Jump to ContentJump to Main Navigation

Clinical Chemistry and Laboratory Medicine (CCLM)

Published in Association with the European Federation of Clinical Chemistry and Laboratory Medicine (EFLM)

Editor-in-Chief: Plebani, Mario

Ed. by Gillery, Philippe / Lackner, Karl J. / Lippi, Giuseppe / Melichar, Bohuslav / Schlattmann, Peter / Tate, Jillian R. / Tsongalis, Gregory J.

12 Issues per year


IMPACT FACTOR 2014: 2.707
Rank 6 out of 30 in category Medical Laboratory Technology in the 2014 Thomson Reuters Journal Citation Report/Science Edition

SCImago Journal Rank (SJR) 2014: 0.741
Source Normalized Impact per Paper (SNIP) 2014: 1.011
Impact per Publication (IPP) 2014: 2.310

VolumeIssuePage

Issues

Annexin V and Phospholipid Metabolism

Françoise Russo-Marie

Citation Information: Clinical Chemistry and Laboratory Medicine. Volume 37, Issue 3, Pages 287–291, ISSN (Print) 1434-6621, DOI: 10.1515/CCLM.1999.050, June 2005

Publication History

Published Online:
2005-06-01

Abstract

Annexins, protein kinases C and cytosolic phospholipase A2 belong to three families of ubiquitous cytoplasmic proteins involved in signal transduction. All annexins share the property of binding to phospholipids in the presence of calcium. Most annexins are substrates for protein kinases C except annexin V, the most ubiquitous and abundant annexin. Protein kinases C (PKC) belong to three distinct groups of kinases, conventional PKCs (cPKCs) that depend on calcium, diacylglycerol and negatively charged phospholipids for their activity, novel PKCs (nPKCs) and atypical PKCs (aPKCs), that do not require calcium for their activity, although they both require negatively charged phospholipids. Cytosolic phospholipase A2 (cPLA2) depends on calcium for its catalytic activity as well as on serine phosphorylation by MAP kinases. We report that annexin V modulates the activity of cPKCs as well as of cPLA2 by interfering with their ability to bind to negatively charged phospholipids and calcium. We propose that annexin V could interfere with the calcium and phospholipid signalling pathway.

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]
Xiang-Shun Cui, Xing-Hui Shen, Chang-Kwon Lee, Yong-Kook Kang, Teruhiko Wakayama, and Nam-Hyung Kim
Stem Cell Discovery, 2011, Volume 01, Number 01, Page 1
[2]
Christopher M.L.S. Bouton, Mir Ahamed Hossain, Laurence P. Frelin, John Laterra, and Jonathan Pevsner
Toxicology and Applied Pharmacology, 2001, Volume 176, Number 1, Page 34
[3]
Monira Hoque, Carles Rentero, Rose Cairns, Francesc Tebar, Carlos Enrich, and Thomas Grewal
Cellular Signalling, 2014, Volume 26, Number 6, Page 1213
[4]
Joanna Bandorowicz-Pikula, Marcin Wos, and Slawomir Pikula
Molecular Membrane Biology, 2012, Volume 29, Number 7, Page 229
[5]
Norman F Neumann and Fernando Galvez
Biotechnology Advances, 2002, Volume 20, Number 5-6, Page 391
[6]
Mikkel H. Andersen, Lars Berglund, Torben E. Petersen, and Jan T. Rasmussen
Biochemical and Biophysical Research Communications, 2002, Volume 292, Number 2, Page 550
[7]
Bent Brachvogel, Heike Welzel, Helga Moch, Klaus von der Mark, Clementine Hofmann, and Ernst Pöschl
Mechanisms of Development, 2001, Volume 109, Number 2, Page 389
[8]
Abdelnaby Khalyfa, Carolyn M Klinge, William C Hall, Xuechun Zhao, Marilyn M Miller, and Eugenia Wang
Experimental Gerontology, 2003, Volume 38, Number 10, Page 1087
[9]
Joseph I Kourie and Harold B Wood
Progress in Biophysics and Molecular Biology, 2000, Volume 73, Number 2-4, Page 91
[10]
Daniel Martins-de-Souza, Maria Lebar, and Christoph W. Turck
European Archives of Psychiatry and Clinical Neuroscience, 2011, Volume 261, Number 3, Page 217
[11]
Joanna Bandorowicz-Pikula, Rene Buchet, and Slawomir Pikula
BioEssays, 2001, Volume 23, Number 2, Page 170

Comments (0)

Please log in or register to comment.