Dermatopontin (DPT) is a 22 kDa extracellular matrix protein that mediates cell-matrix interactions through integrin binding and serves as a communication link between dermal fibroblasts and their extracellular environment. The protein enhances transforming growth factor-beta (TGF-β) biological activity by interacting with decorin, thereby increasing cellular responsiveness to TGF-β signaling 1. DPT inhibits cell proliferation and accelerates collagen fibril formation and stabilization. The gene is broadly expressed across connective tissues including skin, heart, lung, kidney, and bone, with two mRNA species indicating alternative polyadenylation or splicing 2. DPT expression is regulated by cytokines and matrix composition; TGF-β1 increases expression while interleukin-4 reduces it 3. Notably, dermatopontin levels are significantly decreased in fibroblasts from patients with hypertrophic scar and systemic sclerosis skin, suggesting an association between reduced DPT expression and pathogenic fibrosis 3. The protein is tyrosine-sulphated, indicating post-translational modification relevant to its extracellular matrix functions 4. These characteristics position DPT as a regulator of fibroblast behavior and matrix homeostasis with potential relevance to fibrotic disease pathogenesis.