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Evidence for N-formyl chemotactic peptide-stimulated GTPase activity in human neutrophil homogenates

Academic Article
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Overview

authors

  • Hyslop, P. A.
  • Oades, Z. G.
  • Jesaitis, A. J.
  • Painter, R. G.
  • Cochrane, Charles
  • Sklar, L. A.

publication date

  • 1984

journal

  • FEBS Letters  Journal

abstract

  • Neutrophil homogenates contained a high affinity guanosine triphosphatase (GTPase) that was stimulatable (+27%) by the addition of 100 nM N-formyl chemotactic peptide (CHO-pep), but not by 1 microgram X ml-1 phorbolmyristate acetate (PMA). Kinetic analysis of the stimulation demonstrated an apparent lagtime of 14.3 +/- 6.9 s between the addition of CHO-pep and the optimal GTPase stimulation. The GTPase activity (but not CHO-pep-stimulated GTPase activity) was preserved in a highly purified plasma membrane fraction of the homogenate. From these observations we suggest that both a high affinity guanine nucleotide binding protein and GTPase are closely associated with the plasma membrane CHO-pep receptor. The possibility that GTPase activity may influence guanine nucleotide regulation of adenylate cyclase during CHO-pep stimulation of neutrophils is discussed.

subject areas

  • Adenylyl Cyclases
  • Cell-Free System
  • GTP Phosphohydrolases
  • GTP-Binding Proteins
  • Humans
  • Kinetics
  • Neutrophils
  • Phosphoric Monoester Hydrolases
  • Receptors, Cell Surface
  • Receptors, Formyl Peptide
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Identity

International Standard Serial Number (ISSN)

  • 0014-5793

Digital Object Identifier (DOI)

  • 10.1016/0014-5793(84)80065-4

PubMed ID

  • 6141069
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Additional Document Info

start page

  • 165

end page

  • 169

volume

  • 166

issue

  • 1

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