Relevant bibliographies by topics / M1 muscarinic acetylcholine receptor

Academic literature on the topic 'M1 muscarinic acetylcholine receptor'

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Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "M1 muscarinic acetylcholine receptor"

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Greig, Chasen J., Sarah J. Armenia, and Robert A. Cowles. "The M1 muscarinic acetylcholine receptor in the crypt stem cell compartment mediates intestinal mucosal growth." Experimental Biology and Medicine 245, no. 14 (July 1, 2020): 1194–99. http://dx.doi.org/10.1177/1535370220938375.

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Maintenance of the highly plastic intestinal epithelium relies upon stem cells localized to intestinal crypts. Recent evidence suggests muscarinic acetylcholine signaling impacts epithelial barrier function, proliferation, and apoptosis. We hypothesized that the intestinal crypt base would express specific muscarinic acetylcholine receptors that drive proliferation in this critical region. Intestinal segments spanning the small bowel were procured from wild-type C57Bl/6 mice to determine muscarinic acetylcholine receptor mRNA expression and create sections on laser capture microdissection slides for analysis of crypt base cells. RT-PCR was performed using primers targeting the five muscarinic acetylcholine receptor subtypes (M1–M5), LGR5, BIII-tubulin, and GAPDH. To determine the effects of muscarinic agonism in vivo, osmotic pumps delivering the M1 muscarinic acetylcholine receptor agonist McN-A-343 were implanted into wild type mice for one week. Segments were harvested, histologic sections created, and morphometric and proliferative parameters measured. In full-thickness intestinal samples, muscarinic acetylcholine receptor subtypes M1–M4 were found in all regions, while M5 was localized to the proximal jejunum. In crypt-base cells, the M1 muscarinic acetylcholine receptor subtype was the only subtype found and was present in all regions. LGR5 was present in all laser capture microdissection samples, indicating the capture of intestinal stem cells. In vivo experiments conducted with McN-A-343 revealed significantly increased villus height, crypt depth, and crypt-cell proliferation. The presence of M1 muscarinic acetylcholine receptor mRNA within the stem cell niche in the intestinal crypt base coupled with increased mucosal growth with M1 receptor stimulation in vivo suggests that the cholinergic system, via the M1 muscarinic acetylcholine receptor, is a critical mediator of intestinal mucosal homeostasis. Impact statement Localization of a specific subtype of the muscarinic acetylcholine receptor in the crypt stem cell compartment suggests a critical role in intestinal mucosal homeostasis. Here we demonstrate the localization of the M1 muscarinic acetylcholine receptor to the stem cell compartment and demonstrate increase morphometric and proliferative parameters when this is stimulated in vivo. These data provide novel information about this complex signaling microenvironment and offer potential future therapeutic targets for future study.
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Hollmann, Markus W., Lars G. Fischer, Anne M. Byford, and Marcel E. Durieux. "Local Anesthetic Inhibition of m1 Muscarinic Acetylcholine Signaling." Anesthesiology 93, no. 2 (August 1, 2000): 497–509. http://dx.doi.org/10.1097/00000542-200008000-00030.

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Background Local anesthetics inhibit lipid mediator signaling (lysophosphatidate, thromboxane) by acting on intracellular domains of the receptor or on the G protein. On receptors for polar agonists, the ligand-binding pocket could form an additional site of interaction, possibly resulting in superadditive inhibition. The authors therefore investigated the effects of local anesthetics on m1 muscarinic receptor functioning. Methods The authors expressed receptors in isolation using Xenopus oocytes. Using a two-electrode voltage clamp, the authors measured the effects of lidocaine, QX314 (permanently charged), and benzocaine (permanently uncharged) on Ca2+-activated Cl- currents elicited by methylcholine. The authors also characterized the interaction of lidocaine with [3H] quinuclydinyl benzylate ([3H]QNB) binding to m1 receptors. Results Lidocaine inhibited muscarinic signaling with a half-maximal inhibitory concentration (IC50 18 nm) 140-fold less than that of extracellularly administered QX314 (IC50 2.4 microm). Intracellularly injected QX314 (IC50 0.96 mm) and extracellularly applied benzocaine (IC50 1.2 mm) inhibited at high concentrations only. Inhibition of muscarinic signaling by extracellularly applied QX314 and lidocaine was the result of noncompetitive antagonism. Intracellularly injected QX314 and benzocaine inhibited muscarinic and lysophosphatidate signaling at similar concentrations, suggesting an action on the common G-protein pathway. Combined administration of intracellularly injected (IC50 19 microm) and extracellularly applied QX314 (IC50 49 nm) exerted superadditive inhibition. Lidocaine did not displace specific [3H]QNB binding to m1 receptors. Conclusions m1 Muscarinic signaling is inhibited by clinically relevant concentrations of lidocaine and by extracellularly administered QX314, suggesting that the major site of action is a extracellular domain of the muscarinic receptor. An additional less potent but superadditive inhibitory effect on the G-protein is suggested.
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Gericke, Adrian, Jan J. Sniatecki, Veronique G. A. Mayer, Evgeny Goloborodko, Andreas Patzak, Jürgen Wess, and Norbert Pfeiffer. "Role of M1, M3, and M5 muscarinic acetylcholine receptors in cholinergic dilation of small arteries studied with gene-targeted mice." American Journal of Physiology-Heart and Circulatory Physiology 300, no. 5 (May 2011): H1602—H1608. http://dx.doi.org/10.1152/ajpheart.00982.2010.

