Interactions of 12-lipoxygenase with phospholipase A2 isoforms following platelet activation through the glycoprotein VI collagen receptor

Coffey, Marcus Jonathan, Coles, Barbara, Locke, Matthew, Bermudez-Fajardo, Alexandra, Williams, Paula Claire, Jarvis, Gavin E. and O'Donnell, Valerie Bridget ORCID: https://orcid.org/0000-0003-4089-8460 2004. Interactions of 12-lipoxygenase with phospholipase A2 isoforms following platelet activation through the glycoprotein VI collagen receptor. FEBS Letters 576 (1-2) , pp. 165-168. 10.1016/j.febslet.2004.09.007

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Abstract

Recent studies implicate the collagen receptor, glycoprotein VI (GPVI) in activation of platelet 12-lipoxygenase (p12-LOX). Herein, we show that GPVI-stimulated 12-hydro(peroxy)eicosatetraenoic acid (H(P)ETE) synthesis is inhibited by palmityl trifluromethyl ketone or oleyloxyethylphosphocholine , but not bromoenol lactone, implicating secretory and cytosolic, but not calcium-independent phospholipase A2 (PLA2) isoforms. Also, following GPVI activation, 12-LOX co-immunoprecipitates with both cytosolic and secretory PLA2 (sPLA2). Finally, venoms containing sPLA2 acutely activate p12-LOX in a dose-dependent manner. This study shows that platelet 12-H(P)ETE generation utilizes arachidonate substrate from both c- and sPLA2 and that 12-LOX functionally associates with both PLA2 isoforms.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Medicine Systems Immunity Research Institute (SIURI)
Uncontrolled Keywords:	Platelet; 12-Lipoxygenase; Phospholipase A2; 12-Hydro(peroxy)eicosa-tetraenoic acid; Glycoprotein VI
Publisher:	Elsevier
ISSN:	0014-5793
Last Modified:	06 May 2023 02:42
URI:	https://orca.cardiff.ac.uk/id/eprint/18

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