matrilysins

Matrilysins are a subfamily of matrix metalloproteinases (MMPs), a group of zinc-dependent endopeptidases. They are characterized by their specific structure, which includes a catalytic domain containing a zinc-binding motif and a C-terminal domain. In humans, there are two known matrilysins: MMP-7 (also known as matrilysin-1 or PUMP1) and MMP-26 (also known as matrilysin-2 or ENDK).

These enzymes are primarily involved in the remodeling of the extracellular matrix. Unlike some other MMPs that are secreted and function in the interstitial space, matrilysins are often found associated with the cell surface or secreted into lumens of glands. They can cleave a variety of extracellular matrix proteins, including collagen, fibronectin, and laminin, as well as non-matrix substrates like defensins and pro-hormones.

Matrilysins play roles in various physiological processes such as wound healing, tissue development, and inflammation. However, their dysregulation has been implicated in pathological conditions, including cancer. In cancer, matrilysins can contribute to tumor growth, invasion, and metastasis by degrading the extracellular matrix, facilitating cell migration, and releasing growth factors. MMP-7, in particular, has been studied extensively for its role in epithelial cancers. The precise functions and substrates of MMP-26 are less understood compared to MMP-7.