The DOI matches its Crossref record; 46 of the 46 references it cites were found in a registry or an index.
Alternate Stoichiometries of α4β2 Nicotinic Acetylcholine Receptors
Abstract
Two functional types of nicotinic acetylcholine receptors (nAChRs) are expressed when human embryonic kidney cells are permanently transfected with equal amounts of human alpha4 and beta2 subunit cDNAs. Most (82%) of these nAChRs exhibit an EC(50) of 74 +/- 6 microM for ACh, a much lower sensitivity than the remaining fraction (EC(50) of 0.7 +/- 0.4 microM) or than expected from expression of equal amounts of alpha4 and beta2 mRNAs in Xenopus laevis oocytes. We have found three conditions that can increase the number of nAChRs with high sensitivity to activation. These are: 1) transient transfection with additional beta2 subunits, 2) overnight incubation in nicotine, or 3) overnight culture at 29 degrees C. Using metabolic labeling with [(35)S]methionine to measure subunit stoichiometry, we found that the majority of nAChRs had a stoichiometry of (alpha4)(3)(beta2)(2). Overnight treatment with nicotine increased the number of nAChRs and increased the proportion of the (alpha4)(2)(beta2)(3) stoichiometry. Alternate alpha4beta2 nAChR stoichiometries with distinct functional properties raise the possibility for an interesting mode of synaptic regulation for nicotinic signaling in the mammalian brain.
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In the citing paper
“Data from such favorable systems show that nicotine enhances the assembly of functional nAChRs containing the α4 and β2 subunits and also causes the preferential assembly of receptors with (α4)2(β2)3 stoichiometry (Buisson and Bertrand, 2001; Nelson et al., 2003; Kuryatov et al., 2005; Sallette et al., 2005; Vallejo et al., 2005; Son et al., 2009).”
From Nicotine up-regulates α4β2 nicotinic receptors and ER exit sites via stoichiometry-dependent chaperoning (2011) · cites this paper as Nelson et al., 2003
In the citing paper
“Data from such favorable systems show that nicotine enhances the assembly of functional nAChRs containing the α4 and β2 subunits and also causes the preferential assembly of receptors with (α4)2(β2)3 stoichiometry (Buisson and Bertrand, 2001; Nelson et al., 2003; Kuryatov et al., 2005; Sallette et al., 2005; Vallejo et al., 2005; Son et al., 2009).”
From Nicotine up-regulates α4β2 nicotinic receptors and ER exit sites via stoichiometry-dependent chaperoning (2011) · cites this paper as Nelson et al., 2003
In the citing paper
“Because nicotine is thought to increase the assembly of receptors with a (α4)2(β2)3 stoichiometry (Nelson et al., 2003; Son et al., 2009)”
From Nicotine up-regulates α4β2 nicotinic receptors and ER exit sites via stoichiometry-dependent chaperoning (2011) · cites this paper as Nelson et al., 2003
In the citing paper
“In fact, our experiments and previous data (Buisson and Bertrand, 2001; Nelson et al., 2003; Kuryatov et al., 2005; Sallette et al., 2005; Vallejo et al., 2005; Son et al., 2009) suggest a shift from approximately equal contributions of the two stoichiometries in nicotine-naive cells to ∼100% (α4)2(β2)3 after chronic nicotine exposure.”
From Nicotine up-regulates α4β2 nicotinic receptors and ER exit sites via stoichiometry-dependent chaperoning (2011) · cites this paper as Nelson et al., 2003
In the citing paper
“These data correspond with previous results based on glycosylation and molecular weight measures, showing that up-regulation is initiated in the ER (Nelson et al., 2003; Kuryatov et al., 2005; Sallette et al., 2005).”
From Nicotine up-regulates α4β2 nicotinic receptors and ER exit sites via stoichiometry-dependent chaperoning (2011) · cites this paper as Nelson et al., 2003
In the citing paper
“The thermodynamic driving force for this stoichiometry shift is presumably the tighter binding of nicotine to the (α4)2(β2)3 stoichiometry (Nelson et al., 2003).”
From Nicotine up-regulates α4β2 nicotinic receptors and ER exit sites via stoichiometry-dependent chaperoning (2011) · cites this paper as Nelson et al., 2003
In the citing paper
“Several studies suggest that the two forms differ in subunit composition: the high- and low-sensitivity forms would consist of the (α4)2(β2)3 and (α4)3(β2)2 pentamers, respectively (74–76).”
From Nicotine is a selective pharmacological chaperone of acetylcholine receptor number and stoichiometry. Implications for drug discovery (2009) · cites this paper as [76]
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Metadata
- Authors
- Nelson, M. E., Kuryatov, A., Choi, C. H., Zhou, Y., & Lindstrom, J.
- Affiliations
- University of Pennsylvania (US)
- Venue
- Molecular Pharmacology
- Publisher
- Elsevier BV
- Published
- 2003-02
- Volume
- 63
- Issue
- 2
- Pages
- 332-341
- ISSN
- 0026-895X (ISSN-L)
- OpenAlex
- W2337946333
- Semantic Scholar
- dbb214d9298a2934b4b744d775aff014dcfae0be
- Cited by
- 422
- References
- 45
- Citations by year
- 2026: 3 · 2025: 9 · 2024: 9 · 2023: 8 · 2022: 10 · 2021: 14 · 2020: 18 · 2019: 8 · 2018: 10 · 2017: 16 · 2016: 23 · 2015: 29 · 2014: 28 · 2013: 23 · 2012: 31
- FWCI
- 6.32
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Molecular Pharmacology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Neurological Disorders and Stroke (R01NS011323)
- 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
- nicotinic acetylcholine receptors, subunit stoichiometry, acetylcholine sensitivity, nicotine, receptor maturation, transient transfection, temperature effects, human embryonic kidney cells
- MeSH terms
- Cells, Cultured, Humans, Receptors, Nicotinic, Temperature, Transfection, DNA, Complementary, Cholinergic Agonists, Protein Subunits
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