| Literature DB >> 11311150 |
M Geiszt1, M C Dagher, G Molnár, A Havasi, J Faure, M H Paclet, F Morel, E Ligeti.
Abstract
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.Entities:
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Year: 2001 PMID: 11311150 PMCID: PMC1221803 DOI: 10.1042/bj3550851
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857