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- W2279912430 abstract "Tissue fibrosis is a major cause of organ dysfunction during chronic diseases and aging. A critical step in this process is transforming growth factor β1 (TGF-β1)-mediated transformation of fibroblasts into myofibroblasts, cells capable of synthesizing extracellular matrix. Here, we show that SIRT3 controls transformation of fibroblasts into myofibroblasts via suppressing the profibrotic TGF-β1 signaling. We found that Sirt3 knockout (KO) mice with age develop tissue fibrosis of multiple organs, including heart, liver, kidney, and lungs but not whole-body SIRT3-overexpressing mice. SIRT3 deficiency caused induction of TGF-β1 expression and hyperacetylation of glycogen synthase kinase 3β (GSK3β) at residue K15, which negatively regulated GSK3β activity to phosphorylate the substrates Smad3 and β-catenin. Reduced phosphorylation led to stabilization and activation of these transcription factors regulating expression of the profibrotic genes. SIRT3 deacetylated and activated GSK3β and thereby blocked TGF-β1 signaling and tissue fibrosis. These data reveal a new role of SIRT3 to negatively regulate aging-associated tissue fibrosis and discloses a novel phosphorylation-independent mechanism controlling the catalytic activity of GSK3β." @default.
- W2279912430 created "2016-06-24" @default.
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- W2279912430 date "2016-03-01" @default.
- W2279912430 modified "2023-10-15" @default.
- W2279912430 title "SIRT3 Blocks Aging-Associated Tissue Fibrosis in Mice by Deacetylating and Activating Glycogen Synthase Kinase 3β" @default.
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- W2279912430 doi "https://doi.org/10.1128/mcb.00586-15" @default.
- W2279912430 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4760222" @default.
- W2279912430 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26667039" @default.
- W2279912430 hasPublicationYear "2016" @default.
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