Receptor binding of guinea pig and pig vasoactive intestinal peptides by rat lung

Guinea pig vasoactive intestinal peptide (gpVIP) differs from other mammalian VIPs in four of its 28 amino acid residues. In the present study, the gpVIP displaced 125I-labelled pig VIP (pVIP) binding by rat lung membranes with 7.7-fold lower potency than pVIP. Degradation of gpVIP by rat lung membr...

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Bibliographic Details
Published inBiochemical journal Vol. 254; no. 2; pp. 613 - 615
Main Authors Paul, S, Volle, D J, Currie, J
Format Journal Article
LanguageEnglish
Published England 01.09.1988
Subjects
Animals
Binding, Competitive
Cell Membrane - metabolism
Guinea Pigs
lung
Lung - metabolism
Radioimmunoassay
Rats
Rats, Inbred Strains
Receptors, Gastrointestinal Hormone - metabolism
Receptors, Vasoactive Intestinal Peptide
Swine
Vasoactive Intestinal Peptide - metabolism
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Summary:Guinea pig vasoactive intestinal peptide (gpVIP) differs from other mammalian VIPs in four of its 28 amino acid residues. In the present study, the gpVIP displaced 125I-labelled pig VIP (pVIP) binding by rat lung membranes with 7.7-fold lower potency than pVIP. Degradation of gpVIP by rat lung membranes, assessed by radioimmunoassay and h.p.l.c., was 1.9-fold greater than that of pVIP. This difference in degradation of the two peptides was not large enough to account for the lower receptor-binding potency of gpVIP. The amino acid residues that distinguish pVIP from gpVIP are likely to contribute to the interaction of VIP with receptors and peptide hydrolases in lung membranes.
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ISSN:0264-6021
1470-8728
DOI:10.1042/bj2540613