Jump to ContentJump to Main Navigation
Show Summary Details

Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

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

12 Issues per year


IMPACT FACTOR 2015: 2.710
Rank 142 out of 289 in category Biochemistry & Molecular Biology in the 2015 Thomson Reuters Journal Citation Report/Science Edition

SCImago Journal Rank (SJR) 2015: 1.607
Source Normalized Impact per Paper (SNIP) 2015: 0.751
Impact per Publication (IPP) 2015: 2.609

Online
ISSN
1437-4315
See all formats and pricing
Volume 387, Issue 6 (Jun 2006)

Issues

Human kallikrein 4: enzymatic activity, inhibition, and degradation of extracellular matrix proteins

Chistina V. Obiezu
  • Department of Pathology and Laboratory Medicine, Mount Sinai Hospital, 600 University Avenue, Toronto M5G 1X5, ON, Canada and Department of Laboratory Medicine and Pathobiology, University of Toronto, 100 College Street, Toronto M5G 1L5, ON, Canada
/ Iacovos P. Michael
  • Department of Pathology and Laboratory Medicine, Mount Sinai Hospital, 600 University Avenue, Toronto M5G 1X5, ON, Canada and Department of Laboratory Medicine and Pathobiology, University of Toronto, 100 College Street, Toronto M5G 1L5, ON, Canada
/ Michael A. Levesque
  • Department of Pathology and Laboratory Medicine, Mount Sinai Hospital, 600 University Avenue, Toronto M5G 1X5, ON, Canada
/ Eleftherios P. Diamandis
  • Department of Pathology and Laboratory Medicine, Mount Sinai Hospital, 600 University Avenue, Toronto M5G 1X5, ON, Canada and Department of Laboratory Medicine and Pathobiology, University of Toronto, 100 College Street, Toronto M5G 1L5, ON, Canada
Published Online: 2006-06-26 | DOI: https://doi.org/10.1515/BC.2006.094

Abstract

Human kallikrein 4 (hK4) is a member of the expanded family of human kallikreins, a group of 15 secreted proteases. While this protein has been associated with ovarian and prostate cancer prognosis, only limited functional information exists. Therefore, we have undertaken an investigation of its enzymatic properties regarding substrate preference, degradation of extracellular matrix proteins, and its inhibition by various inhibitors. We successfully expressed and purified active recombinant hK4 from supernatants of the Pichia pastoris expression system. This enzyme seems to cleave more efficiently after Arg compared to Lys at the P1 position and exhibits modest specificity for amino acids at positions P2 and P3. hK4 forms complexes with α1-antitrypsin, α2-antiplasmin and α2-macroglobulin. The protease mediates limited degradation of extracellular matrix proteins such as collagen I and IV, and more efficient degradation of the α-chain of fibrinogen. The cleavage of extracellular matrix proteins by hK4 suggests that this enzyme may play a role in tissue remodeling and cancer metastasis.

Keywords: cancer metastasis; extracellular matrix; human kallikrein 4; ovarian cancer; prognostic markers; prostate cancer; serine protease; serine protease inhibitors

References

About the article

Corresponding author


Received: November 11, 2005

Accepted: February 14, 2006

Published Online: 2006-06-26

Published in Print: 2006-06-01


Citation Information: Biological Chemistry, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2006.094. Export Citation

Citing Articles

Here you can find all Crossref-listed publications in which this article is cited. If you would like to receive automatic email messages as soon as this article is cited in other publications, simply activate the “Citation Alert” on the top of this page.

[1]
Tunjung Mahatmanto
Biopolymers, 2015, Volume 104, Number 6, Page 804
[2]
Ruth Anna Fuhrman-Luck, Munasinghage Lakmali Silva, Ying Dong, Helen Irving-Rodgers, Thomas Stoll, Marcus Lachlan Hastie, Daniela Loessner, Jeffrey John Gorman, and Judith Ann Clements
PROTEOMICS - Clinical Applications, 2014, Volume 8, Number 5-6, Page 403
[3]
Daniela Loessner, Stefan Kobel, Judith Clements, Matthias Lutolf, and Dietmar Hutmacher
Microarrays, 2013, Volume 2, Number 3, Page 208
[4]
Hasmik Shahinian, Daniela Loessner, Martin L. Biniossek, Jayachandran N. Kizhakkedathu, Judith A. Clements, Viktor Magdolen, and Oliver Schilling
Molecular Oncology, 2014, Volume 8, Number 1, Page 68
[5]
John D. Bartlett
ISRN Dentistry, 2013, Volume 2013, Page 1
[6]
Daniela Loessner, Simone C. Rizzi, Kathryn S. Stok, Tobias Fuehrmann, Brett Hollier, Viktor Magdolen, Dietmar W. Hutmacher, and Judith A. Clements
Biomaterials, 2013, Volume 34, Number 30, Page 7389
[7]
Nashmil Emami and Eleftherios P. Diamandis
Clinica Chimica Acta, 2007, Volume 381, Number 1, Page 78
[8]
Nashmil Emami and Eleftherios P. Diamandis
Molecular Oncology, 2007, Volume 1, Number 3, Page 269
[9]
Michael Blaber, Hyesook Yoon, Maria A. Juliano, Isobel A. Scarisbrick, and Sachiko I. Blaber
Biological Chemistry, 2010, Volume 391, Number 4
[10]
Peter Goettig, Viktor Magdolen, and Hans Brandstetter
Biochimie, 2010, Volume 92, Number 11, Page 1546
[11]
Ignacio Blanco, Beatriz Lara, and Frederick de Serres
Orphanet Journal of Rare Diseases, 2011, Volume 6, Number 1, Page 14
[12]
Joakim E. Swedberg, Laura V. Nigon, Janet C. Reid, Simon J. de Veer, Carina M. Walpole, Carson R. Stephens, Terry P. Walsh, Thomas K. Takayama, John D. Hooper, Judith A. Clements, Ashley M. Buckle, and Jonathan M. Harris
Chemistry & Biology, 2009, Volume 16, Number 6, Page 633
[13]
Julie L.V. Shaw and Eleftherios P. Diamandis
Biological Chemistry, 2008, Volume 389, Number 11
[14]
Nicolle Kränkel and Paolo Madeddu
Expert Review of Cardiovascular Therapy, 2009, Volume 7, Number 3, Page 215
[15]
Mari Kaarbø, Tove I. Klokk, and Fahri Saatcioglu
BioEssays, 2007, Volume 29, Number 12, Page 1227

Comments (0)

Please log in or register to comment.
Log in