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    Chrna1 cholinergic receptor nicotinic alpha 1 subunit [ Mus musculus (house mouse) ]

    Gene ID: 11435, updated on 27-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    PAI1 inhibits the pathogenesis of primary focal hyperhidrosis by targeting CHRNA1.

    PAI1 inhibits the pathogenesis of primary focal hyperhidrosis by targeting CHRNA1.
    Chen JF, Lin M, Li X, Lin JB., Free PMC Article

    08/7/2023
    A triad of residues aligning to Thr-152, Glu-209, and Lys-211 in Htr3, appear to be involved in side-chain interactions near binding sites in Htr3a (subunit alpha) and muscle-type Chrna1. Data suggest that mutating Htr3a triad to that of Chrna1 increases binding affinity of nicotine to Htr3a. (Htr3 = 5-hydroxytryptamine/serotonin receptor; Chrna1 = cholinergic receptor nicotinic alpha polypeptide 1)

    A triad of residues is functionally transferrable between 5-HT(3) serotonin receptors and nicotinic acetylcholine receptors.
    Mosesso R, Dougherty DA., Free PMC Article

    12/22/2018
    The results indicate that in the absence of the alpha1-nAChR subunit, clusters of nAChRs coupled to SK2 potassium channels as well as functional efferent synapses did form, showing that alpha1 is not necessary for these processes to take place.

    Assessment of the expression and role of the α1-nAChR subunit in efferent cholinergic function during the development of the mammalian cochlea.
    Roux I, Wu JS, McIntosh JM, Glowatzki E., Free PMC Article

    09/9/2017
    Findings suggest the possible role of controlling localised inflammatory response by parasympathetic cholinergic nerves through a1nAChRs of inflammation sites.

    Neuronal control of localized inflammation through expressed nicotinic acetylcholine receptors: a study carried out in mice.
    Thayabaran M, Yasawardene SG.

    12/17/2016
    This study demonstrates that genes coding for CHRNA1 subunits may contain variants associated with statin-induced ADRs.

    Transgenic mouse model reveals an unsuspected role of the acetylcholine receptor in statin-induced neuromuscular adverse drug reactions.
    Grajales-Reyes GE, Báez-Pagán CA, Zhu H, Grajales-Reyes JG, Delgado-Vélez M, García-Beltrán WF, Luciano CA, Quesada O, Ramírez R, Gómez CM, Lasalde-Dominicci JA., Free PMC Article

    02/22/2014
    Chrna1 was co-purified with nicotinic acetylcholine receptor (AChR) in C2C12 myotubes. In addition, Stau1 was found to interact with Chrna1 mRNA, and knocking down of Stau1 by RNAi resulted in defective AChR clustering.

    Agrin induces association of Chrna1 mRNA and nicotinic acetylcholine receptor in C2C12 myotubes.
    Chang YF, Chou HJ, Yen YC, Chang HW, Hong YR, Huang HW, Tseng CN.

    12/8/2012
    These results suggest that in skeletal muscle cells, neural activity reduces the molar ratio of YB-1 relative to its binding AChR alpha mRNA, leading to an increase of ribosome binding to the mRNA, and thus activating translation.

    Translational level of acetylcholine receptor α mRNA in mouse skeletal muscle is regulated by YB-1 in response to neural activity.
    Ohashi S, Moue M, Tanaka T, Kobayashi S.

    01/7/2012
    Chrna1 could be the first transcriptional target of atonal homolog 1 in the inner ear

    The α1 subunit of nicotinic acetylcholine receptors in the inner ear: transcriptional regulation by ATOH1 and co-expression with the γ subunit in hair cells.
    Scheffer D, Sage C, Plazas PV, Huang M, Wedemeyer C, Zhang DS, Chen ZY, Elgoyhen AB, Corey DP, Pingault V.

    07/23/2011
    The nAChRalpha1 gene plays a significant role at the artery wall, and reducing its expression decreases aortic plaque development.

    In vivo knockdown of nicotinic acetylcholine receptor α1 diminishes aortic atherosclerosis.
    Zhang G, Marshall AL, Thomas AL, Kernan KA, Su Y, LeBoeuf RC, Dong XR, Tchao BN., Free PMC Article

    07/2/2011
    These data identify caveolin-3 as a critical component of the signaling machinery that drives nicotinic acetylcholine receptor clustering and controls neuromuscular junction function.

