In vitro activation of the NADPH oxidase by fluoride. Possible involvement of a factor activating GTP hydrolysis on Rac (Rac-GAP). - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue European Journal of Biochemistry Année : 1996

In vitro activation of the NADPH oxidase by fluoride. Possible involvement of a factor activating GTP hydrolysis on Rac (Rac-GAP).

J. Wölfl
  • Fonction : Auteur
M. Geiszt
  • Fonction : Auteur
E. Ligeti
  • Fonction : Auteur

Résumé

The possible mechanism of activation of the NADPH oxidase by fluoride was investigated in the cell-free system. It is shown that the stimulatory effect of fluoride is inhibited by guanosine 5'-O-(2-thiodiphosphate) (GDP[S]) and potentiated by GTP. The effect of fluoride is not additive with GTP[S]. Fluoride activation requires the presence of Mg2+ in millimolar concentration but is independent of Al3+. The activating effect of fluoride is preserved in solubilized membrane extract after removal of the majority of heterotrimeric GTP-binding proteins by immunoadsorption. Fluoride has no direct action either on the nucleotide exchange of GTP hydrolysis of the isolated Rac protein. In contrast, fluoride effectively inhibits Rac-GTPase activity enhanced by a membrane component. In this way, fluoride could prolong the prevalence of Rac in the GTP-bound state and, as a consequence, activate NADPH oxidase. The possibility of the involvement of a membrane-bound Rac GTPase-activating protein activity in the physiological regulation of the enzyme is raised.

Domaines

Immunité innée
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Dates et versions

hal-00820790 , version 1 (06-05-2013)

Identifiants

  • HAL Id : hal-00820790 , version 1
  • PUBMED : 8706742

Citer

J. Wölfl, M. C. Dagher, Alexandra Fuchs, M. Geiszt, E. Ligeti. In vitro activation of the NADPH oxidase by fluoride. Possible involvement of a factor activating GTP hydrolysis on Rac (Rac-GAP).. European Journal of Biochemistry, 1996, 239 (2), pp.369-75. ⟨hal-00820790⟩

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