[3H]Acetylcholine nicotinic recognition sites in human brain: Characterization of agonist binding

Abdu Adem, Barbro Synnergren, Milad Botros, Birgitta Öhman, Bengt Winblad, Agneta Nordberg

Research output: Contribution to journalArticlepeer-review

19 Scopus citations


In the presence of a cholinesterase inhibitor to prevent hydrolysis and atropine to block muscarinic cholinergic receptors, [3H]acetylcholine ([3H]ACh) binding to human brain membranes showed highest levels of nicotinic binding sites in the thalamus. [3H]ACh, in the presence of atropine, binds to heterogenous high-affinity binding sites in human thalamus. Scatchard analysis of the binding gave a Kd of 0.58 nM and a Bmax of 3.3 pmol/g protein for the 'super high-affinity' site and a Kd of 27 nM and a Bmax of 70 pmol/g protein for the 'high-affinity' site. Moreover, in competition studies nicotinic agonists such (-)-nicotine and carbachol displaceable [3H]ACh-specific binding sites consist of both a high- and a low-affinity population of sites. These results indicate that highest levels of [3H]ACh binding in human brain were found in the thalamus. Moreover, the human thalamus was found to have multiple high-affinity nicotinic agonist sites.

Original languageBritish English
Pages (from-to)298-302
Number of pages5
JournalNeuroscience Letters
Issue number3
StatePublished - 29 Dec 1987


  • Agonist
  • Binding site
  • Brain
  • Human
  • Nicotine
  • Thalamus
  • [H]Acetylcholine


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