Holocatalytic state of adenylate cyclase in turkey erythrocyte membranes: formation with guanylylimidodiphosphate plus isoproterenol without effect on affinity of β receptor

Allen M. Spiegel, E. M. Brown, S. A. Fedak, C. J. Woodard, G. D. Aurbach

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Abstract

Turkey erythrocyte membranes contain β adrenergic coupled adenylate cyclase systems that are modulated by guanine nuceotides. Incubation of membranes with Gpp(NH)p plus isoproterenol led to a persistently activated state ('holocatalytic state') of adenylate cyclase independent of agonist. Formation of this holocatalytic state was inhibited by conditions (4°) or by compounds (e.g., GTP, EDTA) that prevented Gpp(NH)p binding or that prevented binding of isoproterenol (e.g., propranolol). None of these agents, however, reduced activity of this activated state once it had been formed. The holocatalytic state, even though resistant to inhibition by propranolol, showed no change in receptor affinity or number of sites as determined by binding of 125I-HYP, a high affinity β adrenergic antagonist. Formation of the holocatalytic state, therefore, involves a modification of the adenylate cyclase system distal to the hormone receptor complex.

Original languageEnglish (US)
Pages (from-to)47-56
Number of pages10
JournalJournal of Cyclic Nucleotide Research
Volume2
Issue number1
StatePublished - 1976
Externally publishedYes

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Erythrocyte Membrane
Isoproterenol
Adenylyl Cyclases
Guanylyl Imidodiphosphate
Membranes
Propranolol
Adrenergic Antagonists
Guanine
Guanosine Triphosphate
Edetic Acid
Adrenergic Agents
Hormones

ASJC Scopus subject areas

  • Medicine(all)

Cite this

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title = "Holocatalytic state of adenylate cyclase in turkey erythrocyte membranes: formation with guanylylimidodiphosphate plus isoproterenol without effect on affinity of β receptor",
abstract = "Turkey erythrocyte membranes contain β adrenergic coupled adenylate cyclase systems that are modulated by guanine nuceotides. Incubation of membranes with Gpp(NH)p plus isoproterenol led to a persistently activated state ('holocatalytic state') of adenylate cyclase independent of agonist. Formation of this holocatalytic state was inhibited by conditions (4°) or by compounds (e.g., GTP, EDTA) that prevented Gpp(NH)p binding or that prevented binding of isoproterenol (e.g., propranolol). None of these agents, however, reduced activity of this activated state once it had been formed. The holocatalytic state, even though resistant to inhibition by propranolol, showed no change in receptor affinity or number of sites as determined by binding of 125I-HYP, a high affinity β adrenergic antagonist. Formation of the holocatalytic state, therefore, involves a modification of the adenylate cyclase system distal to the hormone receptor complex.",
author = "Spiegel, {Allen M.} and Brown, {E. M.} and Fedak, {S. A.} and Woodard, {C. J.} and Aurbach, {G. D.}",
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T2 - formation with guanylylimidodiphosphate plus isoproterenol without effect on affinity of β receptor

AU - Spiegel, Allen M.

AU - Brown, E. M.

AU - Fedak, S. A.

AU - Woodard, C. J.

AU - Aurbach, G. D.

PY - 1976

Y1 - 1976

N2 - Turkey erythrocyte membranes contain β adrenergic coupled adenylate cyclase systems that are modulated by guanine nuceotides. Incubation of membranes with Gpp(NH)p plus isoproterenol led to a persistently activated state ('holocatalytic state') of adenylate cyclase independent of agonist. Formation of this holocatalytic state was inhibited by conditions (4°) or by compounds (e.g., GTP, EDTA) that prevented Gpp(NH)p binding or that prevented binding of isoproterenol (e.g., propranolol). None of these agents, however, reduced activity of this activated state once it had been formed. The holocatalytic state, even though resistant to inhibition by propranolol, showed no change in receptor affinity or number of sites as determined by binding of 125I-HYP, a high affinity β adrenergic antagonist. Formation of the holocatalytic state, therefore, involves a modification of the adenylate cyclase system distal to the hormone receptor complex.

AB - Turkey erythrocyte membranes contain β adrenergic coupled adenylate cyclase systems that are modulated by guanine nuceotides. Incubation of membranes with Gpp(NH)p plus isoproterenol led to a persistently activated state ('holocatalytic state') of adenylate cyclase independent of agonist. Formation of this holocatalytic state was inhibited by conditions (4°) or by compounds (e.g., GTP, EDTA) that prevented Gpp(NH)p binding or that prevented binding of isoproterenol (e.g., propranolol). None of these agents, however, reduced activity of this activated state once it had been formed. The holocatalytic state, even though resistant to inhibition by propranolol, showed no change in receptor affinity or number of sites as determined by binding of 125I-HYP, a high affinity β adrenergic antagonist. Formation of the holocatalytic state, therefore, involves a modification of the adenylate cyclase system distal to the hormone receptor complex.

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