Enhancement of N-formyl-methionyl-leucyl-phenylalanine (fMLP) binding to isolated human neutrophils.
Short chain aliphatic alcohols have previously been found to enhance fMLP binding to human neutrophils, presumably by non-specific mechanisms involving increased membrane hydrophobicity or decreased microviscosity. We report the discovery of highly potent fMLP binding enhancers with 30,000 times the potency of the alcohols. Activity of the compounds is specific since slight changes in structure drastically alter their ability to enhance binding and since closely related compounds inhibit rather than enhance binding. The effects of experimental compounds on enhancement or inhibition of fMLP binding are paralleled by similar actions on fMLP-stimulated shape change of neutrophils.
Psychoyos
S
S
Research Department, CIBA-GEIGY Corporation, Summit, New Jersey 07901.
Smith
C W
CW
D006801:Humans; D066298:In Vitro Techniques; D007700:Kinetics; D009240:N-Formylmethionine Leucyl-Phenylalanine / Q000378:metabolism* / Q000494:pharmacology; D009504:Neutrophils / Q000166:cytology / Q000187:drug effects / Q000378:metabolism*; D044042:Receptors, Formyl Peptide; D011971:Receptors, Immunologic / Q000378:metabolism*
D044042:Receptors, Formyl Peptide; D011971:Receptors, Immunologic; D009240:N-Formylmethionine Leucyl-Phenylalanine