Disease relevance of CHRM1

• We examined the effects of pirmenol and disopyramide on the muscarinic acetylcholine receptor-operated K+ current (I[K.ACh]) in atrial cells and on experimental atrial fibrillation in isolated guinea-pig hearts [1].
• Expression of functional M2 muscarinic acetylcholine receptor in Escherichia coli [2].
• In guinea pigs actively sensitized with ovalbumin, we have observed that nasal hyperreactivity and hypersensitivity to methacholine causes nasal secretion accompanied by an increase in the density of muscarinic acetylcholine receptor (m-ACh.R) following the appearance of nasal symptoms induced by the ovalbumin challenge [3].

High impact information on CHRM1

• Cloning and sequence analysis of DNA complementary to porcine cerebral messenger RNA encoding the muscarinic acetylcholine receptor predict the complete amino-acid sequence of this protein [4].
• However, effects of class III antiarrhythmic drugs on the muscarinic acetylcholine receptor-operated K+ current (IK.ACh), which is important for the repolarization phase of the action potential in atrial cells, have not been thoroughly examined [5].
• The muscarinic acetylcholine receptor from porcine atria has been purified 100,000-fold to homogeneity by solubilization in digitonin/cholate and sequential chromatography on wheat germ agglutinin-agarose, diethylaminoethylagarose, hydroxylapatite, and 3-(2'-aminobenzhydryloxy)tropane-agarose [6].
• Muscarinic acetylcholine receptor stimulation of biliary epithelial cells and its effect on bile secretion in the isolated perfused liver [corrected] [7].
• Reconstitution of the muscarinic acetylcholine receptor. Guanine nucleotide-sensitive high affinity binding of agonists to purified muscarinic receptors reconstituted with GTP-binding proteins (Gi and Go) [8].

Biological context of CHRM1

• Hydrophilic peptides from each subtype were chosen from the large intracellular loop between the fifth and the sixth transmembrane domains, because these loops are distinct in each of the mAChR subtypes and contain determinants for coupling to different GTP-binding proteins, as well as potential sites for phosphorylation [9].
• Reconstitution of the purified porcine atrial muscarinic acetylcholine receptor with purified porcine atrial inhibitory guanine nucleotide binding protein [10].
• Tissue distribution of mRNAs encoding muscarinic acetylcholine receptor subtypes [11].
• AIM: To study if cell membrane chromatography (CMC) could reflect drug-receptor interaction and evaluate the affinity and competitive binding to muscarinic acetylcholine receptor (mAChR) [12].

Anatomical context of CHRM1

• The structure of the muscarinic acetylcholine receptor was investigated by comparing polypeptides identified by sodium dodecyl sulfate (NaDodSO4)-polyacrylamide gel electrophoresis with the size of the intact receptor in cell membranes as determined by target size analysis [13].
• The muscarinic acetylcholine receptor of porcine cerebrum has been purified to apparent homogeneity by affinity chromatography, with conjugated 3-(2'-aminobenzhydryloxy)tropane (ABT) as described previously (Haga, K., and Haga, T. (1983) J. Biol. Chem. 258, 13575-13579) [14].
• We used these subtype-specific antibodies to probe the nature of the mAChR subtypes naturally expressed in avian and mammalian cardiac membranes [9].
• The specific-binding properties of l-[3H]quinuclidinyl benzilate, a muscarinic acetylcholine-receptor antagonist, were investigated in synaptic and other membrane preparations of the guinea pig cochlear nucleus and auditory nerve [15].
• The antagonist binding properties of muscarinic acetylcholine receptor III expressed from the cloned DNA in Xenopus oocytes correspond most closely to those of the pharmacologically defined M2 glandular (III) subtype [16].

Associations of CHRM1 with chemical compounds

• There was no difference between groups in immunoreactivity for the m2 muscarinic acetylcholine receptor, substance P- or met-enkephalin in any of the medullary nuclei examined, nor was there evidence of reactive astrogliosis [17].
• The muscarinic acetylcholine receptor from porcine atria exhibits sialoglycoprotein characteristics based on its sensitivity to neuraminidase digestion and its ability to interact specifically with lectin affinity resins when solubilized with a digitonin/cholate mixed detergent system [18].
• Solubilization and hydrodynamic properties of pig atrial muscarinic acetylcholine receptor in dodecyl beta-D-maltoside [19].
• The distribution of the muscarinic acetylcholine receptor antagonists, quinuclidinyl benzilate and quinuclidinyl benzilate methiodide (both tritiated), in rat, guinea pig, and rabbit [20].
• Glycoprotein properties of the solubilized atrial muscarinic acetylcholine receptor [18].

Physical interactions of CHRM1

• From the present data, we conclude that in tracheal smooth muscle, muscarinic acetylcholine receptor-induced PLD activation is transient in nature and coupled to these receptors via PKC [21].

Analytical, diagnostic and therapeutic context of CHRM1

• Affinity chromatography of the muscarinic acetylcholine receptor [22].
• Purification of recombinant porcine m2 muscarinic acetylcholine receptor from Chinese hamster ovary cells. Circular dichroism spectra and ligand binding properties [23].
• Five different antibodies were prepared and tested for their reactivity and specificity toward different mAChR subtypes by immunoprecipitation of ligand-binding activity and receptor protein and by immunoblot analysis [9].
• The amount of bound Triton X-405 was estimated at 1.011 g/g of mAcChR, which gave an apparent molecular weight of 70 900 (sedimentation) or 68 200 (sedimentation plus gel filtration) for the uncomplexed receptor [24].
• From a newly developed, novel evaluation scheme the anomalous migration of the mAcChR in SDS-PAGE was found to be due to both an excess charge density and an abnormally large shape parameter (Kr), and the true molecular weight of the protein portion of the mAcChR ligand binding polypeptide was estimated to be between 50 000 and 60 000 [24].

References