BIOMAT Database Logo BIOMAT Database Logo

Effect of a new bombesin receptor antagonist, (E)-alkene bombesin isostere, on amylase release from rat pancreatic acini. 1995

M Wada, and R Doi, and R Hosotani, and S Higashide, and T Ibuka, and H Habashita, and K Nakai, and N Fujii, and M Imamura
First Department of Surgery, Kyoto University, Japan.

The short-chain pseudopeptide, [D-Phe6, Leu13 psi (CH2NH)Leu14]bombesin(6-14) (RDI), is reported to be a potent antagonist of bombesin, and development of this type of compound has greatly contributed to the investigation of biological actions of bombesin and its related peptides. We recently synthesized (E)-alkene bombesin isostere by replacing the peptide bond with an (E)-double bond: [D-Phe6, Leu13 psi [(E)CH = CH]Leu14] bombesin(6-14) (EABI). The present study examined the effect of EABI on amylase release from rat pancreatic acini. EABI showed no agonistic activity at concentrations up to 1 microM, and RBI showed slight agonistic activity at concentrations > 10 nM. EABI caused a dose-dependent inhibition of amylase release stimulated by 0.1 nM bombesin, with an IC50 of 6.7 +/- 1.7 nM, and induced almost-complete inhibition at 0.3 microM. RDI caused a dose-dependent inhibition of amylase release, with an IC50 of 68.7 +/- 16 nM. EABI caused a parallel and rightward shift of the entire dose-response curve of bombesin-stimulated amylase release, and the degree of the shift was dependent on the concentrations of EABI. EABI (100 nM) and RDI (100 nM) inhibited amylase releases stimulated by gastrin-releasing peptide (1 nM) and neuromedin-C (1 nM). In contrast, amylase release stimulated by cholecystokinin octapeptide (0.1 nM), carbachol (10 microM), vasoactive intestinal peptide (1 nM), and gastrin-17 (10 nM) was not inhibited by EABI and RDI. The results indicate that EABI is a potent and specific bombesin receptor antagonist.(ABSTRACT TRUNCATED AT 250 WORDS)

UI MeSH Term Description Entries
D008297 Male Males
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010179 Pancreas A nodular organ in the ABDOMEN that contains a mixture of ENDOCRINE GLANDS and EXOCRINE GLANDS. The small endocrine portion consists of the ISLETS OF LANGERHANS secreting a number of hormones into the blood stream. The large exocrine portion (EXOCRINE PANCREAS) is a compound acinar gland that secretes several digestive enzymes into the pancreatic ductal system that empties into the DUODENUM.
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D001839 Bombesin A tetradecapeptide originally obtained from the skins of toads Bombina bombina and B. variegata. It is also an endogenous neurotransmitter in many animals including mammals. Bombesin affects vascular and other smooth muscle, gastric secretion, and renal circulation and function. Bombesin 14,Bombesin Dihydrochloride,Dihydrochloride, Bombesin
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000681 Amylases A group of amylolytic enzymes that cleave starch, glycogen, and related alpha-1,4-glucans. (Stedman, 25th ed) EC 3.2.1.-. Diastase,Amylase
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D017207 Rats, Sprague-Dawley A strain of albino rat used widely for experimental purposes because of its calmness and ease of handling. It was developed by the Sprague-Dawley Animal Company. Holtzman Rat,Rats, Holtzman,Sprague-Dawley Rat,Rats, Sprague Dawley,Holtzman Rats,Rat, Holtzman,Rat, Sprague-Dawley,Sprague Dawley Rat,Sprague Dawley Rats,Sprague-Dawley Rats
D051381 Rats The common name for the genus Rattus. Rattus,Rats, Laboratory,Rats, Norway,Rattus norvegicus,Laboratory Rat,Laboratory Rats,Norway Rat,Norway Rats,Rat,Rat, Laboratory,Rat, Norway,norvegicus, Rattus

Related Publications

M Wada, and R Doi, and R Hosotani, and S Higashide, and T Ibuka, and H Habashita, and K Nakai, and N Fujii, and M Imamura
Effect of bile salt on amylase release from rat pancreatic acini.
December 1985, Scandinavian journal of gastroenterology,
M Wada, and R Doi, and R Hosotani, and S Higashide, and T Ibuka, and H Habashita, and K Nakai, and N Fujii, and M Imamura
Bombesin-induced residual stimulation of amylase release from mouse pancreatic acini.
February 1985, The American journal of physiology,
M Wada, and R Doi, and R Hosotani, and S Higashide, and T Ibuka, and H Habashita, and K Nakai, and N Fujii, and M Imamura
Effect of L364718, a new CCK antagonist, on amylase secretion in isolated rat pancreatic acini.
January 1988, Pancreas,
M Wada, and R Doi, and R Hosotani, and S Higashide, and T Ibuka, and H Habashita, and K Nakai, and N Fujii, and M Imamura
Effect of an intracellular calcium antagonist (TMB-8) on carbamylcholine-induced amylase release from dispersed rat pancreatic acini.
February 1984, Life sciences,
M Wada, and R Doi, and R Hosotani, and S Higashide, and T Ibuka, and H Habashita, and K Nakai, and N Fujii, and M Imamura
Effect of somatostatin on cholecystokinin-induced amylase release in rat pancreatic acini.
July 2001, Pancreas,
M Wada, and R Doi, and R Hosotani, and S Higashide, and T Ibuka, and H Habashita, and K Nakai, and N Fujii, and M Imamura
Effect of extracellular manganese on amylase release from dispersed pancreatic acini.
November 1981, The American journal of physiology,
M Wada, and R Doi, and R Hosotani, and S Higashide, and T Ibuka, and H Habashita, and K Nakai, and N Fujii, and M Imamura
Effect of extracellular calcium on amylase release from dispersed pancreatic acini.
June 1979, The American journal of physiology,
M Wada, and R Doi, and R Hosotani, and S Higashide, and T Ibuka, and H Habashita, and K Nakai, and N Fujii, and M Imamura
Pancreatic polypeptide inhibits amylase release by rat pancreatic acini.
April 1986, The Journal of surgical research,
M Wada, and R Doi, and R Hosotani, and S Higashide, and T Ibuka, and H Habashita, and K Nakai, and N Fujii, and M Imamura
[Action of neuromedin C on amylase release from isolated rat pancreatic acini].
July 1986, Nihon Shokakibyo Gakkai zasshi = The Japanese journal of gastro-enterology,
M Wada, and R Doi, and R Hosotani, and S Higashide, and T Ibuka, and H Habashita, and K Nakai, and N Fujii, and M Imamura
Stimulatory effects of vanadate on amylase release from isolated rat pancreatic acini.
March 1998, Biochemical pharmacology,
Copied contents to your clipboard!