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- Title
Interactions of 12-lipoxygenase with phospholipase A<sub>2</sub> isoforms following platelet activation through the glycoprotein VI collagen receptor
- Authors
Coffey, Marcus J.; Coles, Barbara; Locke, Matthew; Bermudez-Fajardo, Alexandra; Williams, P. Claire; Jarvis, Gavin E.; O'Donnell, Valerie B.
- 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.
- Subjects
COLLAGEN; TOXINS; ANTIGENS; METABOLITES
- Publication
FEBS Letters, 2004, Vol 576, Issue 1/2, p165
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2004.09.007