Uncoupling TGFβ1 signalling from collagen protein synthesis in Dupuytren’s disease: metabolic labelling and proteomics analysis of Dupuytren’s cord, nodule and normal palmar fascia controls (C4PR_LIV)

Dupuytren’s disease is a fibroproliferative disorder of the palmer fascia characterized by flexion contractures in the hand. Dupuytren’s can be treated surgically but disease recurrence rates are high, potentially due to a continual production of matrisomal proteins. Metabolic labelling and proteomics were used to determine the differences in the new synthesis and composition of matrisomal proteins between Dupuytren’s tissue and normal palmar fascia. Dupuytren’s tissue actively synthesised type I collagen, fibronectin, matrix metalloproteinases-2 and -3 (MMP2, MMP3) and Tissue Inhibitor of Metalloproteinases 2 (TIMP2). Both tissues actively synthesized Insulin-Like Growth Factor Binding Protein 7 (IGFBP7). Label-free analysis implicated the TGFβ pathway in the matrisomal profile of Dupuytren’s tissue.