Characterization of membrane-localized and cytosolic Rac-GTPase-activating proteins in human neutrophil granulocytes: contribution to the regulation of NADPH oxidase. - Archive ouverte HAL
Article Dans Une Revue Biochemical Journal Année : 2001

Characterization of membrane-localized and cytosolic Rac-GTPase-activating proteins in human neutrophil granulocytes: contribution to the regulation of NADPH oxidase.

M. Geiszt
  • Fonction : Auteur
G. Molnár
  • Fonction : Auteur
A. Havasi
  • Fonction : Auteur
M. H. Paclet
  • Fonction : Auteur
F. Morel
  • Fonction : Auteur
E. Ligeti
  • Fonction : Auteur

Résumé

We have investigated the intracellular localization and molecular identity of Rac-GTPase-activating proteins (Rac-GAPs) in human neutrophils. Immunoblot analysis detected the presence of both p190RhoGAP and Bcr mainly in the cytosol. An overlay assay performed with [gamma-(32)P]GTP-bound Rac revealed dominant GAP activity related to a 50 kDa protein both in the membrane and cytosol. This activity could be identified by Western blotting and immunoprecipitation with specific antibody directed against the GAP domain of p50RhoGAP. Using a semirecombinant or fully purified cell-free activation assay of the Rac-activated enzyme NADPH oxidase, we demonstrated the regulatory effect of both the membrane-localized and soluble GAPs. We suggest that in neutrophil granulocytes Rac-GAPs have redundant function and represent suitable targets for both the up-regulation and down-regulation of the NADPH oxidase.

Domaines

Immunité innée
Fichier non déposé

Dates et versions

hal-00820778 , version 1 (06-05-2013)

Identifiants

  • HAL Id : hal-00820778 , version 1
  • PUBMED : 11311150

Citer

M. Geiszt, M. C. Dagher, G. Molnár, A. Havasi, J. Faure, et al.. Characterization of membrane-localized and cytosolic Rac-GTPase-activating proteins in human neutrophil granulocytes: contribution to the regulation of NADPH oxidase.. Biochemical Journal, 2001, 355 (Pt 3), pp.851-8. ⟨hal-00820778⟩

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