The regulation of gastrin secretion in the chicken

Mitsuhiro Furuse, G. J. Dockray

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

Chicken gastrin has a C-terminal sequence resembling mammalian cholecystokinin, but its biological properties resemble mammalian gastrin. The mechanisms controlling chicken gastrin release are poorly understood. We have investigated the factors which influence chicken gastrin secretion in vivo. Plasma gastrin concentration was decreased within 12 h of fasting, but tissue gastrin concentrations were not significantly changed even after 24 h of food deprivation. In birds fasted for 24 h and treated with the H+/K+-ATPase inhibitor, omeprazole, plasma gastrin concentration was greatly enhanced indicating the importance of acid inhibition of the gastrin cell. It is well established that amino acids (particularly aromatics like Phe and Trp) and peptides stimulate gastrin release in mammals. In chicken, however, Met, His and Arg were the strongest stimulant amongst the essential amino acids investigated. Of these three amino acids, Met rapidly stimulated gastrin release. The GRP antagonist M216140 did not suppress the Met-induced gastrin release, suggesting that Met did not stimulate GRP release. Aromatic amino acids did not strongly influence gastrin release. Medium chain triacylglycerol, which is rapidly hydrolyzed to fatty acids in the lumen, strongly stimulated gastrin secretion but long chain triacylglycerol had no effect. The data suggest that amino acids (Met, Arg and His) and fatty acids, but not triacylglycerol, are gastrin releasing factors in birds while acid inhibits secretion: there are therefore both similarities and differences between birds and mammals in the control of gastrin release.

Original languageEnglish
Pages (from-to)253-259
Number of pages7
JournalRegulatory Peptides
Volume55
Issue number3
DOIs
Publication statusPublished - Feb 14 1995
Externally publishedYes

Fingerprint

Gastrins
Chickens
Birds
Aromatic Amino Acids
Triglycerides
Mammals
Fatty Acids
Amino Acids
Food Deprivation
Gastrin-Secreting Cells
Plasmas
Acids
Proton-Translocating ATPases
Essential Amino Acids
Omeprazole
Cholecystokinin
Fasting
Adenosine Triphosphatases

All Science Journal Classification (ASJC) codes

  • Physiology
  • Biochemistry
  • Endocrinology
  • Clinical Biochemistry
  • Cellular and Molecular Neuroscience

Cite this

The regulation of gastrin secretion in the chicken. / Furuse, Mitsuhiro; Dockray, G. J.

In: Regulatory Peptides, Vol. 55, No. 3, 14.02.1995, p. 253-259.

Research output: Contribution to journalArticle

Furuse, Mitsuhiro ; Dockray, G. J. / The regulation of gastrin secretion in the chicken. In: Regulatory Peptides. 1995 ; Vol. 55, No. 3. pp. 253-259.
@article{7d1f34ba44854117b777fa925fa81921,
title = "The regulation of gastrin secretion in the chicken",
abstract = "Chicken gastrin has a C-terminal sequence resembling mammalian cholecystokinin, but its biological properties resemble mammalian gastrin. The mechanisms controlling chicken gastrin release are poorly understood. We have investigated the factors which influence chicken gastrin secretion in vivo. Plasma gastrin concentration was decreased within 12 h of fasting, but tissue gastrin concentrations were not significantly changed even after 24 h of food deprivation. In birds fasted for 24 h and treated with the H+/K+-ATPase inhibitor, omeprazole, plasma gastrin concentration was greatly enhanced indicating the importance of acid inhibition of the gastrin cell. It is well established that amino acids (particularly aromatics like Phe and Trp) and peptides stimulate gastrin release in mammals. In chicken, however, Met, His and Arg were the strongest stimulant amongst the essential amino acids investigated. Of these three amino acids, Met rapidly stimulated gastrin release. The GRP antagonist M216140 did not suppress the Met-induced gastrin release, suggesting that Met did not stimulate GRP release. Aromatic amino acids did not strongly influence gastrin release. Medium chain triacylglycerol, which is rapidly hydrolyzed to fatty acids in the lumen, strongly stimulated gastrin secretion but long chain triacylglycerol had no effect. The data suggest that amino acids (Met, Arg and His) and fatty acids, but not triacylglycerol, are gastrin releasing factors in birds while acid inhibits secretion: there are therefore both similarities and differences between birds and mammals in the control of gastrin release.",
author = "Mitsuhiro Furuse and Dockray, {G. J.}",
year = "1995",
month = "2",
day = "14",
doi = "10.1016/0167-0115(94)00113-C",
language = "English",
volume = "55",
pages = "253--259",
journal = "Regulatory Peptides",
issn = "0167-0115",
publisher = "Elsevier",
number = "3",

