Open AccessRoles of pericellular proteolysis by membrane type‐1 matrix metalloproteinase in cancer invasion and angiogenesis
Author(s) -
Seiki Motoharu,
Yana Ikuo
Publication year - 2003
Publication title -
cancer science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.035
H-Index - 141
eISSN - 1349-7006
pISSN - 1347-9032
DOI - 10.1111/j.1349-7006.2003.tb01484.x
Subject(s) - proteolysis , matrix metalloproteinase , angiogenesis , proteases , extracellular matrix , metalloproteinase , microbiology and biotechnology , cancer cell , biology , cancer , tumor progression , cell adhesion molecule , tumor microenvironment , chemistry , cancer research , biochemistry , enzyme , genetics
Behavior of cancer cells is profoundly affected by their microenvironment, which is often controlled by pericellular proteolysis or the processing of protein components, including extracellular matrices, growth factors, cytokines, receptors, cell adhesion molecules, and so on. Matrix metalloproteinases (MMPs) are a family of zinc‐dependent proteases responsible for the proteolytic events in the extracellular milieu. Among the multiple MMPs expressed in a wide range of tumors, membrane type‐1 MMP (MT1‐MMP), which is expressed especially in tumor cells with significant invasive properties, is thought to be particularly important for pericellular proteolysis. Recent studies have elucidated in part how MT1‐MMP is regulated biologically for the promotion of invasion by tumors or for angiogenesis by endothelial cells. Understanding of the proteolysis by, and the regulation of MT1‐MMP, which probably promotes cell invasion, could provide a therapeutic hint as to how to block or delay the progression of cancer.