Effects of ammonia on human neutrophil N-formyl chemotactic peptide receptor-ligand interaction and cytoskeletal association

Abstract

Ammonia is a bacterial metabolite which is commonly used to alter cytoplasmic and lysosomal pH of eukaryotic cells. Here we examine its effect on external N-formyl peptide receptors of human neutrophils. Ammonia does not affect the number of N-formyl peptide receptors on the cell surface, nor the association of the ligand-receptor complex with the cytoskeleton. However, ammonia causes a marked decrease in the affinity of the chemotactic peptide receptor for its ligand. The Kd of untreated cell for the chemotactic peptide was 0.65 ± 0.06 nM, whereas that of ammonia treated cells was 1.02 ± 0.10 nM (Mean ± SEM, N = 6). These results suggest that ammonia can affect external as well as internal cellular components. Since ammonia is used to alter lysosomal and cytoplasmic pH, and is a metabolite of common bacterial pathogens, these results bear directly on its use in cell biology and on its potential as a virulence factor.