Abstract
In this paper, we investigated the subcellular distribution of p190rho guanosine triphosphatase-activating protein (p190 GAP) in human neutrophils stimulated with different agonists. The results show that in neutrophils treated with formyl-methionyl-leucyl-phenylalanine (FMLP) (1) p190 GAP was translocated from the cytosol to the membranes; (2) the translocation of p190 GAP took place only at doses of FMLP that induced the translocation of rac 1 and rac 2 and the activation of the NADPH oxidase; and (3) the kinetic of translocation of p190 GAP paralleled that of rac 1 and rac 2. However, when the agonist was concanavalin A (ConA) or phorbol 12-myristate 13-acetate (PMA), rac 1 and rac 2, but not the p190 GAP, were translocated.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Cell Membrane / metabolism
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Concanavalin A / pharmacology
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Cytosol / metabolism
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Enzyme Activation
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Guanine Nucleotide Exchange Factors*
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Humans
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In Vitro Techniques
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Kinetics
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N-Formylmethionine Leucyl-Phenylalanine / pharmacology*
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NADH, NADPH Oxidoreductases / blood
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NADPH Oxidases
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Neutrophils / drug effects
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Neutrophils / metabolism*
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Nuclear Proteins / metabolism*
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Oxygen Consumption
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Phosphoproteins / metabolism*
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Repressor Proteins
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Tetradecanoylphorbol Acetate / pharmacology*
Substances
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ARHGAP35 protein, human
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Guanine Nucleotide Exchange Factors
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Nuclear Proteins
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Phosphoproteins
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Repressor Proteins
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Concanavalin A
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N-Formylmethionine Leucyl-Phenylalanine
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NADH, NADPH Oxidoreductases
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NADPH Oxidases
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Tetradecanoylphorbol Acetate