Nuclear matrix associated opioid binding sites are increased upon D-Ala2-D-Leu5-enkephalin-induced down-regulation in NG108-15 cells

MM Belcheva, RJ McHale, G. Toth, A. Borsodi, CJ Coscia

Research output: Contribution to journalArticle

Abstract

Nuclear matrix preparations obtained from purified nuclei of NG108-15 cells, display high affinity opioid antagonist binding (1). Under conditions of opioid agonist-induced desensitization of cell surface receptors, nuclear matrix associated opioid binding was abolished, but expectedly binding densities in P20 (membranes sedimenting at 20,000 g) were unaffected. Here, binding changes were monitored in P20 and nuclear matrix fractions during agonist-induced down-regulation. D-Ala2-D-Leu5-enkephalin (DADLE, 0.1 μM, 1 h) treatment of NG108-15 cells caused an increase in nuclear matrix-associated binding, while diminishing that in P20. Taken together with other findings, these results suggest that a subpopulation of opioid binding sites, originally in the plasma membrane, are internalized and migrate to the nuclear matrix.

Original languageEnglish
Pages (from-to)21-22
Number of pages2
JournalRegulatory Peptides
Volume54
Issue number1
DOIs
Publication statusPublished - Nov 10 1994

Fingerprint

Nuclear Matrix
Enkephalins
Opioid Analgesics
Down-Regulation
Binding Sites
Leucine-2-Alanine Enkephalin
Narcotic Antagonists
Cell Surface Receptors
Cell membranes
Membranes
Cell Membrane
Ala(2)-enkephalinamide-met

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology
  • Physiology
  • Neuroscience(all)

Cite this

Nuclear matrix associated opioid binding sites are increased upon D-Ala2-D-Leu5-enkephalin-induced down-regulation in NG108-15 cells. / Belcheva, MM; McHale, RJ; Toth, G.; Borsodi, A.; Coscia, CJ.

In: Regulatory Peptides, Vol. 54, No. 1, 10.11.1994, p. 21-22.

Research output: Contribution to journalArticle

@article{4fa42c9ac1da4f04aeef3a3d826a1bad,
title = "Nuclear matrix associated opioid binding sites are increased upon D-Ala2-D-Leu5-enkephalin-induced down-regulation in NG108-15 cells",
abstract = "Nuclear matrix preparations obtained from purified nuclei of NG108-15 cells, display high affinity opioid antagonist binding (1). Under conditions of opioid agonist-induced desensitization of cell surface receptors, nuclear matrix associated opioid binding was abolished, but expectedly binding densities in P20 (membranes sedimenting at 20,000 g) were unaffected. Here, binding changes were monitored in P20 and nuclear matrix fractions during agonist-induced down-regulation. D-Ala2-D-Leu5-enkephalin (DADLE, 0.1 μM, 1 h) treatment of NG108-15 cells caused an increase in nuclear matrix-associated binding, while diminishing that in P20. Taken together with other findings, these results suggest that a subpopulation of opioid binding sites, originally in the plasma membrane, are internalized and migrate to the nuclear matrix.",
author = "MM Belcheva and RJ McHale and G. Toth and A. Borsodi and CJ Coscia",
year = "1994",
month = "11",
day = "10",
doi = "10.1016/0167-0115(94)90369-7",
language = "English",
volume = "54",
pages = "21--22",
journal = "Regulatory Peptides",
issn = "0167-0115",
publisher = "Elsevier",
number = "1",

}

TY - JOUR

T1 - Nuclear matrix associated opioid binding sites are increased upon D-Ala2-D-Leu5-enkephalin-induced down-regulation in NG108-15 cells

AU - Belcheva, MM

AU - McHale, RJ

AU - Toth, G.

AU - Borsodi, A.

AU - Coscia, CJ

PY - 1994/11/10

Y1 - 1994/11/10

N2 - Nuclear matrix preparations obtained from purified nuclei of NG108-15 cells, display high affinity opioid antagonist binding (1). Under conditions of opioid agonist-induced desensitization of cell surface receptors, nuclear matrix associated opioid binding was abolished, but expectedly binding densities in P20 (membranes sedimenting at 20,000 g) were unaffected. Here, binding changes were monitored in P20 and nuclear matrix fractions during agonist-induced down-regulation. D-Ala2-D-Leu5-enkephalin (DADLE, 0.1 μM, 1 h) treatment of NG108-15 cells caused an increase in nuclear matrix-associated binding, while diminishing that in P20. Taken together with other findings, these results suggest that a subpopulation of opioid binding sites, originally in the plasma membrane, are internalized and migrate to the nuclear matrix.

AB - Nuclear matrix preparations obtained from purified nuclei of NG108-15 cells, display high affinity opioid antagonist binding (1). Under conditions of opioid agonist-induced desensitization of cell surface receptors, nuclear matrix associated opioid binding was abolished, but expectedly binding densities in P20 (membranes sedimenting at 20,000 g) were unaffected. Here, binding changes were monitored in P20 and nuclear matrix fractions during agonist-induced down-regulation. D-Ala2-D-Leu5-enkephalin (DADLE, 0.1 μM, 1 h) treatment of NG108-15 cells caused an increase in nuclear matrix-associated binding, while diminishing that in P20. Taken together with other findings, these results suggest that a subpopulation of opioid binding sites, originally in the plasma membrane, are internalized and migrate to the nuclear matrix.

UR - http://www.scopus.com/inward/record.url?scp=0027948342&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027948342&partnerID=8YFLogxK

U2 - 10.1016/0167-0115(94)90369-7

DO - 10.1016/0167-0115(94)90369-7

M3 - Article

AN - SCOPUS:0027948342

VL - 54

SP - 21

EP - 22

JO - Regulatory Peptides

JF - Regulatory Peptides

SN - 0167-0115

IS - 1

ER -