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National Institute of Environmental Health Sciences

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Publication Detail

Title: Membrane type 1 matrix metalloprotease cleaves laminin-10 and promotes prostate cancer cell migration.

Authors: Bair, Elisabeth L; Chen, Man Ling; McDaniel, Kathy; Sekiguchi, Kiyotoshi; Cress, Anne E; Nagle, Raymond B; Bowden, George Timothy

Published In Neoplasia, (2005 Apr)

Abstract: Disruption of the extracellular matrix by proteases is crucial for tumor invasion. Laminin-10 (Ln-10) has previously been identified as a substrate for cell migration and cell adhesion, and is present in the basal lamina (BL) of both normal prostate and prostate cancer. Here, we investigate a role for membrane type 1 matrix metalloprotease (MT1-MMP) in modifying this Ln-10-rich BL. MT1-MMP is a transmembrane member of the MMP family that has been demonstrated to be upregulated as prostate cancer progresses from normal to prostate intraepithelial neoplasia to invasive cancer, suggesting a role for MT1-MMP in the invasion of prostate cancer. We show that MT1-MMP cleaves the alpha5 chain of purified human Ln-10 from its 350-kDa form into 310-, 190-, 160-, and 45-kDa fragments. This cleavage causes a decrease in DU-145 prostate cancer cell adhesion to purified Ln-10, and an increase in transmigration of DU-145 cells through cleaved Ln-10. We also show that prostate cancer cells expressing membrane-bound MT1-MMP cleave the alpha5 chain of Ln-10. Ln alpha5-chain cleavage is also observed in human prostate cancer tissues. These findings suggest that prostate cancer cells expressing high levels of MT1-MMP have increased invasive potential through their ability to degrade and invade Ln-10 barriers.

PubMed ID: 15967115 Exiting the NIEHS site

MeSH Terms: No MeSH terms associated with this publication

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