Characterization of the human fMLP receptor in neutrophils and in Xenopus oocytes

British Journal of Pharmacology
Sigrid WittmannStephen Daniels

Abstract

1. N-formyl peptides (e.g. fMLP; N-formyl-L-methionyl-L-leucyl-phenylalanine) are potent mediators for inflammatory reactions. We report functional expression in Xenopus oocytes of human fMLP-R98 cDNA, without co-expression of the promiscuous G-protein subunit, Galpha-16. 2. Stimulation of voltage-clamped oocytes (-70 mV) with fMLP produced a dose-dependent biphasic inward current with fast and slow components. Analysis using GTP-gamma-S and cholera and pertussis toxins suggested these currents are mediated by an endogenous G-protein of the Gq family. 3. The fast current reversed at -25 mV and was blocked by SITS (4-acetamido-4'-isothiocyanatostilbene-2,2'-disulphonic acid), suggesting the current is carried by Cl(-). The slow current showed weak inward rectification, was Ca(2+)-dependent and blocked by Cd(2+), 4-AP (4-aminopyridine) and haloperidol, suggesting activation of a mixed population of cation channels. 4. Comparative experiments with human neutrophils using flow cytometric analysis showed that the proportion of neutrophils activated by fMLP was reduced in the presence of SITS, in the absence of external calcium and in the presence of Cd(2+), TEA (tetraethylammonium) and haloperidol but not 4-AP. In addition, the oxid...Continue Reading

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Citations

Mar 29, 2003·International Journal of Pediatric Otorhinolaryngology·Małgorzata KowalskaMaria Wasik
May 7, 2015·Biomolecules·Walter StoiberWolf-Dietrich Krautgartner
Dec 8, 2005·International Immunopharmacology·Sigrid WittmannStephen Daniels
Mar 23, 2015·International Journal of Pharmaceutics·Chrysoula-Evangelia KarachaliouEvangelia Livaniou
Dec 23, 2003·The Journal of Immunology : Official Journal of the American Association of Immunologists·Kiyoshi ItagakiCarl J Hauser
Mar 2, 2011·Archives of Biochemistry and Biophysics·Haein ParkDianne Cox

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