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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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1437-4315
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Volume 387, Issue 6

Issues

The role of kallikrein-related peptidases in prostate cancer: potential involvement in an epithelial to mesenchymal transition

Astrid K. Whitbread
  • Hormone-Dependent Cancer Program, School of Life Sciences and Institute of Health and Biomedical Innovation, Queensland University of Technology, Brisbane 4000, QLD, Australia
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Tara L. Veveris-Lowe
  • Hormone-Dependent Cancer Program, School of Life Sciences and Institute of Health and Biomedical Innovation, Queensland University of Technology, Brisbane 4000, QLD, Australia
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Mitchell G. Lawrence
  • Hormone-Dependent Cancer Program, School of Life Sciences and Institute of Health and Biomedical Innovation, Queensland University of Technology, Brisbane 4000, QLD, Australia
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ David L. Nicol / Judith A. Clements
  • Hormone-Dependent Cancer Program, School of Life Sciences and Institute of Health and Biomedical Innovation, Queensland University of Technology, Brisbane 4000, QLD, Australia
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2006-06-26 | DOI: https://doi.org/10.1515/BC.2006.089

Abstract

Several members of the kallikrein-related peptidase family of serine proteases have proteolytic activities that may affect cancer progression; however, the in vivo significance of these activities remains uncertain. We have demonstrated that expression of PSA or KLK4, but not KLK2, in PC-3 prostate cancer cells changed the cellular morphology from epithelial to spindle-shaped, markedly reduced E-cadherin expression, increased vimentin expression and increased cellular migration. These changes are indicative of an epithelial to mesenchymal transition (EMT), a process important in embryonic development and cancer progression. The potential novel role of kallikrein-related peptidases in this process is the focus of this brief review.

Keywords: E-cadherin; EMT; KLK4; migration; prostate cancer; PSA

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About the article

Corresponding author


Published Online: 2006-06-26

Published in Print: 2006-06-01


Citation Information: Biological Chemistry, Volume 387, Issue 6, Pages 707–714, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2006.089.

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