Matrix metalloproteinase 10 (MMP-10)

Matrix metalloproteinase 10 (MMP-10), also known as stromelysin-2, is a secreted zinc-dependent endopeptidase from the matrix metalloproteinase (MMP) family, encoded by the MMP10 gene[1]. It plays a central role in degrading extracellular matrix components such as proteoglycans and fibronectin, important for normal physiological processes (embryonic development, tissue remodeling, wound healing) and pathological conditions (cancer, metastasis, inflammation, arthritis)[1][3][6][10]. Structurally, MMP-10 contains a signal peptide, pro-domain (for zymogen regulation), catalytic domain (with zinc-dependent activity), and a hemopexin-like domain responsible for substrate specificity and protein-protein interactions[4][6]. MMP-10 activity is tightly regulated by tissue inhibitors of metalloproteinases (TIMPs), notably TIMP-1 and TIMP-2, although the inhibitory interactions are weaker compared to some related MMPs (e.g., MMP-3)[3][4]. Overexpression of MMP-10 is implicated in cancer progression, metastasis, and acts as a potential prognostic biomarker in certain cancers such as oral cancer[1]. Its inhibition is an active area of drug development, but achieving therapeutic specificity remains a challenge due to conserved active sites among MMP family members[4][6].

Other names

Stromelysin-2Transin-2

Inhibition of enzymatic activity (by chelating active site zinc), Competitive inhibition (TIMPs, small molecules like NNGH)