Involvement of oxidative stress-AMPK-Cx43-NLRP3 pathway in extracellular matrix remodeling of gastric smooth muscle cells in rats with diabetic gastroparesis
This study aimed to investigate the changes in oxidative stress, adenosine monophosphate-activated protein kinase (AMPK), connexin43 (Cx43), nucleotide-binding oligomerization domain-like receptor protein 3 (NLRP3) expression, and extracellular matrix (ECM) in the gastric smooth muscle tissues of rats with diabetic gastroparesis (DGP) and high glucose-cultured gastric smooth muscle cells, determine the existence of oxidative stress-AMPK-Cx43-NLRP3 pathway under high glucose condition, and the involvement of this pathway in ECM remodeling in DGP rats. The results showed that with increasing duration of diabetes, oxidation s...
Source: Cell Stress and Chaperones - April 23, 2024 Category: Cytology Authors: Baihui Song Gaoyuan Zhang Yitegele Bao Mohan Zhang Source Type: research

Involvement of oxidative stress-AMPK-Cx43-NLRP3 pathway in extracellular matrix remodeling of gastric smooth muscle cells in rats with diabetic gastroparesis
This study aimed to investigate the changes in oxidative stress, adenosine monophosphate-activated protein kinase (AMPK), connexin43 (Cx43), nucleotide-binding oligomerization domain-like receptor protein 3 (NLRP3) expression, and extracellular matrix (ECM) in the gastric smooth muscle tissues of rats with diabetic gastroparesis (DGP) and high glucose-cultured gastric smooth muscle cells, determine the existence of oxidative stress-AMPK-Cx43-NLRP3 pathway under high glucose condition, and the involvement of this pathway in ECM remodeling in DGP rats. The results showed that with increasing duration of diabetes, oxidation s...
Source: Cell Stress and Chaperones - April 23, 2024 Category: Cytology Authors: Baihui Song Gaoyuan Zhang Yitegele Bao Mohan Zhang Source Type: research

Hsf1 and Hsf2 in normal, healthy human tissues: Immunohistochemistry provokes new questions
Cell Stress Chaperones. 2024 Apr 17:S1355-8145(24)00066-X. doi: 10.1016/j.cstres.2024.04.004. Online ahead of print.ABSTRACTThe heat shock transcription factors Hsf1 and Hsf2 have been studied since many years mainly in the context of stress response and in malignant cells. Their physiological function in non-malignant human cells under non-stress conditions is still largely unknown. To approach this important issue, Joutsen et al. present immunohistochemical staining data on Hsf1 and Hsf2 in 80 non-pathological human tissue samples. The wealth of these data elicits many interesting questions that will spur many future res...
Source: Cell Stress and Chaperones - April 19, 2024 Category: Cytology Authors: Matthias P Mayer Source Type: research

Membraneless and membrane-bound organelles in an anhydrobiotic cell line are protected from desiccation-induced damage
This study offers several exciting avenues for future studies in the animal model and Pv11 cell line that will further our understanding of anhydrobiosis and may lead to advancements in storing sensitive biologics at ambient temperatures for months or years.PMID:38608858 | DOI:10.1016/j.cstres.2024.04.002 (Source: Cell Stress and Chaperones)
Source: Cell Stress and Chaperones - April 12, 2024 Category: Cytology Authors: Clinton J Belott Oleg A Gusev Takahiro Kikawada Michael A Menze Source Type: research

Loss of the histone chaperone UNC-85/ASF1 inhibits the epigenome-mediated longevity and modulates the activity of one-carbon metabolism
Cell Stress Chaperones. 2024 Apr 10;29(3):392-403. doi: 10.1016/j.cstres.2024.04.003. Online ahead of print.ABSTRACTHistone H3/H4 chaperone anti-silencing function 1 (ASF1) is a conserved factor mediating nucleosomal assembly and disassembly, playing crucial roles in processes such as replication, transcription, and DNA repair. Nevertheless, its involvement in aging has remained unclear. Here, we utilized the model organism Caenorhabditis elegans to demonstrate that the loss of UNC-85, the homolog of ASF1, leads to a shortened lifespan in a multicellular organism. Furthermore, we show that UNC-85 is required for epigenome-...
Source: Cell Stress and Chaperones - April 12, 2024 Category: Cytology Authors: Bideep Shrestha Anni I Nieminen Olli Matilainen Source Type: research

