Matrix metallopeptidase 25 (MMP-25)

Matrix metalloproteinase-25 (MMP-25) is a member of the membrane-type MMP (MT-MMP) subfamily, attached to the plasma membrane via a glycosylphosphatidyl inositol anchor. Unlike most MMPs that are secreted as inactive proproteins requiring cleavage for activation, MMP-25 has a specific membrane attachment mechanism. In response to bacterial infection or inflammation, MMP-25 is thought to inactivate alpha-1 proteinase inhibitor, which is a major tissue protectant against proteolytic enzymes released by activated neutrophils. This inactivation facilitates the transendothelial migration of neutrophils to inflammatory sites. Additionally, MMP-25 may play a significant role in tumor invasion and metastasis through the activation of MMP2. The gene was previously referred to as MMP20 but has been renamed MMP25. MMP-25 is also known as MT6-MMP or Leukolysin and is capable of degrading various extracellular matrix components, including proMMP-2, fibronectin, and gelatin.

Other names

MT6-MMP (Membrane-type Matrix Metalloproteinase-6)LeukolysinMMP-20MMP20AMMPL1MT-MMP 6MT6MMPMTMMP6

Cleaves extracellular matrix proteins Activates MMP-2 (proMMP-2)