Characterization of [ 3 H]hemicholinium-3 binding associated with neuronal choline uptake sites in rat brain membranes
Brain Research, ISSN: 0006-8993, Vol: 348, Issue: 2, Page: 321-330
1985
- 93Citations
- 7Captures
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Metrics Details
- Citations93
- Citation Indexes93
- 93
- CrossRef82
- Captures7
- Readers7
Article Description
Hemicholinium-3 (HCh-3) is a potent and specific inhibitor of the high-affinity choline transport process (HAChT) localized on cholinergic neurons. In this study, the specific binding of [ 3 H]HCh-3 (120 Ci/mmol) was characterized in crude synaptic membranes prepared from rat brain. The binding of [ 3 H]HCh-3 to forebrain membranes was saturable, reversible and specific with an apparent Kd under optimal conditions of 35 nM and a B max of 56 fmol/mg protein. The potency of various HAChT inhibitors correlated with their apparent affinities for the specific [ 3 H]HCh-3 binding site. The specific binding of [ 3 H]HCh-3 exhibited an uneven regional distribution in the adult rat brain that corresponded to the activity of the HAChT in these regions. Transsection of the fornix, which causes a degeneration of the septal hippocampal cholinergic pathway, resulted in comparable reductions of the specific [ 3 H]HCh-3 binding and the specific activity of choline acetyltransferase, a presynaptic marker for cholinergic terminals in the hippocampal formation; the lesion did not affect the specific activity of glutamic acid decar☐ylase, a presynaptic marker for GABAergic neurons within the hippocampus. Maximal binding occurred in the presence of 200 mM NaCl: potassium, lithium, rubidium and calcium substituted poorly for sodium; and bromide, fluoride, iodide, sulfate and phosphate were less effective anions than chloride. Increasing concentrations of NaCl increased the affinity of the site for [ 3 H]HCh-3 with no significant effect on the maximal number of sites; the enhancement of affinity was due to a selective slowing of the rate of dissociation of the ligand from its binding site. These findings indicate that [ 3 H]HCh-3 binds to the carrier site mediating the HAChT on cholinergic neurons; thus, this radioligand may be a useful probe for investigating this presynaptic component (HAChT) of cholinergic neurons.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/0006899385904512; http://dx.doi.org/10.1016/0006-8993(85)90451-2; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0022272949&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/4075090; https://linkinghub.elsevier.com/retrieve/pii/0006899385904512; http://dx.doi.org/10.1016/0006-8993%2885%2990451-2; https://dx.doi.org/10.1016/0006-8993%2885%2990451-2
Elsevier BV
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