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Papers In Press, published online ahead of print May 28, 2003
Department of Rheumatology and Inflammation Research, University of Goteborg, Göteborg S-413 46
Corresponding Author: Claes.Dahlgren{at}microbio.gu.se
In neutrophils, coupling of chemoattractants to their cell-surface receptor at low temperature (=15oC) leads to receptor deactivation/desensitization without any triggering of the superoxide anion-generating NADPH-oxidase. We show that the deactivated formyl peptide receptors (FPRs) can be reactivated/resensitized by the cytoskeleton-disrupting drug cytochalasin B. Such cytoskeleton-dependent receptor reactivation occurs also with the closely related receptors FPR like-1 and C5aR, but not with the receptors for interleukin-8 and platelet activating factor. The reactivation state was further characterized with FPR as a model. The signals generated by receptor reactivation induced superoxide production that was terminated in 5-8 min, after which the neutrophils entered a new state of homologous deactivation. FPR antagonists were potent inhibitors of the superoxide production induced by the reactivated receptors, suggesting that the occupied receptors turn into an actively signaling state when the cytoskeleton is disrupted. The signals generated by the reactivated receptor were pertussis toxin-sensitive, indicating involvement of a G-protein. However, no transient elevation of intracellular Ca2+ accompanies the NADPH-oxidase activation. This was not due to a general down-regulation of phospholipase C/Ca2+ signaling, and despite the fact that no intracellular Ca2+ transient was generated, protein kinase C still appeared to be involved in the response. Further, phosphatidylinositol 3-kinase, mitogen-activated protein kinase (p38 MAPK) and MEK (the MAPK/ERK kinase) all participated in the generation of second messengers from the reactivated receptors.
J. Biol. Chem, 10.1074/jbc.M209202200
Submitted on September 9, 2002
Revised on May 23, 2003
Accepted on May 28, 2003
Reactivation of formyl peptide receptors triggers the neutrophil NADPH-oxidase but not a transient rise in intracellular calcium
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