Matrix metalloproteinase-17 (MMP17)

Matrix metalloproteinase-17 (MMP17), also known as membrane-type matrix metalloproteinase 4 (MT4-MMP), is a membrane-bound zinc-dependent endopeptidase of the matrix metalloproteinase family, specifically anchored to the cell surface via a glycosylphosphatidylinositol (GPI) moiety[2][5]. MMP17 is involved in the proteolytic cleavage of extracellular and pericellular substrates, modulating extracellular matrix turnover, activating growth factors, and regulating cell migration and differentiation, especially during embryonic development, tissue remodeling, and in disease states such as cancer and arthritis[1][3][5]. Unlike most MMPs, MMP17 shows unique substrate specificity, limited classical ECM-degrading activity, and is highly expressed in smooth muscle and tumor tissues; it also functions in niche regulation for intestinal stem cells, and may play roles in angiogenesis, vascular development, and pathological matrix remodeling[1][4][5]. While MMP17 is considered a potential therapeutic target, much about its substrate spectrum, regulation, and therapeutic modulation remains unclear, and it is distinguished by atypical structure–function features within the MMP family[3][5].

Other names

MT4-MMPMT4MMPMT-MMP 4MTMMP4membrane-type matrix metalloproteinase 4membrane-type-4 matrix metalloproteinasematrix metallopeptidase 17

Proteolytic cleavage of specific extracellular, membrane, or pericellular proteins (e.g., pro-TNFα, POSTN, OPN)[3][4]. Remodeling of extracellular matrix to modulate cellular microenvironment. Activation or inactivation of signaling molecules via proteolysis