Interactions of 12-lipoxygenase with phospholipase A2isoforms following platelet activation through the glycoprotein VI collagen receptor
| Autor: | Paula Claire Williams, Barbara Coles, Valerie B. O'Donnell, Alexandra Bermudez-Fajardo, Marcus Jonathan Coffey, Matthew Locke, Gavin E. Jarvis |
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| Rok vydání: | 2004 |
| Předmět: |
Blood Platelets
Receptors Collagen 12-Lipoxygenase Eicosatetraenoic acid Blotting Western Biophysics Platelet Membrane Glycoproteins Arachidonate 12-Lipoxygenase Glycoprotein VI Biochemistry Phospholipases A Collagen receptor 03 medical and health sciences chemistry.chemical_compound Lipoxygenase 0302 clinical medicine Phospholipase A2 Structural Biology Genetics Humans Protein Isoforms Platelet Platelet activation Molecular Biology 12-Hydro(peroxy)eicosa-tetraenoic acid 030304 developmental biology 0303 health sciences Phospholipase A biology Chemistry Cell Biology Platelet Activation Precipitin Tests 3. Good health Isoenzymes Phospholipases A2 030220 oncology & carcinogenesis biology.protein lipids (amino acids peptides and proteins) GPVI |
| Zdroj: | FEBS Letters. 576:165-168 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/j.febslet.2004.09.007 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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