A soluble interaction between dibutyryl cyclic guanosine 3′: 5′-monophosphate and cholecystokinin: A possible mechanism for the inhibition of cholecystokinin activity

Laurence J Miller, William M. Reilly, Steven A. Rosenzweig, James D. Jamieson, Vay Liang W Go

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

N2,O2′-dibutyryl cyclic guanosine 3′:5′-monophosphate has been reported to inhibit the activity of cholecystokinin on several different end organ responses and in several species. Although the mechanism of this inhibition is unclear, competitive antagonism at the level of the receptor has been suggested. We have investigated an alternate possibility, that N2,O2′-dibutyryl cyclic guanosine 3′:5′-monophosphate inhibits cholecystokinin action by interacting directly with the peptide while both are in solution. We used antisera with specificities for different regions of cholecystokinin-gastrin peptides and radioiodinated cholecystokinin-33, cholecystokinin-8, and gastrin-17. Our results support the possibility of a soluble interaction between N2,O2′-dibutyryl cyclic guanosine 3′:5′-monophosphate and the peptides of cholecystokinin-gastrin family that is specific for the COOH-terminal (receptor binding) region of these peptides, that is dependent on the concentration of N2,O2′-dibutyryl cyclic guanosine 3′:5′-monophosphate, and that correlates with concentrations that inhibit biologic activity. The proposed N2,O2′-dibutyryl cyclic guanosine 3′:5′-monophosphate-cholecystokinin complex is dispersed by gel filtration chromatography, and is prevented from being formed by certain detergents. This soluble interaction may contribute to or explain the inhibition of cholecystokinin activity by N2,O2′-dibutyryl cyclic guanosine 3′:5′-monophosphate.

Original languageEnglish (US)
Pages (from-to)1505-1511
Number of pages7
JournalGastroenterology
Volume84
Issue number6
StatePublished - 1983

Fingerprint

Guanosine Monophosphate
Cholecystokinin
Peptides
Gastrins
Detergents
Gel Chromatography
Immune Sera

ASJC Scopus subject areas

  • Gastroenterology

Cite this

A soluble interaction between dibutyryl cyclic guanosine 3′ : 5′-monophosphate and cholecystokinin: A possible mechanism for the inhibition of cholecystokinin activity. / Miller, Laurence J; Reilly, William M.; Rosenzweig, Steven A.; Jamieson, James D.; Go, Vay Liang W.

In: Gastroenterology, Vol. 84, No. 6, 1983, p. 1505-1511.

Research output: Contribution to journalArticle

@article{4692e41b38db4fd0817266e087f5c608,
title = "A soluble interaction between dibutyryl cyclic guanosine 3′: 5′-monophosphate and cholecystokinin: A possible mechanism for the inhibition of cholecystokinin activity",
abstract = "N2,O2′-dibutyryl cyclic guanosine 3′:5′-monophosphate has been reported to inhibit the activity of cholecystokinin on several different end organ responses and in several species. Although the mechanism of this inhibition is unclear, competitive antagonism at the level of the receptor has been suggested. We have investigated an alternate possibility, that N2,O2′-dibutyryl cyclic guanosine 3′:5′-monophosphate inhibits cholecystokinin action by interacting directly with the peptide while both are in solution. We used antisera with specificities for different regions of cholecystokinin-gastrin peptides and radioiodinated cholecystokinin-33, cholecystokinin-8, and gastrin-17. Our results support the possibility of a soluble interaction between N2,O2′-dibutyryl cyclic guanosine 3′:5′-monophosphate and the peptides of cholecystokinin-gastrin family that is specific for the COOH-terminal (receptor binding) region of these peptides, that is dependent on the concentration of N2,O2′-dibutyryl cyclic guanosine 3′:5′-monophosphate, and that correlates with concentrations that inhibit biologic activity. The proposed N2,O2′-dibutyryl cyclic guanosine 3′:5′-monophosphate-cholecystokinin complex is dispersed by gel filtration chromatography, and is prevented from being formed by certain detergents. This soluble interaction may contribute to or explain the inhibition of cholecystokinin activity by N2,O2′-dibutyryl cyclic guanosine 3′:5′-monophosphate.",
author = "Miller, {Laurence J} and Reilly, {William M.} and Rosenzweig, {Steven A.} and Jamieson, {James D.} and Go, {Vay Liang W}",
year = "1983",
language = "English (US)",
volume = "84",
pages = "1505--1511",
journal = "Gastroenterology",
issn = "0016-5085",
publisher = "W.B. Saunders Ltd",
number = "6",

