Proteins of the matrix metalloproteinase (MMP) family are zinc containing proteolytic enzymes involved in the breakdown of the extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling. They also play an important role in apoptosis, tumor cell growth, invasion, metastasis, as well as in angiogenesis and wound healing. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. Most of the MMP's contain a common domain structure, which include a signal sequence, a propeptide, a catalytic domain and a hemopexin-like (Hpx) domain. MMP10 degrades proteoglycans, gelatins of type I, III, IV, and V; weakly collagens III, IV, and V. and fibronectin. It activates procollagenase. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.