{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,17]],"date-time":"2026-07-17T11:40:27Z","timestamp":1784288427517,"version":"3.55.0"},"reference-count":36,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2025,4,4]],"date-time":"2025-04-04T00:00:00Z","timestamp":1743724800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Intern J of Cosmetic Sci"],"published-print":{"date-parts":[[2025,10]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:sec><jats:title>Objective<\/jats:title><jats:p>Collagens are widely studied proteins given their implications in the skin extracellular matrix and pathological conditions such as fibrosis. Type V collagen is a member of the fibrillar collagens, and three different polypeptide chains, \u03b11, \u03b12 and \u03b13 form isoforms through associations. The third chain, \u03b13, of type V collagen was initially identified in the placenta, but after decades, it remains poorly characterized. The aim of this study is to investigate the expression and localization of the \u03b13 chain of type V collagen in the skin and its evolution during skin aging. The identification of \u03b13(V) collagen as a target of retinoic acid and its interaction with matrix metalloproteinase\u20109 (MMP\u20109) was investigated.<\/jats:p><\/jats:sec><jats:sec><jats:title>Methods<\/jats:title><jats:p>The expression and localization of \u03b13(V) collagen were assessed by immunodetection in ex\u00a0vivo skin and in keratinocytes using a calcium\u2010differentiated model. The variation in \u03b13(V) collagen expression during aging was studied in ex\u00a0vivo skin from donors of different ages. The modulation of \u03b13(V) collagen by retinoic acid was investigated by qPCR in keratinocytes and by immunofluorescence in ex\u00a0vivo skin biopsies. Silencing of \u03b13(V) collagen was performed using siRNA. The expression of MMP\u20109 was investigated using qPCR.<\/jats:p><\/jats:sec><jats:sec><jats:title>Results<\/jats:title><jats:p>In our study, we showed that \u03b13(V) collagen was abundantly produced by basal skin keratinocytes and in the outer root sheath of the hair. \u03b13(V) collagen expression appears to decrease with age in the skin and in differentiated keratinocytes. We also identified that treatment of keratinocytes and ex\u00a0vivo skin biopsies with retinoic acid induced \u03b13(V) collagen expression. Finally, we showed that inhibition of \u03b13(V) collagen in keratinocytes led to an increase in MMP\u20109 expression.<\/jats:p><\/jats:sec><jats:sec><jats:title>Conclusion<\/jats:title><jats:p>This study provides a better understanding of \u03b13(V) collagen expression and localization in the skin. These findings suggest that \u03b13(V) collagen could contribute to the therapeutic and anti\u2010aging value of retinoic acid on the skin and may open new prospects. Finally, our data shed more light on the functional relationship between \u03b13(V) collagen and MMP\u20109, opening possibilities for anti\u2010aging and eczema treatments.<\/jats:p><\/jats:sec>","DOI":"10.1111\/ics.13062","type":"journal-article","created":{"date-parts":[[2025,4,5]],"date-time":"2025-04-05T09:24:34Z","timestamp":1743845074000},"page":"743-751","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Collagen type V alpha 3 chain is involved in human skin basement membrane physiology and <scp>MMP\u20109<\/scp> regulation"],"prefix":"10.1111","volume":"47","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-4563-8780","authenticated-orcid":false,"given":"Florian","family":"Labarrade","sequence":"first","affiliation":[{"name":"Ashland Specialties France  Sophia Antipolis 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