Translocation of p190rho guanosine triphosphatase-activating protein from cytosol to the membrane in human neutrophils stimulated with different agonists

Biochem Biophys Res Commun. 1996 Feb 27;219(3):859-62. doi: 10.1006/bbrc.1996.0323.

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

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Membrane / metabolism
  • Concanavalin A / pharmacology
  • Cytosol / metabolism
  • Enzyme Activation
  • Guanine Nucleotide Exchange Factors*
  • Humans
  • In Vitro Techniques
  • Kinetics
  • N-Formylmethionine Leucyl-Phenylalanine / pharmacology*
  • NADH, NADPH Oxidoreductases / blood
  • NADPH Oxidases
  • Neutrophils / drug effects
  • Neutrophils / metabolism*
  • Nuclear Proteins / metabolism*
  • Oxygen Consumption
  • Phosphoproteins / metabolism*
  • Repressor Proteins
  • Tetradecanoylphorbol Acetate / pharmacology*

Substances

  • ARHGAP35 protein, human
  • Guanine Nucleotide Exchange Factors
  • Nuclear Proteins
  • Phosphoproteins
  • Repressor Proteins
  • Concanavalin A
  • N-Formylmethionine Leucyl-Phenylalanine
  • NADH, NADPH Oxidoreductases
  • NADPH Oxidases
  • Tetradecanoylphorbol Acetate