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 P 20 (membranes sedimenting at 20,000 g) were unaffected. Here, binding changes were monitored in P 20 and nuclear matrix fractions during agonist-induced down-regulation. D-Ala 2-D-Leu 5-enkephalin (DADLE, 0.1 μM, 1 h) treatment of NG108-15 cells caused an increase in nuclear matrix-associated binding, while diminishing that in P 20. 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.
Published Version
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