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Originally published In Press as doi:10.1074/jbc.M106621200 on September 14, 2001

J. Biol. Chem., Vol. 276, Issue 45, 42043-42049, November 9, 2001
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Defective Gi Protein Coupling in Two Formyl Peptide Receptor Mutants Associated with Localized Juvenile Periodontitis*

Roland Seifert and Katharina Wenzel-SeifertDagger

From the Department of Pharmacology and Toxicology, University of Kansas, Lawrence, Kansas 66045-2505

The formyl peptide receptor (FPR) is a prototypical chemoattractant receptor expressed in neutrophils. It is well known that the FPR couples to Gi proteins to activate phospholipase C, chemotaxis, and cytotoxic cell functions, but the in vivo role of the FPR in man has remained elusive. Recently, F110S and C126W mutations of the FPR have been associated with localized juvenile periodontitis. We studied FPR-F110S and FPR-C126W in comparison with wild-type FPR (FPR-WT) by coexpressing epitope-tagged versions of these receptors with the G protein Galpha i2beta 1gamma 2 in Sf9 insect cells. FPRs were efficiently expressed in Sf9 membranes as assessed by immunoblotting using the beta 2-adrenoreceptor as a standard. FPR-C126W differed from FPR-WT and FPR-F110S in migration on SDS-polyacrylamide gels and tunicamycin-sensitive glycosylation. FPR-WT efficiently reconstituted high-affinity agonist binding and agonist- and inverse agonist-regulated guanosine 5'-O-(3-thiotriphosphate) (GTPgamma S) binding to Galpha i2beta 1gamma 2. In contrast, FPR-F110S only weakly reconstituted agonist-stimulated GTPgamma S binding, and FPR-C126W was completely inefficient. Collectively, our data show almost complete and complete loss of Gi protein coupling in FPR-F110S and FPR-C126W, respectively. The severe functional defects in FPR-F110S and FPR-C126W contrast with the discrete clinical symptoms associated with these mutations, indicating that loss of FPR function in host defense is, for the most part, readily compensated.

* This work was supported by National Institutes of Health Center of Biomedical Research Excellence Award 1-P20-RR15563 and matching support from the State of Kansas and the University of Kansas.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Dept. of Pharmacology and Toxicology, University of Kansas, 5003 Malott Hall, Lawrence, KS 66045-2505. Tel. and Fax: 785-864-3536; E-mail: kwenzel@falcon.cc.ukans.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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