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• W3112370158 endingPage "2646" @default.
• W3112370158 startingPage "2646" @default.
• W3112370158 abstract "Proper processing of collagens COL1 and COL6 is required for normal function of adipose tissue and skeletal muscle. Proteoglycan decorin (DCN) regulates collagen fiber formation. The amino-terminus of DCN is modified with an O-linked glycosaminoglycan (GAG), the function of which has remained unclear. Previously, non-glycanated DCN (ngDCN) was identified as a marker of adipose stromal cells. Here, we identify MMP14 as the metalloprotease that cleaves DCN to generate ngDCN. We demonstrate that mice ubiquitously lacking DCN GAG (ngDCN mice) have reduced matrix rigidity, enlarged adipocytes, fragile skin, as well as skeletal muscle hypotrophy, fibrosis, and dysfunction. Our results indicate that DCN deglycanation results in reduced intracellular DCN—collagen binding and increased production of truncated COL6 chains, leading to aberrant procollagen processing and extracellular localization. This study reveals that the GAG of DCN functions to regulate collagen assembly in adipose tissue and skeletal muscle and uncovers a new mechanism of matrix dysfunction in obesity and aging." @default.
• W3112370158 created "2020-12-21" @default.
• W3112370158 creator A5021912710 @default.
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• W3112370158 creator A5086132910 @default.
• W3112370158 creator A5088225640 @default.
• W3112370158 creator A5090039043 @default.
• W3112370158 date "2020-12-09" @default.
• W3112370158 modified "2023-10-15" @default.
• W3112370158 title "Glycosaminoglycan Modification of Decorin Depends on MMP14 Activity and Regulates Collagen Assembly" @default.
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• W3112370158 doi "https://doi.org/10.3390/cells9122646" @default.
• W3112370158 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7764107" @default.
• W3112370158 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/33317052" @default.
• W3112370158 hasPublicationYear "2020" @default.
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