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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Anatomical distribution of sodium-dependent [(3)H]naloxone binding sites in rat brain.

The sulfhydryl alkylating reagent N-ethylmaleimide (NEM) blocks opioid receptor binding and receptor/G-protein coupling. Sodium partially restores [(3)H]naloxone binding after inhibition by NEM to reveal sodium-dependent [(3)H]naloxone sites, defined as binding in the presence of 50-100 mM NaCl after treatment of membranes or sections with 750 microM NEM. In the present study, receptor autoradiography of [(3)H]naloxone binding in control and NEM-treated tissue was used to examine the anatomical distribution of sodium-dependent [(3)H]naloxone sites in rat brain. In brain membranes, the pharmacology of sodium-dependent [(3)H]naloxone sites was consistent with that of mu opioid receptors. Relatively high IC(50) values for agonists and lack of effect of Gpp(NH)p on DAMGO displacement of [(3)H]naloxone binding in NEM-treated membranes indicated that the sodium-dependent sites were low affinity sites, presumably uncoupled from G-proteins. Autoradiograms revealed that NEM treatment dramatically reduced [(3)H]naloxone binding in all brain regions. However, [(3)H]naloxone binding was increased in specific regions in NEM-treated sections in the presence of sodium, including bed nucleus of the stria terminalis, interpeduncular nucleus, periaqueductal gray, parabrachial nucleus, locus coeruleus, and commissural nucleus tractus solitarius. Sodium-dependent [(3)H]naloxone binding sites were not found in other areas that exhibited [(3)H]naloxone binding in control tissue, including the striatum and thalamus. These studies revealed the presence of a subpopulation of [(3)H]naloxone binding sites which are sodium-dependent and have a unique regional distribution in the rat brain.[1]


  1. Anatomical distribution of sodium-dependent [(3)H]naloxone binding sites in rat brain. Sim-Selley, L.J., Xiao, R., Childers, S.R. Synapse (2000) [Pubmed]
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