    Caveolin-3 promotes nicotinic acetylcholine receptor clustering and regulates neuromuscular junction activity.
    Hezel M, de Groat WC, Galbiati F., Free PMC Article

    03/29/2010
    fibroblast nicotinic receptor alpha1 binds urokinase and promotes renal fibrosis

    A novel signaling pathway: fibroblast nicotinic receptor alpha1 binds urokinase and promotes renal fibrosis.
    Zhang G, Kernan KA, Thomas A, Collins S, Song Y, Li L, Zhu W, Leboeuf RC, Eddy AA., Free PMC Article

    01/21/2010
    The local anaesthetics proadifen and adiphenine inhibit nicotinic receptors by different molecular mechanisms.

    The local anaesthetics proadifen and adiphenine inhibit nicotinic receptors by different molecular mechanisms.
    Spitzmaul G, Gumilar F, Dilger JP, Bouzat C., Free PMC Article

    01/21/2010
    In this mouse experiemntal myasthenia gravis study demonstrated that Acetylcholine receptor-alpha1 subunit expression was increase with varying disease severity.

    Acetylcholine receptor-alpha subunit expression in myasthenia gravis: a role for the autoantigen in pathogenesis?
    Sheng JR, Li LC, Prabhakar BS, Meriggioli MN., Free PMC Article

    01/21/2010
    In S269I, mutant the peak-current amplitude decreases along trains of nearly saturating ACh pulses delivered at physiologically relevant frequencies, consistent with enhanced entry into desensitization in congenital myasthenic syndrome.

    Decremental response to high-frequency trains of acetylcholine pulses but unaltered fractional Ca2+ currents in a panel of "slow-channel syndrome" nicotinic receptor mutants.
    Elenes S, Decker M, Cymes GD, Grosman C., Free PMC Article

    01/21/2010
    Data suggest that the alpha1 nicotinic acetylcholine receptor might play an important role in mechanotransduction of tensile stress loading on maxillofacial skeletal myocytes.

    Effects of tensile stress on the alpha1 nicotinic acetylcholine receptor expression in maxillofacial skeletal myocytes.
    Wu X, Gao H, Xiao D, Luo S, Zhao Z.

    01/21/2010
    HDAC4 is a neural activity-regulated deacetylase and a key signaling component that relays neural activity to the muscle transcriptional machinery through Dach2, myogenin, and nAChR

    The histone deacetylase HDAC4 connects neural activity to muscle transcriptional reprogramming.
    Cohen TJ, Waddell DS, Barrientos T, Lu Z, Feng G, Cox GA, Bodine SC, Yao TP.

    01/21/2010
    the interaction between alpha AChR M1 and M2 domains plays a key role in channel gating

    Role of pairwise interactions between M1 and M2 domains of the nicotinic receptor in channel gating.
    Corradi J, Spitzmaul G, De Rosa MJ, Costabel M, Bouzat C., Free PMC Article

    01/21/2010
    Receptors with neutral side chains at position 89 function well, if side chain is less perturbing than amide of asparagine (nitro or keto groups allow function) or if a compensating backbone mutation is introduced to relieve unfavorable electrostatics.

    Chemical-scale studies on the role of a conserved aspartate in preorganizing the agonist binding site of the nicotinic acetylcholine receptor.
    Cashin AL, Torrice MM, McMenimen KA, Lester HA, Dougherty DA., Free PMC Article

    01/21/2010
    These two residues (and homologous sites in epsilon; subunit) are not involved in specific interactions with nicotinic agonist, and they affect activation of nicotinic receptor by shaping overall structure of agonist binding site.

    Contributions of the non-alpha subunit residues (loop D) to agonist binding and channel gating in the muscle nicotinic acetylcholine receptor.
    Akk G., Free PMC Article

    01/21/2010
    In murine muscle-type AChR alpha transmembrane 3 domain, tryptophan substitution at positions Phe-284, Ala-287, and Ile-290 produces a significant increase in normalized macroscopic response in channel gating, primarily the channel closing rate.

    Tryptophan substitutions reveal the role of nicotinic acetylcholine receptor alpha-TM3 domain in channel gating: differences between Torpedo and muscle-type AChR.
    Navedo M, Nieves M, Rojas L, Lasalde-Dominicci JA.

    01/21/2010
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