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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: 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 383, Issue 7-8

Issues

Human Tissue Kallikreins: A New Enzymatic Cascade Pathway?

G. M. Yousef / E. P. Diamandis
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.2002.113

Abstract

Serine proteases are proteolytic enzymes with an active serine residue in their catalytic site. Kallikreins are a subgroup of the serine protease family which is known to have diverse physiological functions. The human kallikrein gene family has now been fully characterized and includes 15 members tandemly located on chromosome 19q13.4. Here we discuss the common structural features of kallikreins at the DNA, mRNA and protein levels and summarize their tissue expression and hormonal regulation patterns. Kallikreins are expressed in many tissues including the salivary gland, endocrine tissues such as testis, prostate, breast and endometrium, and in the central nervous system. Most genes appear to be under steroid hormone regulation. The occurrence of several splice variants is common among kallikreins, and some of the splice variants seem to be tissuespecific and might be related to certain pathological conditions. Kallikreins are secreted in an inactive zymogen form which is activated by cleavage of an Nterminal peptide. Some kalikreins can undergo autoactivation while others may be activated by other kallikreins or other proteases. Most kallikreins are predicted to have trypsinlike enzymatic activity except three which are probably chymotrypsinlike. New, but mainly circumstantial evidence, suggests that at least some kallikreins may be part of a novel enzymatic cascade pathway which is turnedon in aggressive forms of ovarian and probably other cancers.

About the article

Published Online: 2005-06-01

Published in Print: 2002-08-27


Citation Information: Biological Chemistry, Volume 383, Issue 7-8, Pages 1045–1057, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2002.113.

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