}

TY - JOUR

T1 - The regulation of gastrin secretion in the chicken

AU - Furuse, Mitsuhiro

AU - Dockray, G. J.

PY - 1995/2/14

Y1 - 1995/2/14

N2 - Chicken gastrin has a C-terminal sequence resembling mammalian cholecystokinin, but its biological properties resemble mammalian gastrin. The mechanisms controlling chicken gastrin release are poorly understood. We have investigated the factors which influence chicken gastrin secretion in vivo. Plasma gastrin concentration was decreased within 12 h of fasting, but tissue gastrin concentrations were not significantly changed even after 24 h of food deprivation. In birds fasted for 24 h and treated with the H+/K+-ATPase inhibitor, omeprazole, plasma gastrin concentration was greatly enhanced indicating the importance of acid inhibition of the gastrin cell. It is well established that amino acids (particularly aromatics like Phe and Trp) and peptides stimulate gastrin release in mammals. In chicken, however, Met, His and Arg were the strongest stimulant amongst the essential amino acids investigated. Of these three amino acids, Met rapidly stimulated gastrin release. The GRP antagonist M216140 did not suppress the Met-induced gastrin release, suggesting that Met did not stimulate GRP release. Aromatic amino acids did not strongly influence gastrin release. Medium chain triacylglycerol, which is rapidly hydrolyzed to fatty acids in the lumen, strongly stimulated gastrin secretion but long chain triacylglycerol had no effect. The data suggest that amino acids (Met, Arg and His) and fatty acids, but not triacylglycerol, are gastrin releasing factors in birds while acid inhibits secretion: there are therefore both similarities and differences between birds and mammals in the control of gastrin release.

AB - Chicken gastrin has a C-terminal sequence resembling mammalian cholecystokinin, but its biological properties resemble mammalian gastrin. The mechanisms controlling chicken gastrin release are poorly understood. We have investigated the factors which influence chicken gastrin secretion in vivo. Plasma gastrin concentration was decreased within 12 h of fasting, but tissue gastrin concentrations were not significantly changed even after 24 h of food deprivation. In birds fasted for 24 h and treated with the H+/K+-ATPase inhibitor, omeprazole, plasma gastrin concentration was greatly enhanced indicating the importance of acid inhibition of the gastrin cell. It is well established that amino acids (particularly aromatics like Phe and Trp) and peptides stimulate gastrin release in mammals. In chicken, however, Met, His and Arg were the strongest stimulant amongst the essential amino acids investigated. Of these three amino acids, Met rapidly stimulated gastrin release. The GRP antagonist M216140 did not suppress the Met-induced gastrin release, suggesting that Met did not stimulate GRP release. Aromatic amino acids did not strongly influence gastrin release. Medium chain triacylglycerol, which is rapidly hydrolyzed to fatty acids in the lumen, strongly stimulated gastrin secretion but long chain triacylglycerol had no effect. The data suggest that amino acids (Met, Arg and His) and fatty acids, but not triacylglycerol, are gastrin releasing factors in birds while acid inhibits secretion: there are therefore both similarities and differences between birds and mammals in the control of gastrin release.

UR - http://www.scopus.com/inward/record.url?scp=0028981119&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028981119&partnerID=8YFLogxK

U2 - 10.1016/0167-0115(94)00113-C

DO - 10.1016/0167-0115(94)00113-C

M3 - Article

C2 - 7761624

AN - SCOPUS:0028981119

VL - 55

SP - 253

EP - 259

JO - Regulatory Peptides

JF - Regulatory Peptides

SN - 0167-0115

IS - 3

ER -