A chemotactic receptor for val(ala)-gly-ser-glu on human.

Abstract

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.

• Authors: R N Boswell, K F Austen, E J Goetzl
• Journal: Immunological communications (Immunol Commun) Vol. 5 Issue 6 Pg. 469-79 ( 1976) ISSN: 0090-0877 [Print] United States
• PMID: 992702 (Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Receptors, Drug
• Glutamine
• Serine
• Valine
• Alanine
• Glycine

Topics

• Alanine
• Chemotaxis, Leukocyte
• Eosinophils (immunology)
• Glutamine
• Glycine
• Receptors, Drug (immunology)
• Serine
• Valine