<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Sabeh F</submitter><funding>Breast Cancer Research Foundation</funding><funding>NIBIB NIH HHS</funding><funding>NIDDK NIH HHS</funding><funding>NHLBI NIH HHS</funding><funding>Margolies Family Discovery Fund for Cancer Research</funding><funding>NCI NIH HHS</funding><funding>National Institutes of Health</funding><funding>NIH HHS</funding><pagination>e202312091</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11244150</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>223(9)</volume><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</pubmed_abstract><journal>The Journal of cell biology</journal><pubmed_title>Mmp14-dependent remodeling of the pericellular-dermal collagen interface governs fibroblast survival.</pubmed_title><pmcid>PMC11244150</pmcid><funding_grant_id>R01 HL085339</funding_grant_id><funding_grant_id>P30 DK020572</funding_grant_id><funding_grant_id>P41-EB015890</funding_grant_id><funding_grant_id>R01 CA071699</funding_grant_id><funding_grant_id>R01-CA-071699-16-A1</funding_grant_id><funding_grant_id>T32 CA009676</funding_grant_id><funding_grant_id>RO1-HL085339</funding_grant_id><funding_grant_id>P41 EB015890</funding_grant_id><pubmed_authors>Gimenez LE</pubmed_authors><pubmed_authors>Sabeh F</pubmed_authors><pubmed_authors>Kurup A</pubmed_authors><pubmed_authors>Botvinick E</pubmed_authors><pubmed_authors>Olson AW</pubmed_authors><pubmed_authors>Li XY</pubmed_authors><pubmed_authors>Weiss SJ</pubmed_authors><pubmed_authors>Cho JS</pubmed_authors></additional><is_claimable>false</is_claimable><name>Mmp14-dependent remodeling of the pericellular-dermal collagen interface governs fibroblast survival.</name><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</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 Sep</publication><modification>2026-05-02T14:28:19.655Z</modification><creation>2026-04-07T18:06:07.844Z</creation></dates><accession>S-EPMC11244150</accession><cross_references><pubmed>38990714</pubmed><doi>10.1083/jcb.202312091</doi></cross_references></HashMap>