Membraneless and Membrane-bound Organelles in an Anhydrobiotic Cell Line are Protected from Desiccation-induced Damage
This study offers several exciting avenues for future studies in the animal model and Pv11 cell line that will further our understanding of anhydrobiosis and may lead to advancements in storing sensitive biologics at ambient temperatures for months or years.PMID:38608858 | DOI:10.1016/j.cstres.2024.04.002 (Source: Cell Stress and Chaperones)
Source: Cell Stress and Chaperones - April 12, 2024 Category: Cytology Authors: Clinton J Belott Oleg A Gusev Takahiro Kikawada Michael A Menze Source Type: research

Loss of the histone chaperone UNC-85/ASF1 inhibits the epigenome-mediated longevity and modulates the activity of one-carbon metabolism
Cell Stress Chaperones. 2024 Apr 10;29(3):392-403. doi: 10.1016/j.cstres.2024.04.003. Online ahead of print.ABSTRACTHistone H3/H4 chaperone anti-silencing function 1 (ASF1) is a conserved factor mediating nucleosomal assembly and disassembly, playing crucial roles in processes such as replication, transcription, and DNA repair. Nevertheless, its involvement in aging has remained unclear. Here, we utilized the model organism Caenorhabditis elegans to demonstrate that the loss of UNC-85, the homolog of ASF1, leads to a shortened lifespan in a multicellular organism. Furthermore, we show that UNC-85 is required for epigenome-...
Source: Cell Stress and Chaperones - April 12, 2024 Category: Cytology Authors: Bideep Shrestha Anni I Nieminen Olli Matilainen Source Type: research

Membraneless and Membrane-bound Organelles in an Anhydrobiotic Cell Line are Protected from Desiccation-induced Damage
This study offers several exciting avenues for future studies in the animal model and Pv11 cell line that will further our understanding of anhydrobiosis and may lead to advancements in storing sensitive biologics at ambient temperatures for months or years.PMID:38608858 | DOI:10.1016/j.cstres.2024.04.002 (Source: Cell Stress and Chaperones)
Source: Cell Stress and Chaperones - April 12, 2024 Category: Cytology Authors: Clinton J Belott Oleg A Gusev Takahiro Kikawada Michael A Menze Source Type: research

Loss of the histone chaperone UNC-85/ASF1 inhibits the epigenome-mediated longevity and modulates the activity of one-carbon metabolism
Cell Stress Chaperones. 2024 Apr 10:S1355-8145(24)00065-8. doi: 10.1016/j.cstres.2024.04.003. Online ahead of print.ABSTRACTHistone H3/H4 chaperone ASF1 is a conserved factor mediating nucleosomal assembly and disassembly, playing crucial roles in processes such as replication, transcription, and DNA repair. Nevertheless, its involvement in aging has remained unclear. Here, we utilized the model organism Caenorhabditis elegans to demonstrate that the loss of UNC-85, the homolog of ASF1, leads to a shortened lifespan in a multicellular organism. Furthermore, we show that UNC-85 is required for epigenome-mediated longevity, ...
Source: Cell Stress and Chaperones - April 12, 2024 Category: Cytology Authors: Bideep Shrestha Anni I Nieminen Olli Matilainen Source Type: research

Membraneless and Membrane-bound Organelles in an Anhydrobiotic Cell Line are Protected from Desiccation-induced Damage
This study offers several exciting avenues for future studies in the animal model and Pv11 cell line that will further our understanding of anhydrobiosis and may lead to advancements in storing sensitive biologics at ambient temperatures for months or years.PMID:38608858 | DOI:10.1016/j.cstres.2024.04.002 (Source: Cell Stress and Chaperones)
Source: Cell Stress and Chaperones - April 12, 2024 Category: Cytology Authors: Clinton J Belott Oleg A Gusev Takahiro Kikawada Michael A Menze Source Type: research

