Abstract
Vanadate (V) potentiated (4- to 10-fold) the activation of cellular phospholipase A2 (PLA2) induced by H2O2 (H), a phorbol ester (T), a Ca(2+)-ionophore (A) and opsonized zymosan in macrophages. V+H induced in intact cells the activation and translocation of PLA2 and protein kinase C (PKC) to the plasma membrane. V+H and V+T+A induced strong chemiluminescence (CL) which was abrogated by a specific NADPH oxidase inhibitor diphenylene iodonium (DPI). DPI markedly suppressed the stimulation of PLA2 by V+T+A and V+OZ. The results suggest that the formation of endogenous reactive oxygen species (ROS) is important for PLA2 activation.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Enzyme Activation
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Female
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Hydrogen Peroxide / pharmacology
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Macrophages / drug effects
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Macrophages / metabolism
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Mice
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Mice, Inbred Strains
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NADH, NADPH Oxidoreductases / antagonists & inhibitors
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NADH, NADPH Oxidoreductases / metabolism
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NADPH Oxidases
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Onium Compounds / pharmacology
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Oxygen / metabolism*
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Phospholipases A / metabolism*
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Phospholipases A2
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Protein Kinase C / metabolism
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Protein-Tyrosine Kinases / metabolism
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Vanadates / pharmacology
Substances
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Onium Compounds
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Vanadates
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diphenyleneiodonium
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Hydrogen Peroxide
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NADH, NADPH Oxidoreductases
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NADPH Oxidases
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Protein-Tyrosine Kinases
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Protein Kinase C
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Phospholipases A
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Phospholipases A2
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Oxygen