Uncoupling by proteolysis of alpha-adrenergic receptor-mediated inhibition of adenylate cyclase in human platelets

Nicolas Ferry, Serge Adnot, A. Borsodi, Marie Lise Lacombe, Georges Guellaën, Jacques Hanoune

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Mild proteolytic treatment of human platelet membranes by alpha-chymotrypsin increased basal adenylate cyclase activity and abolished the inhibition induced by epinephrine in the presence of GTP. This treatment did not alter the total number of yohimbine binding sites, but markedly decreased the proportion of high affinity, GTP-sensitive sites for epinephrine as assessed from epinephrine competition studies. The effect of proteolysis was dose-dependent upon both adenylate cyclase inhibition and alpha2-adrenergic binding sites, with a half-maximal effect occurring at similar alpha-chymotrypsin concentration. These results support the concept that only one protein is responsible for the GTP regulation of receptor and inhibition of cyclase.

Original languageEnglish
Pages (from-to)708-714
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume108
Issue number2
DOIs
Publication statusPublished - Sep 30 1982

Fingerprint

Proteolysis
Enzyme inhibition
Receptors, Adrenergic, alpha
Platelets
Guanosine Triphosphate
Adenylyl Cyclases
Epinephrine
Blood Platelets
Binding Sites
Yohimbine
Adrenergic Agents
Membranes
Proteins
alpha-chymotrypsin

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Uncoupling by proteolysis of alpha-adrenergic receptor-mediated inhibition of adenylate cyclase in human platelets. / Ferry, Nicolas; Adnot, Serge; Borsodi, A.; Lacombe, Marie Lise; Guellaën, Georges; Hanoune, Jacques.

In: Biochemical and Biophysical Research Communications, Vol. 108, No. 2, 30.09.1982, p. 708-714.

Research output: Contribution to journalArticle

Ferry, Nicolas ; Adnot, Serge ; Borsodi, A. ; Lacombe, Marie Lise ; Guellaën, Georges ; Hanoune, Jacques. / Uncoupling by proteolysis of alpha-adrenergic receptor-mediated inhibition of adenylate cyclase in human platelets. In: Biochemical and Biophysical Research Communications. 1982 ; Vol. 108, No. 2. pp. 708-714.
@article{6908a29af7454284ac8b56e06f884577,
title = "Uncoupling by proteolysis of alpha-adrenergic receptor-mediated inhibition of adenylate cyclase in human platelets",
abstract = "Mild proteolytic treatment of human platelet membranes by alpha-chymotrypsin increased basal adenylate cyclase activity and abolished the inhibition induced by epinephrine in the presence of GTP. This treatment did not alter the total number of yohimbine binding sites, but markedly decreased the proportion of high affinity, GTP-sensitive sites for epinephrine as assessed from epinephrine competition studies. The effect of proteolysis was dose-dependent upon both adenylate cyclase inhibition and alpha2-adrenergic binding sites, with a half-maximal effect occurring at similar alpha-chymotrypsin concentration. These results support the concept that only one protein is responsible for the GTP regulation of receptor and inhibition of cyclase.",
author = "Nicolas Ferry and Serge Adnot and A. Borsodi and Lacombe, {Marie Lise} and Georges Guella{\"e}n and Jacques Hanoune",
year = "1982",
month = "9",
day = "30",
doi = "10.1016/0006-291X(82)90887-7",
language = "English",
volume = "108",
pages = "708--714",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "2",

}

TY - JOUR

T1 - Uncoupling by proteolysis of alpha-adrenergic receptor-mediated inhibition of adenylate cyclase in human platelets

AU - Ferry, Nicolas

AU - Adnot, Serge

AU - Borsodi, A.

AU - Lacombe, Marie Lise

AU - Guellaën, Georges

AU - Hanoune, Jacques

PY - 1982/9/30

Y1 - 1982/9/30

N2 - Mild proteolytic treatment of human platelet membranes by alpha-chymotrypsin increased basal adenylate cyclase activity and abolished the inhibition induced by epinephrine in the presence of GTP. This treatment did not alter the total number of yohimbine binding sites, but markedly decreased the proportion of high affinity, GTP-sensitive sites for epinephrine as assessed from epinephrine competition studies. The effect of proteolysis was dose-dependent upon both adenylate cyclase inhibition and alpha2-adrenergic binding sites, with a half-maximal effect occurring at similar alpha-chymotrypsin concentration. These results support the concept that only one protein is responsible for the GTP regulation of receptor and inhibition of cyclase.

AB - Mild proteolytic treatment of human platelet membranes by alpha-chymotrypsin increased basal adenylate cyclase activity and abolished the inhibition induced by epinephrine in the presence of GTP. This treatment did not alter the total number of yohimbine binding sites, but markedly decreased the proportion of high affinity, GTP-sensitive sites for epinephrine as assessed from epinephrine competition studies. The effect of proteolysis was dose-dependent upon both adenylate cyclase inhibition and alpha2-adrenergic binding sites, with a half-maximal effect occurring at similar alpha-chymotrypsin concentration. These results support the concept that only one protein is responsible for the GTP regulation of receptor and inhibition of cyclase.

UR - http://www.scopus.com/inward/record.url?scp=0020461792&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0020461792&partnerID=8YFLogxK

U2 - 10.1016/0006-291X(82)90887-7

DO - 10.1016/0006-291X(82)90887-7

M3 - Article

C2 - 6293500

AN - SCOPUS:0020461792

VL - 108

SP - 708

EP - 714

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 2

ER -