Membrane Type 1 Matrix Metalloprotease Cleaves Laminin-10 and Promotes Prostate Cancer Cell Migration

Bair, Elisabeth L.; Chen, Man Ling; McDaniel, Kathy et al.

Neoplasia, 2005, 7(4), 380-389

Number of Access:619（2025-08-18 14:28 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/71825

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Title
Membrane Type 1 Matrix Metalloprotease Cleaves Laminin-10 and Promotes Prostate Cancer Cell Migration
Creator
CreatorName
Bair, Elisabeth L.
CreatorName
Chen, Man Ling
CreatorName
McDaniel, Kathy
NRID
1000050187845 1000050187845
researchmap permalink
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Scopus Author ID
7201662709 7201662709
ORCID
0000-0002-6433-1410 0000-0002-6433-1410
CreatorName
Sekiguchi, Kiyotoshi
CreatorName
Cress, Anne E.
CreatorName
Nagle, Raymond B.
CreatorName
Bowden, George Timothy
Subject
Laminin-10
MT1-MMP
prostate
MMP-14
invasion
Description
Elisabeth L. Bair, Man Ling Chen, Kathy McDaniel, Kiyotoshi Sekiguchi, Anne E. Cress, Raymond B. Nagle, and George Timothy Bowden, "Membrane Type 1 Matrix Metalloprotease Cleaves Laminin-10 and Promotes Prostate Cancer Cell Migration", Neoplasia, Vol. 7 (4), pp. 380-389, Elsevier, 2005
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 α5 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 α5 chain of Ln-10. Ln α5-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.
Publisher
Elsevier
Source Title
Neoplasia
Volume (Issue)
7(4)
Page
380-389
Date of Issued
2005-04
Language
English
Handle URL
https://hdl.handle.net/11094/71825
eISSN
14765586
Relation.isIdenticalTo
DOI (Publisher Version)
https://doi.org/10.1593/neo.04619
Access Rights
open access
CopyRight
© 2005 Neoplasia Press, Inc. Published by Elsevier Inc. This article is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 3.0 Unported License.
oaire:version
Version of Record
Category
学術雑誌論文 Journal Article