Loss of the histone chaperone UNC-85/ASF1 inhibits the epigenome-mediated longevity and modulates the activity of one-carbon metabolism
Cell Stress Chaperones. 2024 Apr 10:S1355-8145(24)00065-8. doi: 10.1016/j.cstres.2024.04.003. Online ahead of print.ABSTRACTHistone H3/H4 chaperone ASF1 is a conserved factor mediating nucleosomal assembly and disassembly, playing crucial roles in processes such as replication, transcription, and DNA repair. Nevertheless, its involvement in aging has remained unclear. Here, we utilized the model organism Caenorhabditis elegans to demonstrate that the loss of UNC-85, the homolog of ASF1, leads to a shortened lifespan in a multicellular organism. Furthermore, we show that UNC-85 is required for epigenome-mediated longevity, ...
Source: Cell Stress and Chaperones - April 12, 2024 Category: Cytology Authors: Bideep Shrestha Anni I Nieminen Olli Matilainen Source Type: research

Loss of the histone chaperone UNC-85/ASF1 inhibits the epigenome-mediated longevity and modulates the activity of one-carbon metabolism
Cell Stress Chaperones. 2024 Apr 10:S1355-8145(24)00065-8. doi: 10.1016/j.cstres.2024.04.003. Online ahead of print.ABSTRACTHistone H3/H4 chaperone ASF1 is a conserved factor mediating nucleosomal assembly and disassembly, playing crucial roles in processes such as replication, transcription, and DNA repair. Nevertheless, its involvement in aging has remained unclear. Here, we utilized the model organism Caenorhabditis elegans to demonstrate that the loss of UNC-85, the homolog of ASF1, leads to a shortened lifespan in a multicellular organism. Furthermore, we show that UNC-85 is required for epigenome-mediated longevity, ...
Source: Cell Stress and Chaperones - April 12, 2024 Category: Cytology Authors: Bideep Shrestha Anni I Nieminen Olli Matilainen Source Type: research

Membraneless and Membrane-bound Organelles in an Anhydrobiotic Cell Line are Protected from Desiccation-induced Damage
This study offers several exciting avenues for future studies in the animal model and Pv11 cell line that will further our understanding of anhydrobiosis and may lead to advancements in storing sensitive biologics at ambient temperatures for months or years.PMID:38608858 | DOI:10.1016/j.cstres.2024.04.002 (Source: Cell Stress and Chaperones)
Source: Cell Stress and Chaperones - April 12, 2024 Category: Cytology Authors: Clinton J Belott Oleg A Gusev Takahiro Kikawada Michael A Menze Source Type: research

Discovery and Validation of a Novel Inhibitor of HYPE-mediated AMPylation
Cell Stress Chaperones. 2024 Apr 8:S1355-8145(24)00063-4. doi: 10.1016/j.cstres.2024.04.001. Online ahead of print.ABSTRACTAMPylation-the covalent transfer of an AMP from ATP onto a target protein-is catalyzed by the human enzyme HYPE/FicD to regulate its substrate, the heat shock chaperone BiP. HYPE-mediated AMPylation of BiP is critical for maintaining proteostasis in the ER (endoplasmic reticulum) and mounting an UPR (unfolded protein response) in times of proteostatic imbalance. Thus, manipulating HYPE's enzymatic activity is a key therapeutic strategy towards the treatment of various protein misfolding diseases, inclu...
Source: Cell Stress and Chaperones - April 10, 2024 Category: Cytology Authors: Ali Camara Heerak Chugh Alyssa George Lukas Dolidze Kevin Ryu Katrina J Holly Daniel P Flaherty Seema Mattoo Source Type: research

Discovery and Validation of a Novel Inhibitor of HYPE-mediated AMPylation
Cell Stress Chaperones. 2024 Apr 8:S1355-8145(24)00063-4. doi: 10.1016/j.cstres.2024.04.001. Online ahead of print.ABSTRACTAMPylation-the covalent transfer of an AMP from ATP onto a target protein-is catalyzed by the human enzyme HYPE/FicD to regulate its substrate, the heat shock chaperone BiP. HYPE-mediated AMPylation of BiP is critical for maintaining proteostasis in the ER (endoplasmic reticulum) and mounting an UPR (unfolded protein response) in times of proteostatic imbalance. Thus, manipulating HYPE's enzymatic activity is a key therapeutic strategy towards the treatment of various protein misfolding diseases, inclu...
Source: Cell Stress and Chaperones - April 10, 2024 Category: Cytology Authors: Ali Camara Heerak Chugh Alyssa George Lukas Dolidze Kevin Ryu Katrina J Holly Daniel P Flaherty Seema Mattoo Source Type: research