}

TY - JOUR

T1 - A soluble interaction between dibutyryl cyclic guanosine 3′

T2 - 5′-monophosphate and cholecystokinin: A possible mechanism for the inhibition of cholecystokinin activity

AU - Miller, Laurence J

AU - Reilly, William M.

AU - Rosenzweig, Steven A.

AU - Jamieson, James D.

AU - Go, Vay Liang W

PY - 1983

Y1 - 1983

N2 - N2,O2′-dibutyryl cyclic guanosine 3′:5′-monophosphate has been reported to inhibit the activity of cholecystokinin on several different end organ responses and in several species. Although the mechanism of this inhibition is unclear, competitive antagonism at the level of the receptor has been suggested. We have investigated an alternate possibility, that N2,O2′-dibutyryl cyclic guanosine 3′:5′-monophosphate inhibits cholecystokinin action by interacting directly with the peptide while both are in solution. We used antisera with specificities for different regions of cholecystokinin-gastrin peptides and radioiodinated cholecystokinin-33, cholecystokinin-8, and gastrin-17. Our results support the possibility of a soluble interaction between N2,O2′-dibutyryl cyclic guanosine 3′:5′-monophosphate and the peptides of cholecystokinin-gastrin family that is specific for the COOH-terminal (receptor binding) region of these peptides, that is dependent on the concentration of N2,O2′-dibutyryl cyclic guanosine 3′:5′-monophosphate, and that correlates with concentrations that inhibit biologic activity. The proposed N2,O2′-dibutyryl cyclic guanosine 3′:5′-monophosphate-cholecystokinin complex is dispersed by gel filtration chromatography, and is prevented from being formed by certain detergents. This soluble interaction may contribute to or explain the inhibition of cholecystokinin activity by N2,O2′-dibutyryl cyclic guanosine 3′:5′-monophosphate.

AB - N2,O2′-dibutyryl cyclic guanosine 3′:5′-monophosphate has been reported to inhibit the activity of cholecystokinin on several different end organ responses and in several species. Although the mechanism of this inhibition is unclear, competitive antagonism at the level of the receptor has been suggested. We have investigated an alternate possibility, that N2,O2′-dibutyryl cyclic guanosine 3′:5′-monophosphate inhibits cholecystokinin action by interacting directly with the peptide while both are in solution. We used antisera with specificities for different regions of cholecystokinin-gastrin peptides and radioiodinated cholecystokinin-33, cholecystokinin-8, and gastrin-17. Our results support the possibility of a soluble interaction between N2,O2′-dibutyryl cyclic guanosine 3′:5′-monophosphate and the peptides of cholecystokinin-gastrin family that is specific for the COOH-terminal (receptor binding) region of these peptides, that is dependent on the concentration of N2,O2′-dibutyryl cyclic guanosine 3′:5′-monophosphate, and that correlates with concentrations that inhibit biologic activity. The proposed N2,O2′-dibutyryl cyclic guanosine 3′:5′-monophosphate-cholecystokinin complex is dispersed by gel filtration chromatography, and is prevented from being formed by certain detergents. This soluble interaction may contribute to or explain the inhibition of cholecystokinin activity by N2,O2′-dibutyryl cyclic guanosine 3′:5′-monophosphate.

UR - http://www.scopus.com/inward/record.url?scp=0020568028&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0020568028&partnerID=8YFLogxK

M3 - Article

C2 - 6301926

AN - SCOPUS:0020568028

VL - 84

SP - 1505

EP - 1511

JO - Gastroenterology

JF - Gastroenterology

SN - 0016-5085

IS - 6

ER -