{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Sabeh F"],"funding":["Breast Cancer Research Foundation","NIBIB NIH HHS","NIDDK NIH HHS","NHLBI NIH HHS","Margolies Family Discovery Fund for Cancer Research","NCI NIH HHS","National Institutes of Health","NIH HHS"],"pagination":["e202312091"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11244150"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["223(9)"],"pubmed_abstract":["Dermal fibroblasts deposit type I collagen, the dominant extracellular matrix molecule found in skin, during early postnatal development. Coincident with this biosynthetic program, fibroblasts proteolytically remodel pericellular collagen fibrils by mobilizing the membrane-anchored matrix metalloproteinase, Mmp14. Unexpectedly, dermal fibroblasts in Mmp14-/- mice commit to a large-scale apoptotic program that leaves skin tissues replete with dying cells. A requirement for Mmp14 in dermal fibroblast survival is recapitulated in vitro when cells are embedded within, but not cultured atop, three-dimensional hydrogels of crosslinked type I collagen. In the absence of Mmp14-dependent pericellular proteolysis, dermal fibroblasts fail to trigger β1 integrin activation and instead actuate a TGF-β1"],"journal":["The Journal of cell biology"],"pubmed_title":["Mmp14-dependent remodeling of the pericellular-dermal collagen interface governs fibroblast survival."],"pmcid":["PMC11244150"],"funding_grant_id":["R01 HL085339","P30 DK020572","P41-EB015890","R01 CA071699","R01-CA-071699-16-A1","T32 CA009676","RO1-HL085339","P41 EB015890"],"pubmed_authors":["Gimenez LE","Sabeh F","Kurup A","Botvinick E","Olson AW","Li XY","Weiss SJ","Cho JS"],"additional_accession":[]},"is_claimable":false,"name":"Mmp14-dependent remodeling of the pericellular-dermal collagen interface governs fibroblast survival.","description":"Dermal fibroblasts deposit type I collagen, the dominant extracellular matrix molecule found in skin, during early postnatal development. Coincident with this biosynthetic program, fibroblasts proteolytically remodel pericellular collagen fibrils by mobilizing the membrane-anchored matrix metalloproteinase, Mmp14. Unexpectedly, dermal fibroblasts in Mmp14-/- mice commit to a large-scale apoptotic program that leaves skin tissues replete with dying cells. A requirement for Mmp14 in dermal fibroblast survival is recapitulated in vitro when cells are embedded within, but not cultured atop, three-dimensional hydrogels of crosslinked type I collagen. In the absence of Mmp14-dependent pericellular proteolysis, dermal fibroblasts fail to trigger β1 integrin activation and instead actuate a TGF-β1","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Sep","modification":"2026-05-02T14:28:19.655Z","creation":"2026-04-07T18:06:07.844Z"},"accession":"S-EPMC11244150","cross_references":{"pubmed":["38990714"],"doi":["10.1083/jcb.202312091"]}}