Document Detail


Effects of potent bombesin antagonist on exocrine pancreatic secretion in rats.
MedLine Citation:
PMID:  1717952     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Recent synthesis of specific, potent bombesin receptor antagonists allows examination of the role of bombesin-like peptides in physiological processes in vivo. We characterized effects of [D-Phe6]bombesin(6-13)-methyl-ester (BME) on pancreatic enzyme secretion stimulated by the C-terminal decapeptide of gastrin releasing peptide (GRP-10), food intake, and diversion of bile-pancreatic juice in rats. In isolated pancreatic acini, BME had no agonistic effects on amylase secretion but competitively inhibited responses to GRP-10, yielding a pA2 value of 8.89 +/- 0.19. In conscious rats with gastric, jugular vein, bile-pancreatic, and duodenal cannulas, basal enzyme secretion (bile-pancreatic juice recirculated) was not affected by the antagonist. Maximal amylase response to GRP-10 (0.5 nmol/kg/h) was inhibited dose dependently by BME, reaching 97% inhibition at a dose of 400 nmol/kg/h. The dose response curve of amylase secretion stimulated by GRP-10 was shifted to the right by 40 nmol/kg/h BME, but maximal amylase response was unaltered, suggesting competitive inhibition in vivo. Liquid food intake and bile-pancreatic juice diversion caused substantial increases in amylase secretion; neither response was altered during administration of 400 pmol/kg/h BME. These results demonstrate that BME is a potent, competitive antagonist of pancreatic responses to bombesin-like peptides in vitro and in vivo. Lack of effect of BME on basal pancreatic secretion or responses to liquid food intake or diversion of bile-pancreatic juice in rats suggests that endogenous bombesin-like peptides do not act either directly or indirectly to mediate these responses.
Authors:
G Varga; R D Reidelberger; R M Liehr; L J Bussjaeger; D H Coy; T E Solomon
Publication Detail:
Type:  In Vitro; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Peptides     Volume:  12     ISSN:  0196-9781     ISO Abbreviation:  Peptides     Publication Date:    1991 May-Jun
Date Detail:
Created Date:  1991-10-31     Completed Date:  1991-10-31     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  8008690     Medline TA:  Peptides     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  493-7     Citation Subset:  IM    
Affiliation:
Department of Medicine, Kansas University Medical Center, Kansas City 66103.
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MeSH Terms
Descriptor/Qualifier:
Amylases / secretion
Animals
Biliopancreatic Diversion
Bombesin / analogs & derivatives*,  antagonists & inhibitors*,  pharmacology
Eating
Male
Pancreas / drug effects*,  enzymology,  secretion
Peptide Fragments / pharmacology*
Rats
Rats, Inbred Strains
Receptors, Bombesin
Receptors, Neurotransmitter / drug effects,  physiology
Grant Support
ID/Acronym/Agency:
CA 45153/CA/NCI NIH HHS
Chemical
Reg. No./Substance:
0/Peptide Fragments; 0/Receptors, Bombesin; 0/Receptors, Neurotransmitter; 130800-38-3/bombesin (6-13), Phe(6) methyl ester-; 31362-50-2/Bombesin; 81608-30-2/neuromedin C; EC 3.2.1.-/Amylases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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