Chick Optic Lobe Contains a Developmentally Regulated α2α5β2 Nicotinic Receptor Subtype

2000 ◽  
Vol 58 (2) ◽  
pp. 300-311 ◽  
Author(s):  
Barbara Balestra ◽  
Silvia Vailati ◽  
Milena Moretti ◽  
Wolfang Hanke ◽  
Francesco Clementi ◽  
...  
Keyword(s):  
Nicotinic Receptor ◽  
Optic Lobe ◽  
Receptor Subtype ◽  
Developmentally Regulated ◽  
Chick Optic Lobe

Anti-Peptide Specific Antibodies for the Characterization of Different α Subunits of α-Bungarotoxin Binding Acetylcholine Receptors Present in Chick Optic Lobe

1993 ◽  
Vol 13 (1-4) ◽  
pp. 453-465 ◽  
Author(s):  
Cecilia Gotti ◽  
Milena Moretti ◽  
Renato Longhi ◽  
Luca Briscini ◽  
Ernesto Manera ◽  
...  
Keyword(s):  
Acetylcholine Receptors ◽  
Optic Lobe ◽  
Specific Antibodies ◽  
Chick Optic Lobe ◽  
Α Subunits

Ontogenic development of membrane lipids in the chick optic lobe

1996 ◽  
Vol 14 (2) ◽  
pp. 93-104 ◽  
Author(s):  
Emilio A. Rivas ◽  
Maria Del Carmen Fernández-Tomé ◽  
Juan C. Biancotti ◽  
Norma B. Sterin-Spezia ◽  
Sara Fiszer de Plazas
Keyword(s):  
Optic Lobe ◽  
Membrane Lipids ◽  
Ontogenic Development ◽  
Chick Optic Lobe

scholarly journals Nicotinic acetylcholine receptor from chick optic lobe.

1982 ◽  
Vol 79 (4) ◽  
pp. 1321-1325 ◽  
Author(s):  
R. I. Norman ◽  
F. Mehraban ◽  
E. A. Barnard ◽  
J. O. Dolly
Keyword(s):  
Acetylcholine Receptor ◽  
Nicotinic Acetylcholine Receptor ◽  
Optic Lobe ◽  
Nicotinic Acetylcholine ◽  
Chick Optic Lobe

scholarly journals EphB Receptors Co-Distribute with a Nicotinic Receptor Subtype and Regulate Nicotinic Downstream Signaling in Neurons

2008 ◽  
Vol 38 (2) ◽  
pp. 236-244 ◽  
Author(s):  
Zhaoping Liu ◽  
William G. Conroy ◽  
Tamara M. Stawicki ◽  
Qiang Nai ◽  
Robert A. Neff ◽  
...  
Keyword(s):  
Nicotinic Receptor ◽  
Receptor Subtype ◽  
Downstream Signaling ◽  
Ephb Receptors

Spinal Muscarinic and Nicotinic Subtypes Activated by Clonidine in Postincisional Pain

2005 ◽  
Vol 103 (6) ◽  
pp. 1253-1258 ◽  
Author(s):  
Frédéric Duflo ◽  
Emmanuel Boselli ◽  
Philippe Ryvlin ◽  
Dominique Chassard
Keyword(s):  
Postoperative Pain ◽  
Receptor Antagonist ◽  
Muscarinic Receptor ◽  
Nicotinic Receptor ◽  
Receptor Subtype ◽  
Receptor Subtypes ◽  
Muscarinic Antagonist ◽  
Alpha7 Nicotinic Receptor ◽  
Intrathecal Clonidine ◽  
Nicotinic Receptor Antagonist

Background A recent model of acute incisional pain has been characterized that strongly parallels the postoperative period in patients experiencing evoked pain. In that setting, abundant literature has revealed antihypersensitive effects produced by intrathecally administered alpha2-adrenergic receptor agonists, such as clonidine, in both animals and humans. Recent reports have suggested an obligatory role of spinal acetylcholine receptors in the analgesic action of intrathecal clonidine. The authors sought to determine the involvement of spinal muscarinic and nicotinic receptor subpopulations in the antihypersensitivity effect of intrathecal clonidine in a rodent model for human postoperative pain. Methods After intrathecal catheterization, rats underwent superficial plantar incision. Clonidine or a combination of clonidine and muscarinic receptor subtype antagonists (M1, M2, M3, and M4) or nicotinic receptor subtype antagonists (alpha4beta2 and alpha7) were intrathecally administered, and withdrawal thresholds to mechanical stimuli were examined. Results Spinal clonidine maximally reduced hypersensitivity adjacent to the wound 30 min after its injection. When animals were intrathecally pretreated with the M1 muscarinic antagonist toxin MT-7, the M3 muscarinic antagonist 4-diphenylacetoxy-N-methylpiperidine, and the M4 muscarinic antagonist toxin MT-3, clonidine lost its antihypersensitive action. When animals were intrathecally pretreated with the alpha4beta2 nicotinic receptor antagonist dihydro-beta-erythroidine, but not with the alpha7 nicotinic receptor antagonist methyllycaconitine, the antihypersensitivity action of clonidine was abolished. Conclusions These data indicate for the first time that the clonidine-induced increase in punctuate mechanical threshold is mediated via the activation of all but M2 muscarinic receptor subtypes, and via the activation of alpha4beta2 but not alpha7 nicotinic receptor subtypes in a rodent model for human postoperative pain.

