Abstract
In this paper, we show that the p125 ras guanosine triphosphatase-activating protein (p125 GAP) is present in the cytosol of human neutrophils and is transiently tyrosine phosphorylated and translocated to the membranes upon cell activation with formyl-methionyl-leucyl-phenylalanine (FMLP). When concanavalin A (ConA) or phorbol 12-myristate 13-acetate (PMA), which both induced a long-lasting respiratory burst, were used as stimuli, tyrosine phosphorylation and translocation of p125 GAP did not occur.
Publication types
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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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GTPase-Activating Proteins
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Humans
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Kinetics
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N-Formylmethionine Leucyl-Phenylalanine / pharmacology*
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Neutrophils / drug effects
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Neutrophils / physiology*
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Phosphorylation
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Phosphotyrosine / analysis
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Proteins / analysis
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Proteins / isolation & purification
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Proteins / metabolism*
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Respiratory Burst / physiology
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Subcellular Fractions / metabolism
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Tetradecanoylphorbol Acetate / pharmacology
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Tyrosine / metabolism
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ras GTPase-Activating Proteins
Substances
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GTPase-Activating Proteins
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Proteins
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ras GTPase-Activating Proteins
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Concanavalin A
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Phosphotyrosine
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Tyrosine
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N-Formylmethionine Leucyl-Phenylalanine
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Tetradecanoylphorbol Acetate