Abstract:
:SH-SY5Y neural cells expressing mu- and delta-opioid receptors were maintained viable in isotonic, sodium-free buffer in vitro. Intracellular sodium levels were manipulated by various methods, and ligand binding to intact cells was studied. In physiological buffer containing 118 mM sodium, [3H]Tyr-D-Ala-Gly-(Me)Phe-Gly-ol ([3H]-DAMGO) and [3H]naltrexone bound to mu receptor with KD values of 3.1 and 0.32 nM and Bmax values of 94 and 264 fmol/mg of protein, respectively. Replacement of sodium by choline decreased the affinity of the antagonist and increased Bmax for [3H]DAMGO, without significantly affecting the other corresponding binding parameters. Depolarizing concentrations of KCl (34 mM) in physiological buffer decreased the intracellular sodium levels by 67%, but this did not decrease the [3H]DAMGO binding to the cells. Incubation of cells with monensin and ouabain increased the intracellular sodium levels dramatically (from 78 to 250 and 300 nmol/mg, respectively), with no changes in agonist binding parameters. Ethylisopropylamiloride inhibited [3H]DAMGO and [3H]naloxone binding to intact cells with EC50 values of 24 and 3,600 nM, respectively. Adenylyl cyclase activities measured in intact cells, at different concentrations of sodium, showed the physiological significance of this ion in signal transduction. Potency of DAMGO in inhibiting the forskolin-stimulated adenylyl cyclase activity was significantly higher at lower concentrations of sodium. However, inhibition reached the maximal level only at 50 mM sodium, and typical sigmoidal dose-response curves were obtained only in the presence of 118 mM sodium. Furthermore, even at low or high intracellular sodium levels, DAMGO inhibition of cyclic AMP levels was normal. These results support a role for extracellular sodium in regulating not only the ligand interactions with the receptor, but also the signal transduction through the mu receptor.
journal_name
J Neurochemjournal_title
Journal of neurochemistryauthors
Yabaluri N,Medzihradsky Fdoi
10.1046/j.1471-4159.1997.68031053.xsubject
Has Abstractpub_date
1997-03-01 00:00:00pages
1053-61issue
3eissn
0022-3042issn
1471-4159journal_volume
68pub_type
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