Proteolytic Processing of Laminin-332 by Hepsin and Matriptase and Its Role in Prostate Cancer Progression

Abstract

Laminin-332 is lost in prostate cancer progression. Laminin-332 is known to be cleaved by various cell surface proteases, including MMPs, and this cleavage facilitates migration of cancer cells. We have found that Laminin-332 is individually cleaved by two serine proteases, hepsin and matriptase, and that this cleavage enhances migration of human prostate cancer cells in vitro. Hepsin is over-expressed in more than 90% prostate cancer cases. Similarly, matriptase is over-expressed in human prostate cancer cases and expression of both proteases correlates with tumor progression. However, the mechanism(s) by which these two serine proteases play a role in prostate cancer is unknown. We found that Hepsin/matriptase overexpressing prostate cancer cells, LNCaP show significantly increased migration on Ln-332. This project aims to define the role played by the cleavage of Laminin-332 by hepsin and matriptase in prostate cancer.

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Document Details

Document Type
Technical Report
Publication Date
Sep 01, 2010
Accession Number
ADA548821

Entities

People

  • Manisha Tripathi

Organizations

  • Vanderbilt University

Tags

DTIC Thesaurus Topics

  • Amino Acids
  • Biological Sciences
  • Cell Movement
  • Cells
  • Cellular Structures
  • Chemical Synthesis
  • Chemistry
  • Databases
  • Department Of Defense
  • Diseases And Disorders
  • Epithelial Cells
  • Mass Spectrometry
  • Molecular Biology
  • Neoplasms
  • Neutral Amino Acids
  • Prostate Cancer
  • Tissues

Fields of Study

  • Biology
  • Chemistry

Readers

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  • Molecular Biology and Genetics