Matrix metalloproteinase-26 (MMP-26)

Matrix metalloproteinase-26 (MMP-26), also known as matrilysin-2 or endometase, is a zinc-dependent endopeptidase that belongs to the matrix metalloproteinase family. Unlike many other MMPs, MMP-26 lacks a hemopexin-like C-terminal domain and is one of the smallest MMPs, with a structure consisting mainly of a catalytic and pro-domain[1][5]. Its primary biological function is to degrade a range of extracellular matrix (ECM) components such as type IV collagen, fibronectin, vitronectin, fibrinogen, and casein. It can also activate other MMPs (notably MMP-9), thereby playing a significant role in tissue remodeling[1][3][5]. MMP-26 is predominantly expressed in epithelial-derived cancers, including breast, prostate, lung, and endometrial carcinoma, where it promotes cancer cell invasion, angiogenesis, and tumor progression, particularly in estrogen-dependent malignancies[5][6]. Overexpression of MMP-26 correlates with increased malignancy, greater invasiveness, and higher angiogenic potential in tumors. It functions as an oncogenic protease and its inhibition can block cancer cell migration and invasion. Its physiological roles are balanced by tissue inhibitors of metalloproteinases (TIMPs), especially TIMP-4[5]. MMP-26 is thus an important therapeutic target and biomarker in oncology, though drug development is complicated by potential safety concerns due to its role in normal tissue processes[1][2][5][6].

Other names

matrilysin-2endometaseMMP26MMP-26MGC126590MGC126592matrilysin 2

Inhibition of enzymatic (proteolytic) activity on extracellular matrix substrates Neutralization by monoclonal antibody (experimental in vitro/in vivo)[6]