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Volume 271, Number 25, Issue of June 21, 1996 pp. 15267-15271
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Direct or C5a-induced Activation of Heterotrimeric G_i2 Proteins in Human Neutrophils Is Associated with Interaction between Formyl Peptide Receptors and the Cytoskeleton

(Received for publication, September 18, 1995, and in revised form, February 21, 1996)

Eva Särndahl , Gary M. Bokoch ^¶ , François Boulay , Olle Stendahl ^'' and Tommy Andersson

From the Departments of  Cell Biology and ^'' Medical Microbiology, Linköping University, S-581 85 Linköping, Sweden, the ^¶ Departments of Immunology and Cell Biology, Research Institute of Scripps Clinic, La Jolla, California 92037, and  DBMS/Laboratoire de Biochimie, CEA-Grenoble, 17 rue des Martyrs, 38054 Grenoble Cedex 9, France

The binding of ligands to N-formyl peptide chemoattractant receptors in human neutrophils results in a rapid association of these receptors with a cytoskeletal fraction and a specific activation and release of G_i2 -subunits from this fraction. In the present study we could show that pretreating neutrophils with GDPS prevented the fMet-Leu-Phe-induced association of its receptor with a cytoskeletal fraction and also blocked the release of G_i2 -subunits from the same cytoskeletal fraction. In contrast, direct activation of G_i2 proteins by addition of GTPS or AlF₄ not only caused a release of G_i2 -subunits from the cytoskeleton but also an association of formyl peptide receptors with the cytoskeleton. The receptor for complement fragment 5a, which transduces its signaling through the same G_i2 protein, triggers both a release of G_i2 -subunits from the cytoskeleton fraction and, of even greater interest, an association between formyl peptide receptors and the cytoskeleton. The close relationship between the activation and release of G_i2 -subunits from the cytoskeleton and the association of formyl peptide receptors with the cytoskeleton might, however, not be a matter of protein-protein exchange, since the increased binding of formyl peptide receptors to the cytoskeleton occurs more rapidly than the release of G_i2 -subunits from the cytoskeleton. The present findings suggest a possible mechanism for the initiation of formyl peptide receptor desensitization during neutrophil locomotion.

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