Regulation of Μ-Opioid Receptor in Neural Cells by Extracellular Sodium
dc.contributor.author | Yabaluri, Nirmala | en_US |
dc.date.accessioned | 2010-04-01T15:26:16Z | |
dc.date.available | 2010-04-01T15:26:16Z | |
dc.date.issued | 1997-03 | en_US |
dc.identifier.citation | Yabaluri, Nirmala (1997). "Regulation of Μ-Opioid Receptor in Neural Cells by Extracellular Sodium." Journal of Neurochemistry 68(3): 1053-1061. <http://hdl.handle.net/2027.42/65917> | en_US |
dc.identifier.issn | 0022-3042 | en_US |
dc.identifier.issn | 1471-4159 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/65917 | |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=9048750&dopt=citation | en_US |
dc.description.abstract | SH-SY5Y neural cells expressing Μ- and Δ-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 m M sodium, [ 3 H]Tyr-d-Ala-Gly-(Me)Phe-Gly-ol ([ 3 H]-DAMGO) and [ 3 H]naltrexone bound to Μ receptor with K D values of 3.1 and 0.32 n M and B max values of 94 and 264 fmol/mg of protein, respectively. Replacement of sodium by choline decreased the affinity of the antagonist and increased B max for [ 3 H]DAMGO, without significantly affecting the other corresponding binding parameters. Depolarizing concentrations of KCl (34 m M ) in physiological buffer decreased the intracellular sodium levels by 67%, but this did not decrease the [ 3 H]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 [ 3 H]DAMGO and [ 3 H]naloxone binding to intact cells with EC 50 values of 24 and 3,600 n M , 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 m M sodium, and typical sigmoidal dose-response curves were obtained only in the presence of 118 m M 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 Μ receptor. | en_US |
dc.format.extent | 926059 bytes | |
dc.format.extent | 3110 bytes | |
dc.format.mimetype | application/pdf | |
dc.format.mimetype | text/plain | |
dc.publisher | Blackwell Science Ltd | en_US |
dc.rights | Blackwell Science Inc | en_US |
dc.subject.other | Sodium | en_US |
dc.subject.other | Opioid Receptor | en_US |
dc.subject.other | Potassium | en_US |
dc.subject.other | Amiloride | en_US |
dc.subject.other | Monensin | en_US |
dc.subject.other | Cyclic AMP | en_US |
dc.title | Regulation of Μ-Opioid Receptor in Neural Cells by Extracellular Sodium | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Neurosciences | en_US |
dc.subject.hlbtoplevel | Health Sciences | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | Departments of Biological Chemistry and Pharmacology, University of Michigan Medical School, Ann Arbor, Michigan, U.S.A. | en_US |
dc.identifier.pmid | 9048750 | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/65917/1/j.1471-4159.1997.68031053.x.pdf | |
dc.identifier.doi | 10.1046/j.1471-4159.1997.68031053.x | en_US |
dc.identifier.source | Journal of Neurochemistry | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
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