[3H]bradykinin receptor binding in mammalian tissue membranes

R. B. Innis, D. C. Manning, J. M. Stewart, Solomon H Snyder

Research output: Contribution to journalArticle

Abstract

[3H]Bradykinin binds to membranes from a variety of mammalian tissues in a saturable fashion with a dissociation constant of about 5 nM. Highest levels of binding are detected in guinea pig ileum, colon, and duodenum and in the estrous rat uterus. The relative potencies of bradykinin derivatives in competing for these binding sites in guinea pig ileum membranes correlate with their contractile potencies in the ileum better than with contractile effects in the uterus. Thus, receptor recognition sites may differ in ileum and uterus. Monovalent and divalent and divalent cations at physiological concentrations reduce [3H]bradykinin binding. Of the monovalent cations, sodium lowers binding 50% at about 80 mM. Among the divalent cations, calcium lowers binding about 50% at 5 mM, suggesting a link to the calcium conductance channel.

Original languageEnglish (US)
Pages (from-to)2630-2634
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume78
Issue number4 II
StatePublished - 1981

Fingerprint

Bradykinin Receptors
Ileum
Bradykinin
Uterus
Membranes
Divalent Cations
Guinea Pigs
Monovalent Cations
Calcium Channels
Duodenum
Colon
Sodium
Binding Sites
Calcium

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

[3H]bradykinin receptor binding in mammalian tissue membranes. / Innis, R. B.; Manning, D. C.; Stewart, J. M.; Snyder, Solomon H.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 78, No. 4 II, 1981, p. 2630-2634.

Research output: Contribution to journalArticle

@article{974706fefad54457845543a630a9d55d,
title = "[3H]bradykinin receptor binding in mammalian tissue membranes",
abstract = "[3H]Bradykinin binds to membranes from a variety of mammalian tissues in a saturable fashion with a dissociation constant of about 5 nM. Highest levels of binding are detected in guinea pig ileum, colon, and duodenum and in the estrous rat uterus. The relative potencies of bradykinin derivatives in competing for these binding sites in guinea pig ileum membranes correlate with their contractile potencies in the ileum better than with contractile effects in the uterus. Thus, receptor recognition sites may differ in ileum and uterus. Monovalent and divalent and divalent cations at physiological concentrations reduce [3H]bradykinin binding. Of the monovalent cations, sodium lowers binding 50{\%} at about 80 mM. Among the divalent cations, calcium lowers binding about 50{\%} at 5 mM, suggesting a link to the calcium conductance channel.",
author = "Innis, {R. B.} and Manning, {D. C.} and Stewart, {J. M.} and Snyder, {Solomon H}",
year = "1981",
language = "English (US)",
volume = "78",
pages = "2630--2634",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
number = "4 II",

}

TY - JOUR

T1 - [3H]bradykinin receptor binding in mammalian tissue membranes

AU - Innis, R. B.

AU - Manning, D. C.

AU - Stewart, J. M.

AU - Snyder, Solomon H

PY - 1981

Y1 - 1981

N2 - [3H]Bradykinin binds to membranes from a variety of mammalian tissues in a saturable fashion with a dissociation constant of about 5 nM. Highest levels of binding are detected in guinea pig ileum, colon, and duodenum and in the estrous rat uterus. The relative potencies of bradykinin derivatives in competing for these binding sites in guinea pig ileum membranes correlate with their contractile potencies in the ileum better than with contractile effects in the uterus. Thus, receptor recognition sites may differ in ileum and uterus. Monovalent and divalent and divalent cations at physiological concentrations reduce [3H]bradykinin binding. Of the monovalent cations, sodium lowers binding 50% at about 80 mM. Among the divalent cations, calcium lowers binding about 50% at 5 mM, suggesting a link to the calcium conductance channel.

AB - [3H]Bradykinin binds to membranes from a variety of mammalian tissues in a saturable fashion with a dissociation constant of about 5 nM. Highest levels of binding are detected in guinea pig ileum, colon, and duodenum and in the estrous rat uterus. The relative potencies of bradykinin derivatives in competing for these binding sites in guinea pig ileum membranes correlate with their contractile potencies in the ileum better than with contractile effects in the uterus. Thus, receptor recognition sites may differ in ileum and uterus. Monovalent and divalent and divalent cations at physiological concentrations reduce [3H]bradykinin binding. Of the monovalent cations, sodium lowers binding 50% at about 80 mM. Among the divalent cations, calcium lowers binding about 50% at 5 mM, suggesting a link to the calcium conductance channel.

UR - http://www.scopus.com/inward/record.url?scp=0019555970&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0019555970&partnerID=8YFLogxK

M3 - Article

VL - 78

SP - 2630

EP - 2634

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 4 II

ER -