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Acetylcholine regulates perfusion of numerous organs via changes in local blood flow involving muscarinic receptor-induced release of vasorelaxing agents from the endothelium. The purpose of the present study was to determine the role of M1, M3, and M5 muscarinic acetylcholine receptors in vasodilation of small arteries using gene-targeted mice deficient in either of the three receptor subtypes (M1R−/−, M3R−/−, or M5R−/− mice, respectively). Muscarinic receptor gene expression was determined in murine cutaneous, skeletal muscle, and renal interlobar arteries using real-time PCR. Moreover, respective arteries from M1R−/−, M3R−/−, M5R−/−, and wild-type mice were isolated, cannulated with micropipettes, and pressurized. Luminal diameter was measured using video microscopy. mRNA for all five muscarinic receptor subtypes was detected in all three vascular preparations from wild-type mice. However, M3 receptor mRNA was found to be most abundant. Acetylcholine produced dose-dependent dilation in all three vascular preparations from M1R−/−, M5R−/−, and wild-type mice. In contrast, cholinergic dilation was virtually abolished in arteries from M3R−/− mice. Deletion of either M1, M3, or M5 receptor genes did not affect responses to nonmuscarinic vasodilators, such as substance P and nitroprusside. These findings provide the first direct evidence that M3 receptors mediate cholinergic vasodilation in cutaneous, skeletal muscle, and renal interlobar arteries. In contrast, neither M1 nor M5 receptors appear to be involved in cholinergic responses of the three vascular preparations tested.
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Lai, Jiunu, Xuesi M. Shao, Richard W. Pan, Edward Dy, Cindy H. Huang, and Jack L. Feldman. "RT-PCR reveals muscarinic acetylcholine receptor mRNA in the pre-Bötzinger complex." American Journal of Physiology-Lung Cellular and Molecular Physiology 281, no. 6 (December 1, 2001): L1420—L1424. http://dx.doi.org/10.1152/ajplung.2001.281.6.l1420.

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Muscarinic receptors mediate the postsynaptic excitatory effects of acetylcholine (ACh) on inspiratory neurons in the pre-Bötzinger complex (pre-BötC), the hypothesized site for respiratory rhythm generation. Because pharmacological tools for identifying the subtypes of the muscarinic receptors that underlie these effects are limited, we probed for mRNA for these receptors in the pre-BötC. We used RT-PCR to determine the expression of muscarinic receptor subtypes in tissue punches of the pre-BötC taken from rat medullary slices. Cholinergic receptor subtype M2 and M3 mRNAs were observed in the first round of PCR amplification. All five subtypes, M1–M5, were observed in the second round of amplification. Our results suggest that the majority of muscarinic receptor subtypes in the pre-BötC are M2 and M3, with minor expression of M1, M4, and M5.
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Jiang, Shangtong, Yanfang Li, Cuilin Zhang, Yingjun Zhao, Guojun Bu, Huaxi Xu, and Yun-Wu Zhang. "M1 muscarinic acetylcholine receptor in Alzheimer’s disease." Neuroscience Bulletin 30, no. 2 (March 3, 2014): 295–307. http://dx.doi.org/10.1007/s12264-013-1406-z.

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Anju, T. R., and C. S. Paulose. "Cortical cholinergic dysregulation as a long-term consequence of neonatal hypoglycemia." Biochemistry and Cell Biology 93, no. 1 (February 2015): 47–53. http://dx.doi.org/10.1139/bcb-2014-0035.

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Neonatal hypoglycemia limits the glucose supply to cells, affecting the function of brain due to its high energy demand. This can cause long-term consequences in brain function, leading to memory and cognitive deficits. The present study evaluated the cholinergic functional regulation in cerebral cortex of one month old rats exposed to neonatal hypoglycemia to understand the long-term effects of early life stress. Receptor binding and gene expression studies were done in the cerebral cortex to analyze the changes in total muscarinicreceptors, muscarinic M1, M2, M3 receptors, and the enzymes involved in acetylcholine metabolism, cholineacetyl transferase and acetylcholine esterase. Neonatal hypoglycemia decreased total muscarinic receptors (p < 0.001) with reduced muscarinic M1, M2, and M3 receptor genes (p < 0.001) in one month old rats. The reduction in acetylcholine metabolism is indicated by the downregulated cholineacetyl transferase, upregulated acetylcholine esterase, and decreased vesicular acetylcholine transporter expression. These alterations in cholinergic function in one month old rat brain indicates the longterm consequences of neonatal hypoglycemia in cortical function, which can contribute to the onset of many disease conditions in later stages of life.
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Anju, T. R., and C. S. Paulose. "Striatal cholinergic functional alterations in hypoxic neonatal rats: Role of glucose, oxygen, and epinephrine resuscitation." Biochemistry and Cell Biology 91, no. 5 (October 2013): 350–56. http://dx.doi.org/10.1139/bcb-2012-0102.

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Molecular processes regulating cholinergic functions play an important role in the control of respiration under hypoxia. Cholinergic alterations and its further complications in respiration due to hypoxic insult in neonatal rats and the effect of glucose, oxygen, and epinephrine resuscitation was evaluated in the present study. Receptor binding and gene expression studies were done in the corpus striatum to analyse the changes in total muscarinic receptors, muscarinic M1, M2, M3 receptors, and the enzymes involved in acetylcholine metabolism, choline acetyltransferase and acetylcholinesterase. Neonatal hypoxia decreased total muscarinic receptors with reduced expression of muscarinic M1, M2, and M3 receptor genes. The reduction in acetylcholine metabolism is indicated by the downregulated choline acetyltransferase and upregulated acetyl cholinesterase expression. These cholinergic disturbances were reversed to near control in glucose-resuscitated hypoxic neonates. The adverse effects of immediate oxygenation and epinephrine administration are also reported. The present findings points to the cholinergic alterations due to neonatal hypoxic shock and suggests a proper resuscitation method to ameliorate these striatal changes.
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Santiago, