressing constitutively active MEK1 or ras activated CCN2 promoter activity. Thus CCN2 is likely to act downstream of ras in PANC-1 cells. CCN2 is overe...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1567676</comments>
            <pubDate>Sat, 01 Sep 2007 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1567676</guid>        </item>
        <item>
            <title>Domain-specific CCN3 antibodies as unique tools for structural and functional studies.</title>
            <link>http://www.medworm.com/index.php?rid=1567675&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18481200%26dopt%3DAbstract</link>
            <description>Authors: Lazar N, Manara C, Navarro S, Bleau AM, Llombart-Bosch A, Scotlandi K, Planque N, Perbal B
    CCN3 is a member of the CCN family of cell growth and differentiation regulators that play key roles during embryonic development, and are associated with severe human pathologies. The level of CCN genes' expression is of prognostic value in several types of tumors. In the present manuscript, we report the isolation and characterization of a new set of antibodies targeted against each individual module of the human CCN3 protein. The need for module-specific antibodies stemmed from recent reports indicating that the expression of truncated CCN variant proteins was associated with development of cancers. Each of the four CCN3 modules were expressed as GST fusion proteins and used for rabbi...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1567675</comments>
            <pubDate>Sat, 01 Sep 2007 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1567675</guid>        </item>
        <item>
            <title>Specific inhibitor of MEK-mediated cross-talk between ERK and p38 MAPK during differentiation of human osteosarcoma cells.</title>
            <link>http://www.medworm.com/index.php?rid=1567674&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18481201%26dopt%3DAbstract</link>
            <description>Authors: Shimo T, Matsumura S, Ibaragi S, Isowa S, Kishimoto K, Mese H, Nishiyama A, Sasaki A
    Osteosarcoma is the most common primary malignant bone tumor, accounting for approximately 20% of all primary sarcomas in bone. Although treatment modalities have been improved over the past decades, it is still a tumor with a high mortality rate in children and young adults. Based on histological considerations, osteosarcoma arises from impaired differentiation of these immature cells into more mature types and that correction of this impairment may reduce malignancy and increase the efficiency of chemotherapy. The purpose of this study was to determine the effect of specific inhibitors of MAPK extracellular signaling-regulated kinase (ERK) kinase (MEK) and p38 on the differentiation of human...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1567674</comments>
            <pubDate>Sat, 01 Sep 2007 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1567674</guid>        </item>
        <item>
            <title>Role of the PI3-kinase/mTor pathway in the regulation of the stearoyl CoA desaturase (SCD1) gene expression by insulin in liver.</title>
            <link>http://www.medworm.com/index.php?rid=1567673&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18481202%26dopt%3DAbstract</link>
            <description>Authors: Mauvoisin D, Rocque G, Arfa O, Radenne A, Boissier P, Mounier C
    The stearoyl-CoA desaturase 1 (SCD1) catalyzes the synthesis of monounsaturated fatty acids. This enzyme is a critical control point regulating hepatic lipogenesis and lipid oxidation. Therefore SCD1 may be a potential therapeutic target in the treatment of obesity and metabolic syndrome. Regulation of SCD1 expression occurs primarily at the level of transcription. In the present study, we characterized the insulin response elements (IREs) and the insulin signaling pathway mediating the regulation of SCD1 gene transcription in liver. In chicken embryo hepatocytes (CEH) and HepG2 cells, insulin stimulates SCD1 promoter activity by 2.5 folds. This activation is mediated by two different IREs on the chicken promoter,...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1567673</comments>
            <pubDate>Sat, 01 Sep 2007 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1567673</guid>        </item>
        <item>
            <title>CCN5 expression in mammals : I. Embryonic and fetal tissues of mouse and human.</title>
            <link>http://www.medworm.com/index.php?rid=1567672&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18481203%26dopt%3DAbstract</link>
            <description>Authors: Jones JA, Gray MR, Oliveira BE, Koch M, Castellot JJ
    The six proteins of the CCN family have important roles in development, angiogenesis, cell motility, proliferation, and other fundamental cell processes. To date, CCN5 distribution in developing rodents and humans has not been mapped comprehensively. CCN5 strongly inhibits adult smooth muscle cell proliferation and motility. Its anti-proliferative action predicts that CCN5 would not be present in developing tissues until the proliferation phase of tissue morphogenesis is complete. However, estrogen induces CCN5 expression in epithelial and smooth muscle cells, suggesting that CCN5 might be widely expressed in embryonic tissues exposed to high levels of estrogen. 9-16 day murine embryos and fetuses and 3-7 month human fetal t...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1567672</comments>
            <pubDate>Sat, 01 Sep 2007 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1567672</guid>        </item>
        <item>
            <title>CCN5 Expression in mammals. II. Adult rodent tissues.</title>
            <link>http://www.medworm.com/index.php?rid=1567671&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18481204%26dopt%3DAbstract</link>
            <description>Authors: Gray MR, Malmquist JA, Sullivan M, Blea M, Castellot JJ
    CCN5 is a secreted heparin- and estrogen-regulated matricellular protein that inhibits vertebrate smooth muscle cell proliferation and motility. CCN5 is expressed throughout murine embryonic development in most organs and tissues. However, after embryonic development is complete, we hypothesized that CCN5 distribution would be largely restricted to small set of tissues, including smooth muscle cells of the arteries, uterus, airway, and digestive tract. Because CCN5 inhibits proliferation of smooth muscle cells in vitro, it might function to prevent excessive growth in vivo. In contrast, another member of the CCN family, CCN2, promotes smooth muscle cell proliferation in vitro, and thus it was expected that its expression ...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1567671</comments>
            <pubDate>Sat, 01 Sep 2007 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1567671</guid>        </item>
        <item>
            <title>CCN proteins, microenvironment, communication and signaling: why did we need a new journal?</title>
            <link>http://www.medworm.com/index.php?rid=1567670&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18481205%26dopt%3DAbstract</link>
            <description>Authors: Perbal A, Perbal B
    
    PMID: 18481205 [PubMed - as supplied by publisher] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
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            <pubDate>Fri, 01 Jun 2007 04:00:00 +0100</pubDate>
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            <title>Interaction of TACC proteins with the FHL family: implications for ERK signaling.</title>
            <link>http://www.medworm.com/index.php?rid=1567669&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18481206%26dopt%3DAbstract</link>
            <description>Authors: Lauffart B, Sondarva GV, Gangisetty O, Cincotta M, Still IH
    The Transforming acidic coiled coil (TACC) proteins play a conserved role in normal development and tumorigenesis through interactions with multiple complexes involved in transcription, translation, and centrosomal dynamics. However, despite significant work on the function of TACC3 in the control of centrosomal mechanics, relatively little functional data is known about the family's founding member, TACC1. From a continued analysis of clones isolated by an unbiased yeast two-hybrid assay, we now show direct physical interactions between the TACC1 and the FHL (Four and a Half LIM-only) family of proteins. The authenticity of these interactions was validated both in vitro and in cellular systems. The FHLs exhibit diver...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
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            <pubDate>Fri, 01 Jun 2007 04:00:00 +0100</pubDate>
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            <title>The 5' untranslated regions (UTRs) of CCN1, CCN2, and CCN4 exhibit cryptic promoter activity.</title>
            <link>http://www.medworm.com/index.php?rid=1567668&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18481207%26dopt%3DAbstract</link>
            <description>Authors: Huang BL, Dornbach LM, Lyons KM
    CCNs are structurally related matricellular proteins that are highly expressed in many embryonic and adult tissues, including the skeletal system and tumors, where canonical cap-dependent translation is suppressed under hypoxic environments. CCNs are encoded by mRNAs containing long G/C rich 5'-untranslated regions (5'-UTRs). Given that they are expressed under conditions of cellular stress, it has been suggested that the long G/C-rich regions contain internal ribosomal entry sites (IRES) that allow these mRNAS to be translated under conditions where cap-dependent translation is suppressed. Previously published work supported this possibility. However, recent studies have shown that a number of previously reported cellular IRES elements do not i...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
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            <pubDate>Fri, 01 Jun 2007 04:00:00 +0100</pubDate>
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            <title>Differential role of reactive oxygen species in the activation of mitogen-activated protein kinases and Akt by key receptors on B-lymphocytes: CD40, the B cell antigen receptor, and CXCR4.</title>
            <link>http://www.medworm.com/index.php?rid=1567667&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18481208%26dopt%3DAbstract</link>
            <description>CONCLUSION: The differential requirement for ROS in the activation of ERK, JNK, p38, and Akt by the BCR, CD40, and CXCR4 likely reflects the multiplicity of upstream activators for each of these kinases, only some of which may be regulated in a redox-dependent manner. These findings support the idea that ROS are important second messengers in B cells and suggest that oxidants or anti-oxidants could be used to modulate B cell activation.
    PMID: 18481208 [PubMed - in process] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
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            <pubDate>Fri, 01 Jun 2007 04:00:00 +0100</pubDate>
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        <item>
            <title>CCN2 (Connective Tissue Growth Factor) is essential for extracellular matrix production and integrin signaling in chondrocytes.</title>
            <link>http://www.medworm.com/index.php?rid=1567666&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18481209%26dopt%3DAbstract</link>
            <description>Authors: Nishida T, Kawaki H, Baxter RM, Deyoung RA, Takigawa M, Lyons KM
    The matricellular protein CCN2 (Connective Tissue Growth Factor; CTGF) is an essential mediator of ECM composition, as revealed through analysis of Ccn2 deficient mice. These die at birth due to complications arising from impaired endochondral ossification. However, the mechanism(s) by which CCN2 mediates its effects in cartilage are unclear. We investigated these mechanisms using Ccn2 ( -/- ) chondrocytes. Expression of type II collagen and aggrecan were decreased in Ccn2 (-/-) chondrocytes, confirming a defect in ECM production. Ccn2 ( -/- ) chondrocytes also exhibited impaired DNA synthesis and reduced adhesion to fibronectin. This latter defect is associated with decreased expression of alpha5 integrin. Moreo...</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
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            <pubDate>Fri, 01 Jun 2007 04:00:00 +0100</pubDate>
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            <title>Report on the fourth international workshop on the CCN family of genes.</title>
            <link>http://www.medworm.com/index.php?rid=1567665&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18481210%26dopt%3DAbstract</link>
            <description>Authors: Kubota S, Yeger H, Perbal B, Takigawa M
    
    PMID: 18481210 [PubMed - in process] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1567665</comments>
            <pubDate>Fri, 01 Jun 2007 04:00:00 +0100</pubDate>
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        <item>
            <title>Fourth international workshop on the CCN family of genes: Abstracts and posters October 18-21, 2006.</title>
            <link>http://www.medworm.com/index.php?rid=1567664&amp;cid=s_37234_67_f&amp;fid=37234&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18481211%26dopt%3DAbstract</link>
            <description>Authors: 
    
    PMID: 18481211 [PubMed - in process] (Source: Journal of Cell Communication and Signaling)</description>
            <author>Journal of Cell Communication and Signaling</author>
            <type>journals</type>
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            <pubDate>Fri, 01 Jun 2007 04:00:00 +0100</pubDate>
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