scholarly journals Nicotinic acetylcholine receptors (version 2019.4) in the IUPHAR/BPS Guide to Pharmacology Database

2019 ◽  
Vol 2019 (4) ◽  
Author(s):  
Cecilia Gotti ◽  
Michael. J. Marks ◽  
Neil S. Millar ◽  
Susan Wonnacott
Keyword(s):  
Nicotinic Acetylcholine Receptors ◽  
Nicotinic Receptor ◽  
Acetylcholine Receptors ◽  
Nicotinic Receptors ◽  
Receptor Subtype ◽  
Receptor Subtypes ◽  
Nicotinic Acetylcholine ◽  
Α Subunit

Nicotinic acetylcholine receptors are members of the Cys-loop family of transmitter-gated ion channels that includes the GABAA, strychnine-sensitive glycine and 5-HT3 receptors [210, 3, 155, 220, 252]. All nicotinic receptors are pentamers in which each of the five subunits contains four α-helical transmembrane domains. Genes encoding a total of 17 subunits (α1-10, β1-4, γ, δ and ε) have been identified [117]. All subunits with the exception of α8 (present in avian species) have been identified in mammals. All α subunits possess two tandem cysteine residues near to the site involved in acetylcholine binding, and subunits not named α lack these residues [155]. The orthosteric ligand binding site is formed by residues within at least three peptide domains on the α subunit (principal component), and three on the adjacent subunit (complementary component). nAChRs contain several allosteric modulatory sites. One such site, for positive allosteric modulators (PAMs) and allosteric agonists, has been proposed to reside within an intrasubunit cavity between the four transmembrane domains [257, 85]; see also [103]). The high resolution crystal structure of the molluscan acetylcholine binding protein, a structural homologue of the extracellular binding domain of a nicotinic receptor pentamer, in complex with several nicotinic receptor ligands (e.g.[33]) and the crystal structure of the extracellular domain of the α1 subunit bound to α-bungarotoxin at 1.94 Å resolution [53], has revealed the orthosteric binding site in detail (reviewed in [210, 117, 37, 193]). Nicotinic receptors at the somatic neuromuscular junction of adult animals have the stoichiometry (α1)2β1δε, whereas an extrajunctional (α1)2β1γδ receptor predominates in embryonic and denervated skeletal muscle and other pathological states. Other nicotinic receptors are assembled as combinations of α(2-6) and &beta(2-4) subunits. For α2, α3, α4 and β2 and β4 subunits, pairwise combinations of α and β (e.g. α3β4 and α4β2) are sufficient to form a functional receptor in vitro, but far more complex isoforms may exist in vivo (reviewed in [94, 91, 155]). There is strong evidence that the pairwise assembly of some α and β subunits can occur with variable stoichiometry [e.g. (α4)2(β2)2 or (α4)3(β2)2] which influences the biophysical and pharmacological properties of the receptor [155]. α5 and β3 subunits lack function when expressed alone, or pairwise, but participate in the formation of functional hetero-oligomeric receptors when expressed as a third subunit with another α and β pair [e.g. α4α5αβ2, α4αβ2β3, α5α6β2, see [155] for further examples]. The α6 subunit can form a functional receptor when co-expressed with β4 in vitro, but more efficient expression ensues from incorporation of a third partner, such as β3 [256]. The α7, α8, and α9 subunits form functional homo-oligomers, but can also combine with a second subunit to constitute a hetero-oligomeric assembly (e.g. α7β2 and α9α10). For functional expression of the α10 subunit, co-assembly with α9 is necessary. The latter, along with the α10 subunit, appears to be largely confined to cochlear and vestibular hair cells. Comprehensive listings of nicotinic receptor subunit combinations identified from recombinant expression systems, or in vivo, are given in [155]. In addition, numerous proteins interact with nicotinic ACh receptors modifying their assembly, trafficking to and from the cell surface, and activation by ACh (reviewed by [154, 9, 115]).The nicotinic receptor Subcommittee of NC-IUPHAR has recommended a nomenclature and classification scheme for nicotinic acetylcholine (nACh) receptors based on the subunit composition of known, naturally- and/or heterologously-expressed nACh receptor subtypes [139]. Headings for this table reflect abbreviations designating nACh receptor subtypes based on the predominant α subunit contained in that receptor subtype. An asterisk following the indicated α subunit denotes that other subunits are known to, or may, assemble with the indicated α subunit to form the designated nACh receptor subtype(s). Where subunit stoichiometries within a specific nACh receptor subtype are known, numbers of a particular subunit larger than 1 are indicated by a subscript following the subunit (enclosed in parentheses – see also [44]).

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