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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

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

12 Issues per year


IMPACT FACTOR 2016: 3.273

CiteScore 2016: 3.01

SCImago Journal Rank (SJR) 2016: 1.679
Source Normalized Impact per Paper (SNIP) 2016: 0.800

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1437-4315
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Volume 391, Issue 1 (Jan 2010)

Issues

Potential role of multiple members of the kallikrein-related peptidase family of serine proteases in activating latent TGFβ1 in semen

Nashmil Emami
  • Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto M5G 1L5, Ontario, Canada
  • Department of Pathology and Laboratory Medicine, Mount Sinai Hospital, Toronto M5G 1X5, Ontario, Canada
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Eleftherios P. Diamandis
  • Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto M5G 1L5, Ontario, Canada
  • Department of Pathology and Laboratory Medicine, Mount Sinai Hospital, Toronto M5G 1X5, Ontario, Canada
  • Department of Clinical Biochemistry, University Health Network, Toronto M5G 2C4, Ontario, Canada
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2009-11-17 | DOI: https://doi.org/10.1515/bc.2010.007

Abstract

Transforming growth factor β1 (TGFβ1) has been implicated as a key contributor of immunosuppression in seminal plasma. The biochemical mechanisms that lead to production of active seminal TGFβ1 are not fully understood. It is plausible that TGFβ1 activation is partly induced simultaneously with the release of motile spermatozoa following liquefaction of the semen coagulum. Several members of the kallikrein-related peptidase (KLK) family are involved in the regulation of semen liquefaction. This study examines the involvement of these KLKs in TGFβ1 activation in vitro and ex vivo, in seminal plasma. Latent TGFβ1 was rapidly activated by KLK14. The latency-associated propeptide (LAP) was shown to be cleaved by KLK14 into small peptide fragments, providing a possible mechanism for TGFβ1 activation. KLK14 also cleaved the latent TGFβ binding protein 1 (LTBP1). KLK1, 2, and 5 might also contribute to TGFβ1 activation by nicking the LAP motif and inducing conformational changes that aid in subsequent processing of LAP or through LTBP1 cleavage. Our study provides strong evidence for the involvement of multiple members of the seminal KLK cascade in activation of latent TGFβ1 in seminal plasma. These findings might have clinical implications in infertility treatment of cases with concurrent delayed liquefaction and TGFβ1-related semen antigenicity.

Keywords: immunosuppression; kallikrein-related peptidase; latency associated propeptide; semen antigenicity; semen liquefaction; seminal plasma; transforming growth factor β1 (TGFβ1)

About the article

Corresponding author


Received: 2009-03-30

Accepted: 2009-09-14

Published Online: 2009-11-17

Published in Print: 2010-01-01


Citation Information: Biological Chemistry, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/bc.2010.007.

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