The possible role of protein phosphatase 2A in the sodium sensitivity of the receptor binding of opiate antagonists naloxone and naltrindole

A. Murányi, P. Gergely, Gy M. Nagy, M. Fekete

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

In striatal membrane preparation used for receptor binding experiments high levels of protein phosphatase I and 2A activities were detected using [32P]phosphorylase a as substrate. Sodium chloride decreased the activity of protein phosphatase 2A and increased the activity of protein phosphatase 1 in a concentration-dependent manner. Sodium chloride facilitated the saturation binding of naloxone and naltrindole in rat striatal membrane preparation preincubated with ATP (50 μM) and MgCl2 (5 mM). Preincubation with calyculin A (1 nM) further increased the binding of naloxone. Addition of okadaic acid in a concentration of 2 nM, which is specific for the inhibition of protein phosphatase 2A, augmented the number of binding sites of naloxone or naltrindole. The results suggest a protein phosphatase- dependent regulation of the binding of opiate ligands in the striatum.

Original languageEnglish
Pages (from-to)273-279
Number of pages7
JournalBrain Research Bulletin
Volume44
Issue number3
DOIs
Publication statusPublished - 1997

Fingerprint

naltrindole
Protein Phosphatase 2
Opioid Receptors
Naloxone
Corpus Striatum
Sodium
Sodium Chloride
Opiate Alkaloids
Phosphorylase a
Protein Phosphatase 1
Okadaic Acid
Magnesium Chloride
Membranes
Phosphoprotein Phosphatases
Adenosine Triphosphate
Binding Sites
Ligands

Keywords

  • Naloxone
  • Naltrindole
  • Opioid receptor binding
  • Protein phosphatase
  • Sodium

ASJC Scopus subject areas

  • Neuroscience(all)

Cite this

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title = "The possible role of protein phosphatase 2A in the sodium sensitivity of the receptor binding of opiate antagonists naloxone and naltrindole",
abstract = "In striatal membrane preparation used for receptor binding experiments high levels of protein phosphatase I and 2A activities were detected using [32P]phosphorylase a as substrate. Sodium chloride decreased the activity of protein phosphatase 2A and increased the activity of protein phosphatase 1 in a concentration-dependent manner. Sodium chloride facilitated the saturation binding of naloxone and naltrindole in rat striatal membrane preparation preincubated with ATP (50 μM) and MgCl2 (5 mM). Preincubation with calyculin A (1 nM) further increased the binding of naloxone. Addition of okadaic acid in a concentration of 2 nM, which is specific for the inhibition of protein phosphatase 2A, augmented the number of binding sites of naloxone or naltrindole. The results suggest a protein phosphatase- dependent regulation of the binding of opiate ligands in the striatum.",
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T1 - The possible role of protein phosphatase 2A in the sodium sensitivity of the receptor binding of opiate antagonists naloxone and naltrindole

AU - Murányi, A.

AU - Gergely, P.

AU - Nagy, Gy M.

AU - Fekete, M.

PY - 1997

Y1 - 1997

N2 - In striatal membrane preparation used for receptor binding experiments high levels of protein phosphatase I and 2A activities were detected using [32P]phosphorylase a as substrate. Sodium chloride decreased the activity of protein phosphatase 2A and increased the activity of protein phosphatase 1 in a concentration-dependent manner. Sodium chloride facilitated the saturation binding of naloxone and naltrindole in rat striatal membrane preparation preincubated with ATP (50 μM) and MgCl2 (5 mM). Preincubation with calyculin A (1 nM) further increased the binding of naloxone. Addition of okadaic acid in a concentration of 2 nM, which is specific for the inhibition of protein phosphatase 2A, augmented the number of binding sites of naloxone or naltrindole. The results suggest a protein phosphatase- dependent regulation of the binding of opiate ligands in the striatum.

AB - In striatal membrane preparation used for receptor binding experiments high levels of protein phosphatase I and 2A activities were detected using [32P]phosphorylase a as substrate. Sodium chloride decreased the activity of protein phosphatase 2A and increased the activity of protein phosphatase 1 in a concentration-dependent manner. Sodium chloride facilitated the saturation binding of naloxone and naltrindole in rat striatal membrane preparation preincubated with ATP (50 μM) and MgCl2 (5 mM). Preincubation with calyculin A (1 nM) further increased the binding of naloxone. Addition of okadaic acid in a concentration of 2 nM, which is specific for the inhibition of protein phosphatase 2A, augmented the number of binding sites of naloxone or naltrindole. The results suggest a protein phosphatase- dependent regulation of the binding of opiate ligands in the striatum.

KW - Naloxone

KW - Naltrindole

KW - Opioid receptor binding

KW - Protein phosphatase

KW - Sodium

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