A chemotactic receptor for val(ala)-gly-ser-glu on human.
Preferential eosinophil chemotactic activity is an in vitro and in vivo property of eosinophil chemotactic factor of anaphylaxis (ECF-A), a mixture of two peptides, Val-Gly-Ser-Glu and Ala-Gly-Ser-Glu, isolated from extracts and anaphylactic diffusates of human lung tissue. Purified native and synthetic ECF-A share with the synthetic N-formyl methionyl peptides such features as in vitro activity in nanomolar amounts, high dose inhibition of effect and a requirement for hydrophobic amino acid residues. The capacity of the substituents of ECF-A, Val-Gly-Ser, Ala-Gly-Ser, and Gly-Ser-Glu to modulate eosinophil chemotaxis has permitted a preliminary functional characterization of an eosinophil surface receptor. The activity, specificity, and structural characteristics of the active tetrapeptides suggest that distinct interactions of the peptide with a stereospecific receptor on the eosinophil surface is required for chemotactic movement.
D000409:Alanine; D002634:Chemotaxis, Leukocyte; D004804:Eosinophils / Q000276:immunology*; D005973:Glutamine; D005998:Glycine; D011955:Receptors, Drug / Q000276:immunology*; D012694:Serine; D014633:Valine
D011955:Receptors, Drug; D005973:Glutamine; D012694:Serine; D014633:Valine; D000409:Alanine; D005998:Glycine