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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

Immunofluorometric activity-based probe analysis of active KLK6 in biological fluids

Katerina Oikonomopoulou
  • 1Department of Pathology and Laboratory Medicine, Mount Sinai Hospital and Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto M5T 3L9, Ontario, Canada
  • Other articles by this author:
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/ Kristina K. Hansen
  • 2Department of Pharmacology and Therapeutics, and Department of Medicine, University of Calgary, Faculty of Medicine, Calgary T2N 4N1, Alberta, Canada
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/ Amos Baruch / Morley D. Hollenberg
  • 4Department of Pharmacology and Therapeutics, and Department of Medicine, University of Calgary, Faculty of Medicine, Calgary T2N 4N1, Alberta, Canada
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/ Eleftherios P. Diamandis
  • 5Department of Pathology and Laboratory Medicine, Mount Sinai Hospital and Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto M5T 3L9, Ontario, Canada
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  • De Gruyter OnlineGoogle Scholar
Published Online: 2008-05-15 | DOI: https://doi.org/10.1515/BC.2008.086

Abstract

Immunoassay measurements of human kallikrein-related peptidases (KLKs) such as prostate-specific antigen (KLK3) are of great value as diagnostic indices of cancer. Despite extensive knowledge of the abundance of immunoreactive KLKs in normal and cancer-related settings, there is little information available about the proportion of immunoreactive KLK that represents active enzyme in such samples. Using KLK6 as a prototype enzyme, we have developed an assay using a serine proteinase-targeted activity-based probe coupled to antibody capture. By employing activity-based labeling, we were able to quantify the proportion of enzymatically active relative to total immunoreactive KLK6 in crude cerebrospinal fluid from routine analyses and ascites fluid from ovarian cancer patients, as well as in supernatants from cancer cell lines. Our approach allowed monitoring of pro-KLK6 conversion to its active enzyme species and demonstrated that up to 5% of immunoreactive KLK6 detected in clinical samples represents active enzyme. We suggest that this new activity-based probe assay will prove of value as a complement to routine KLK immunoassay measurements for validating KLKs as cancer biomarkers.

Keywords: activity-based probes; ascites fluid; cerebrospinal fluid; human kallikrein-related peptidases; serine proteinases; trypsin-like activity

About the article

Corresponding author


Received: 2007-12-11

Accepted: 2008-02-18

Published Online: 2008-05-15

Published in Print: 2008-06-01


Citation Information: Biological Chemistry, Volume 389, Issue 6, Pages 747–756, ISSN (Online) 14374315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2008.086.

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