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Enhancement of protein kinase C-dependent O2 (bar dot) production in Epstein-Barr virus-transformed B lymphocytes by p120(Ras-GAP) antisense oligonucleotide

Academic Article
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Overview

authors

  • Schmid, E.
  • Koziol, James
  • Babior, Bernard Macy

publication date

  • April 1996

journal

  • Journal of Biological Chemistry  Journal

abstract

  • The mammalian Ras GTPase-activating protein (p120Ras-GAP) interacts with activated members of the Ras superfamily of GTP-binding proteins to accelerate their deactivation by sharply increasing their rates of GTP hydrolysis. Among the Ras-family proteins interacting with p120Ras-GAP is Rap1A/Krev1, whose activity is not affected by p120Ras-GAP but which competes with Ras for p120Ras-GAP. A second protein that interacts with p120Ras-GAP is P190Rac-GAP, which activates the GTPase of guanine nucleotide-binding proteins of the Rho family (including Rac1 and Rac2). Both these p120Ras-GAP-binding proteins are of interest in connection with the regulation of the respiratory burst oxidase, Rap1A/Krev1 because it copurifies with cytochrome b558 and p190Ras-GAP because it inhibits the Rac2-dependent activation of the respiratory burst oxidase in a cell-free system. Using an 18-mer antisense oligonucleotide, we were able to decrease the expression of p120Ras-GAP in Epstein-Barr virus-transformed B lymphocytes. Under conditions where p120Ras-GAP expression was significantly depressed by antisense oligonucleotides, we observed a 40% increase in protein kinase C-dependent but not receptor-dependent O2 production. In contrast, sense and scrambled oligonucleotides had no effect on either p120Ras-GAP expression or O2 production. Our results suggest a role for p120Ras-GAP as a negative regulator in the protein kinase C-mediated activation of the respiratory burst oxidase.

subject areas

  • B-Lymphocytes
  • Base Sequence
  • Cell Line
  • Cell Transformation, Viral
  • Enzyme Inhibitors
  • GTP-Binding Proteins
  • GTPase-Activating Proteins
  • Herpesvirus 4, Human
  • Humans
  • Ionomycin
  • Kinetics
  • Molecular Sequence Data
  • NADH, NADPH Oxidoreductases
  • NADPH Oxidase
  • Oligonucleotides, Antisense
  • Protein Kinase C
  • Proteins
  • Superoxides
  • Tetradecanoylphorbol Acetate
  • Time Factors
  • rac GTP-Binding Proteins
  • ras GTPase-Activating Proteins
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

PubMed ID

  • 8621595
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Additional Document Info

start page

  • 9320

end page

  • 9325

volume

  • 271

issue

  • 16

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