ADP‐Ribosylation with Pertussis Toxin Modulates the GTP‐Sensitive Opioid Ligand Binding in Digitonin‐Soluble Extracts of Rat Brain Membranes

Yung H. Wong, Catherine D. Demoliou‐Mason, Eric A. Barnard

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12 Citations (Scopus)

Abstract

Pertussis toxin‐catalyzed ADP‐ribosylation of the guanine nucleotide‐binding proteins Gi and Go is shown to proceed in Mg2+‐digitonin extracts from rat brain; the Mr 41,000 and Mr 39,000 peptides are labelled there as in the membranes. The ADP‐ribosylation in detergent solution retains the differential sensitivity to guanine nucleotide analogues. This reaction also removes the partial inhibition by the guanine nucleotides of the binding of opioid agonists, as does the same treatment in the membranes. The partial inhibition of agonist binding by Na+, however, is left unchanged. The binding of the antagonist naloxone is little affected by Na+ or by guanine nucleotides in the treated membranes, but the treated soluble receptors show an enhanced binding in high‐Na+ medium, although still guanine nucleotide insensitive. The data suggest that the toxin reaction in the absence of guanine nucleotides and agonist stabilizes the opioid receptor in a receptor‐G‐protein coupled state which is no longer sensitive to guanine nucleotides but retains its sensitivity to the Na+ ions.

Original languageEnglish
Pages (from-to)114-121
Number of pages8
JournalJournal of Neurochemistry
Volume51
Issue number1
DOIs
Publication statusPublished - 1988

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Guanine Nucleotides
Pertussis Toxin
Opioid Analgesics
Rats
Brain
Ligands
Membranes
Digitonin
Whooping Cough
Guanine
Opioid Receptors
Naloxone
Detergents
Ions
Peptides
Proteins

Keywords

  • G/G proteins
  • Pertussis toxin
  • Rat brain opioid receptors

Cite this

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title = "ADP‐Ribosylation with Pertussis Toxin Modulates the GTP‐Sensitive Opioid Ligand Binding in Digitonin‐Soluble Extracts of Rat Brain Membranes",
abstract = "Pertussis toxin‐catalyzed ADP‐ribosylation of the guanine nucleotide‐binding proteins Gi and Go is shown to proceed in Mg2+‐digitonin extracts from rat brain; the Mr 41,000 and Mr 39,000 peptides are labelled there as in the membranes. The ADP‐ribosylation in detergent solution retains the differential sensitivity to guanine nucleotide analogues. This reaction also removes the partial inhibition by the guanine nucleotides of the binding of opioid agonists, as does the same treatment in the membranes. The partial inhibition of agonist binding by Na+, however, is left unchanged. The binding of the antagonist naloxone is little affected by Na+ or by guanine nucleotides in the treated membranes, but the treated soluble receptors show an enhanced binding in high‐Na+ medium, although still guanine nucleotide insensitive. The data suggest that the toxin reaction in the absence of guanine nucleotides and agonist stabilizes the opioid receptor in a receptor‐G‐protein coupled state which is no longer sensitive to guanine nucleotides but retains its sensitivity to the Na+ ions.",
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author = "Wong, {Yung H.} and Demoliou‐Mason, {Catherine D.} and Barnard, {Eric A.}",
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T1 - ADP‐Ribosylation with Pertussis Toxin Modulates the GTP‐Sensitive Opioid Ligand Binding in Digitonin‐Soluble Extracts of Rat Brain Membranes

AU - Wong, Yung H.

AU - Demoliou‐Mason, Catherine D.

AU - Barnard, Eric A.

PY - 1988

Y1 - 1988

N2 - Pertussis toxin‐catalyzed ADP‐ribosylation of the guanine nucleotide‐binding proteins Gi and Go is shown to proceed in Mg2+‐digitonin extracts from rat brain; the Mr 41,000 and Mr 39,000 peptides are labelled there as in the membranes. The ADP‐ribosylation in detergent solution retains the differential sensitivity to guanine nucleotide analogues. This reaction also removes the partial inhibition by the guanine nucleotides of the binding of opioid agonists, as does the same treatment in the membranes. The partial inhibition of agonist binding by Na+, however, is left unchanged. The binding of the antagonist naloxone is little affected by Na+ or by guanine nucleotides in the treated membranes, but the treated soluble receptors show an enhanced binding in high‐Na+ medium, although still guanine nucleotide insensitive. The data suggest that the toxin reaction in the absence of guanine nucleotides and agonist stabilizes the opioid receptor in a receptor‐G‐protein coupled state which is no longer sensitive to guanine nucleotides but retains its sensitivity to the Na+ ions.

AB - Pertussis toxin‐catalyzed ADP‐ribosylation of the guanine nucleotide‐binding proteins Gi and Go is shown to proceed in Mg2+‐digitonin extracts from rat brain; the Mr 41,000 and Mr 39,000 peptides are labelled there as in the membranes. The ADP‐ribosylation in detergent solution retains the differential sensitivity to guanine nucleotide analogues. This reaction also removes the partial inhibition by the guanine nucleotides of the binding of opioid agonists, as does the same treatment in the membranes. The partial inhibition of agonist binding by Na+, however, is left unchanged. The binding of the antagonist naloxone is little affected by Na+ or by guanine nucleotides in the treated membranes, but the treated soluble receptors show an enhanced binding in high‐Na+ medium, although still guanine nucleotide insensitive. The data suggest that the toxin reaction in the absence of guanine nucleotides and agonist stabilizes the opioid receptor in a receptor‐G‐protein coupled state which is no longer sensitive to guanine nucleotides but retains its sensitivity to the Na+ ions.

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