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

Abstract : 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.
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https://hal.archives-ouvertes.fr/hal-00820790
Contributor : Marie-Claire Dagher Connect in order to contact the contributor
Submitted on : Monday, May 6, 2013 - 4:17:01 PM
Last modification on : Monday, November 8, 2021 - 11:56:01 AM

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

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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, Wiley, 1996, 239 (2), pp.369-75. ⟨hal-00820790⟩

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