Matrilysin 1 influences colon carcinoma cell migration by cleavage of the laminin-5 beta3 chain.

Matrilysin 1 [matrix metalloproteinase 7 (MMP7)] is one of the most important metalloproteinases expressed in human tissues. This enzyme is generally not expressed by normal differentiated epithelial colon cells, but has been shown to be up-regulated in human colon adenomas and adenocarcinomas. Little is known about the role of MMP7 in cell invasion and its involvement in proteolytic processes.

[Matrilysin-1 and cancer pathology].

Matrilysin-1 has a considerable importance in the progression of cancers, namely digestive, ones inasmuch as it fulfils a direct function of deterioration on molecular targets at different levels and interferes as well in the activation of other proteolytic systems. Its low expression in sound tissues increases distinctly in mild cellular proliferations like adenomas to increase even more in carcinomas and be involved at the level of tumoral development as well as in a metastatical proliferation. It acts during the different stages of malignant transformation, splitting the E-cadherin, an intercellular adhesive molecule of epithelia, matrix molecules in the tumor-stroma interface and integrins which link matrix components to epithelial cells.