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Dupuytren's disease can be treated surgically, but disease recurrence rates are high, potentially due to continual production of matrisomal proteins. Here, metabolic labelling and proteomics identified differences in the new synthesis and composition of matrisomal proteins between Dupuytren's tissue and normal PF. Dupuytren's tissue actively synthesised type I collagen, fibronectin (FN1), matrix metalloproteinases\u20102 and \u20103 (MMP2, MMP3) and tissue inhibitor of metalloproteinases 2 (TIMP2). Both tissues actively synthesised insulin\u2010like growth factor binding protein 7 (IGFBP7). Label\u2010free analysis implicated the transforming growth factor\u2010\u03b2 (TGF\u03b2) pathway in the matrisomal profile of Dupuytren's tissue. The effect of TGF\u03b2 isoforms on\n                    <jats:italic>COL1<\/jats:italic>\n                    mRNA expression was first tested in cultured young and aged equine tenocytes.\n                    <jats:italic>COL1A1<\/jats:italic>\n                    mRNA responded to treatment with all TGF\u03b2 isoforms and was more highly expressed in cells from aged samples. In aged human cells,\n                    <jats:italic>COL1A1<\/jats:italic>\n                    and\n                    <jats:italic>COL1A2<\/jats:italic>\n                    mRNA was higher in cells derived from Dupuytren's tissue than normal PF and in response to TGF\u03b21, but no changes in\n                    <jats:italic>COL1A1<\/jats:italic>\n                    or\n                    <jats:italic>COL1A2<\/jats:italic>\n                    CpG methylation were detected. TGF\u03b21 treatment only resulted in increased type I collagen protein accumulation in the media of Dupuytren's nodule cells. In three\u2010dimensional cultures,\n                    <jats:italic>COL1A1<\/jats:italic>\n                    mRNA was lower in normal PF than in Dupuytren's cells, but TGF\u03b21 treatment only increased type I collagen accumulation in the media of normal PF cultures, and TGF\u03b21 inhibition did not alter new collagen protein synthesis. TGF\u03b21 inhibition in Dupuytren's tissue explants did not alter the proportion of homotrimeric type I collagen, nor was this changed in skin or tendon of the tight\u2010skin (TSK) mouse, a naturally occurring model of indirect TGF\u03b21 activation. Therefore, the role of TGF\u03b2 in Dupuytren's disease may be predominantly related to myofibroblast phenoconversion and contractility rather than directly altering collagen protein synthesis. \u00a9 2026 The Author(s).\n                    <jats:italic>The Journal of Pathology<\/jats:italic>\n                    published by John Wiley &amp; Sons Ltd on behalf of The Pathological Society of Great Britain and Ireland.\n                  <\/jats:p>","DOI":"10.1002\/path.70020","type":"journal-article","created":{"date-parts":[[2026,1,27]],"date-time":"2026-01-27T05:31:11Z","timestamp":1769491871000},"page":"383-397","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Uncoupling\n                    <scp>TGF\u03b21<\/scp>\n                    signalling from collagen protein synthesis in Dupuytren's disease"],"prefix":"10.1002","volume":"268","author":[{"given":"Gabriella","family":"Cooper","sequence":"first","affiliation":[{"name":"Department of Musculoskeletal and Ageing Science, Institute of Life Course and Medical Sciences University of Liverpool  Liverpool UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jade A","family":"Gumbs","sequence":"additional","affiliation":[{"name":"Department of Musculoskeletal and Ageing Science, Institute of Life Course and Medical Sciences University of Liverpool  Liverpool UK"},{"name":"The Medical Research Council Versus Arthritis Centre for Integrated Research into Musculoskeletal Ageing (CIMA)  Liverpool UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sahem","family":"Alkharabsheh","sequence":"additional","affiliation":[{"name":"Department of Musculoskeletal and Ageing Science, Institute of Life Course and Medical Sciences University of Liverpool  Liverpool UK"},{"name":"Faculty of Allied Medical 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S","family":"O'Heneghan\u2010Yates","sequence":"additional","affiliation":[{"name":"Department of Musculoskeletal and Ageing Science, Institute of Life Course and Medical Sciences University of Liverpool  Liverpool UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rama","family":"Ijaz","sequence":"additional","affiliation":[{"name":"Department of Musculoskeletal and Ageing Science, Institute of Life Course and Medical Sciences University of Liverpool  Liverpool UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Emma","family":"Beamish","sequence":"additional","affiliation":[{"name":"Department of Musculoskeletal and Ageing Science, Institute of Life Course and Medical Sciences University of Liverpool  Liverpool UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lisa A","family":"Menezes","sequence":"additional","affiliation":[{"name":"Department of Musculoskeletal and Ageing Science, Institute of Life Course and Medical Sciences 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