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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 2017: 3.022

CiteScore 2017: 2.81

SCImago Journal Rank (SJR) 2017: 1.562
Source Normalized Impact per Paper (SNIP) 2017: 0.705

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1437-4315
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Volume 383, Issue 12

Issues

Expression of the Tissue Kallikrein-Kinin Cascade in Granulosa Cells of the Ovary

J. Plendl / C. Snyman / K.D. Bhoola
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.2002.215

Abstract

The serine protease, tissue kininogenase (kallikrein), belongs to a unique family of enzymes that cleaves the decapeptide, kallidin, from the endogenous substrate kininogen. By analysis of genealogy patterns rat KLK gene family members have been detected in ovarian luteinizing granulosa cells of both gonadotrophin treated and nontreated control rats. Recently, we demonstrated that tissue kininogenase showed intense immunolabeling in angiogenic endothelial cells isolated from bovine mature and regressing corpora lutea. Therefore, the question to answer was whether granulosa cells associated with ovarian vascularization possess the same capacity to express the kallikreinkinin cascade as do microvascular endothelial cells. As a first step, experiments were designed to determine the expression and visualization of tissue kininogenase (both active and pro forms) as well as kininogen and kinin receptors in granulosa cells of different developmental stages and segments of the ovarian follicle by immunoperoxidase assay, confocal fluorescent microscopy and in situ hybridization.

About the article

Published Online: 2005-06-01

Published in Print: 2002-12-09


Citation Information: Biological Chemistry, Volume 383, Issue 12, Pages 1917–1924, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2002.215.

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