metalloproteinase10

Metalloproteinase-10, also known as stromelysin-2, is a member of the matrix metalloproteinase (MMP) family. It is a secreted, zinc-dependent endopeptidase encoded by the MMP10 gene in humans. Like other MMPs, it participates in remodeling the extracellular matrix (ECM) and in processing various non-matrix substrates, contributing to tissue repair, development, and inflammation.

The enzyme is produced as an inactive zymogen and is activated by proteolytic removal of its propeptide. Its catalytic domain contains the conserved zinc-binding motif characteristic of MMPs and is followed by a hemopexin-like C-terminal domain that contributes to substrate recognition and specificity. Activation often involves other proteases present in the tissue microenvironment, such as other MMPs.

MMP-10 degrades multiple ECM components, including certain collagens, laminin, fibronectin, and proteoglycans, supporting ECM remodeling. It can also participate in the activation or processing of other proteases and signaling molecules, thereby influencing cellular behavior in tissues undergoing remodeling or inflammatory responses.

Regulation of MMP-10 occurs at multiple levels. Its expression is inducible by inflammatory cytokines such as interleukin-1 and tumor necrosis factor-alpha and by cellular stress. Activity is tightly controlled by endogenous inhibitors known as tissue inhibitors of metalloproteinases (TIMPs).

Clinical and research relevance of MMP-10 lies in its altered expression in various diseases, including osteoarthritis, rheumatoid arthritis, and certain cancers, where it may contribute to invasion and metastasis through ECM degradation. Because broad-spectrum MMP inhibitors have shown limited clinical success, interest continues in understanding MMP-10’s specific roles to identify targeted therapeutic strategies.