Eosinophil Chemotactic Peptide Sequences in Rat α-CGRP: Activation of a Novel Trophic Action by Neutral Endopeptidase 24.11

• Published in: Annals of the New York Academy of Sciences 1992-06, Vol.657 (1), p.405-411
• Main Authors: DAVIES, DAWN, MEDEIROS, MARGARET S., KEEN, JEFF, TURNER, ANTHONY J., HAYNES, LAURENCE W.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Analysis of Variance; Animals; Calcitonin Gene-Related Peptide - chemistry; Calcitonin Gene-Related Peptide - metabolism; Calcitonin Gene-Related Peptide - pharmacology; Chemotaxis, Leukocyte - drug effects; Eosinophils - drug effects; Eosinophils - physiology; Lymphokines - chemistry; Lymphokines - metabolism; Molecular Sequence Data; Neprilysin - metabolism; Peptide Fragments - pharmacology; Rats; Sequence Homology, Nucleic Acid; Substrate Specificity
• ISSN: 0077-8923; 1749-6632
• DOI: 10.1111/j.1749-6632.1992.tb22786.x

Rat alpha- and alpha-CGRP are substrates for endopeptidase 24.11 in vitro. Cleavage of both peptides occurs at several points, including an unusual substrate recognition site to the amino side of ala36. In alpha-CGRP this resulted in the early formation of val32-gly-ser-glu35, a sequence previously reported to be a component of the eosinophil chemotactic factor of anaphylaxis (ECF-A). The biological activity of this peptide fragment was confirmed by bioassay. Chemotactic activity in other hydrolysis fragments of both alpha- and beta-CGRP was observed. Both alpha- and beta-CGRP could thus serve as precursors to different eosinophil chemotactic peptide fragments. A novel function of endopeptidase 24.11 may be to modify rather than to terminate the biological activity of CGRP peptides.