Cited by 181Nicotinic Acetylcholine Receptors StudyNeuroscience and Neuropharmacology ResearchReceptor Mechanisms and Signaling

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Stable expression, pharmacologic properties and regulation of the human neuronal nicotinic acetylcholine alpha 4 beta 2 receptor.

Gopalakrishnan, M, Monteggia, L M, Anderson, D J, Molinari, E J, Piattoni-Kaplan, M, Donnelly-Roberts, D, Arneric, S P, Sullivan, J P·1996·The Journal of Pharmacology and Experimental Therapeutics

DOI 10.1016/s0022-3565(25)12264-7

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Abstract

(-)-Nicotine, the prototypical agonist for neuronal nicotinic acetylcholine receptors (nAChR) has been shown to bind with high affinity to the rodent and avian alpha 4 beta 2 nAChR subtype. This subtype may represent a primary molecular target for some of the beneficial central nervous system effects i.e., cognitive enhancement, anxiolysis, analgesia, neuroprotection, of (-)-nicotine and related ligands. However, a detailed study of the human alpha 4 beta 2 subunit combination has not yet been reported. In this study, we stably coexpressed the human neuronal alpha 4 and beta 2 nAChR subunits in human embryonic kidney (HEK) 293 cells and studied its pharmacological and regulatory properties. [3H]Cytisine bound to stably transfected cells with high affinity (KD value, 0.2 +/- 0.04 nM) and with a Bmax value of 1359 +/- 91 fmol/mg protein. A good correlation (r = 0.98) was observed between binding affinities in transfected cells and in native neuronal preparations for a series of nAChR ligands. 86Rb+ efflux studies showed that stably transfected cells express functional ion channels that are sensitive to blockade by dihydro-beta-erythroidine. (+/-)-Epibatidine, (-)-nicotine, 1,1-dimethyl-4-phenylpiperazinium, (S)-3-methyl-5-(1-methyl-2-pyrrolidinyl)isoxazole (ABT-418), acetylcholine and (-)-cytisine stimulated 86Rb+ efflux with EC50 values of 0.02, 3.9, 2.5, 10, 44 and 38 microM, respectively. Treatment of transfected cells with (-)-nicotine for 7 days led to a significant increase in the density of [3H](-)-cytisine binding sites (EC50 = 0.56 microM) and a significant enhancement in the sensitivity of ACh. Specific binding or (-)-nicotine-evoked cation efflux was not detected in untransfected cells. Analysis of total cellular RNA from transfected, but not untransfected cells, showed the expected fragment sizes corresponding to the human alpha 4 and beta 2 subunit mRNA. These results demonstrate that stable expression of the human alpha 4 beta 2 nAChR subunit combination can give rise to functional ion channels that bind [3H](-)-cytisine with high affinity, exhibit homologous regulation and evoke agonist-induced cation flux with pharmacological properties consistent with native neuronal alpha 4 beta 2 nAChR.

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Authors: Gopalakrishnan, M., Monteggia, L. M., Anderson, D. J., Molinari, E. J., Piattoni-Kaplan, M., Donnelly-Roberts, D., Arneric, S. P., & Sullivan, J. P.
Affiliations: Abbott (United States) (US)
ORCID: Gopalakrishnan, M
Monteggia, L M
Sullivan, J P
Venue: The Journal of Pharmacology and Experimental Therapeutics
Publisher: Elsevier BV
Published: 1996-01
Volume: 276
Issue: 1
Pages: 289-297
ISSN: 0022-3565 (ISSN-L)
DOI: 10.1016/s0022-3565(25)12264-7
OpenAlex: W2238918217
Cited by: 178
References: 0
Citations by year: 2024: 1 · 2023: 1 · 2022: 2 · 2021: 1 · 2020: 2 · 2017: 4 · 2016: 6 · 2015: 2 · 2014: 2 · 2013: 7 · 2012: 3
FWCI: 6.18
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Journal of Pharmacology and Experimental Therapeutics (publishedVersion)
PubMed (publishedVersion)
PubMed
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nicotinic Acetylcholine Receptors Study
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
Keywords: neuronal nicotinic acetylcholine receptors, alpha4beta2 nAChR, nicotine, 86Rb efflux, ion channel function, receptor desensitization, receptor resensitization, receptor internalization, receptor trafficking
MeSH terms: Quinolizidine Alkaloids, Alkaloids, Animals, Azocines, Base Sequence, Cells, Cultured, Humans, Kidney, Kinetics, Male, Molecular Sequence Data, Neurons, Nicotine, Quinolizines, Receptors, Nicotinic, RNA, Messenger, Stereoisomerism, Transfection, Tritium, Up-Regulation, Rats, Sprague-Dawley, DNA, Complementary, Nicotinic Agonists, Rats

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Stable expression, pharmacologic properties and regulation of the human neuronal nicotinic acetylcholine alpha 4 beta 2 receptor.

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