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 2013: 2.955
Rank 5 out of 29 in category Medical Laboratory Technology in the 2013 Thomson Reuters Journal Citation Report/Science Edition

SCImago Journal Rank (SJR): 0.860
Source Normalized Impact per Paper (SNIP): 1.046



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:


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.

Comments (0)

Please log in or register to comment.