To investigate the mechanisms underlying matrix deposition in Dupuytren's disease, the expression of gelatinase A (MMP-2), the tissue inhibitor of metalloproteinase-2 (TIMP-2), transforming growth factor beta 1 (TGF-β1), decorin (DCN), and periostin was studied. The level of relative MMP-2 activation was investigated using zymography. The mRNA expression of MMP-2, TIMP-2, TGF-β1, and DCN was detected using reverse transcription polymerase chain reaction (RT-PCR), while the presence of protein was detected using immunohistochemical (IHC) and Western blot techniques. The level of MMP-2 activation was significantly elevated in tissues with Dupuytren's contracture. RT-PCR demonstrated significantly higher expression of MMP-2, TIMP-2, TGF-β1, and DCN mRNA in the pathological tissues; and the IHC and immunoblotting studies revealed elevated expression of TGF-β1, DCN, and periostin. The balance between MMP-2 and TIMP-2 was disrupted in patients with Dupuytren's disease. TGF-β1, DCN, and periostin are involved in extracellular matrix (ECM) homeostasis in Dupuytren's contracture.