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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 389, Issue 6

Issues

Prostatic trypsin-like kallikrein-related peptidases (KLKs) and other prostate-expressed tryptic proteinases as regulators of signalling via proteinase-activated receptors (PARs)

Andrew J. Ramsay
  • 1Institute of Health and Biomedical Innovation, Queensland University of Technology, 6 Musk Avenue, Kelvin Grove, Queensland 4059, Australia
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/ Janet C. Reid
  • 2Institute of Health and Biomedical Innovation, Queensland University of Technology, 6 Musk Avenue, Kelvin Grove, Queensland 4059, Australia
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/ Mark N. Adams
  • 3Institute of Health and Biomedical Innovation, Queensland University of Technology, 6 Musk Avenue, Kelvin Grove, Queensland 4059, Australia
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/ Hemamali Samaratunga / Ying Dong
  • 5Institute of Health and Biomedical Innovation, Queensland University of Technology, 6 Musk Avenue, Kelvin Grove, Queensland 4059, Australia
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/ Judith A. Clements
  • 6Institute of Health and Biomedical Innovation, Queensland University of Technology, 6 Musk Avenue, Kelvin Grove, Queensland 4059, Australia
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/ John D. Hooper
  • 7Institute of Health and Biomedical Innovation, Queensland University of Technology, 6 Musk Avenue, Kelvin Grove, Queensland 4059, Australia
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Published Online: 2008-05-15 | DOI: https://doi.org/10.1515/BC.2008.078

Abstract

The prostate is a site of high expression of serine proteinases including members of the kallikrein-related peptidase (KLK) family, as well as other secreted and membrane-anchored serine proteinases. It has been known for some time that members of this enzyme family elicit cellular responses by acting directly on cells. More recently, it has been recognised that for serine proteinases with specificity for cleavage after arginine and lysine residues (trypsin-like or tryptic enzymes) these cellular responses are often mediated by cleavage of members of the proteinase-activated receptor (PAR) family – a four member sub-family of G protein-coupled receptors. Here, we review the expression of PARs in prostate, the ability of prostatic trypsin-like KLKs and other prostate-expressed tryptic enzymes to cleave PARs, as well as the prostate cancer-associated consequences of PAR activation. In addition, we explore the dysregulation of trypsin-like serine proteinase activity through the loss of normal inhibitory mechanisms and potential interactions between these dysregulated enzymes leading to aberrant PAR activation, intracellular signalling and cancer-promoting cellular changes.

Keywords: cancer; kallikrein-related peptidase; prostate; proteinase-activated receptor; serine proteinase

About the article

Corresponding author


Published Online: 2008-05-15

Published in Print: 2008-06-01


Citation Information: Biological Chemistry, Volume 389, Issue 6, Pages 653–668, ISSN (Online) 14374315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2008.078.

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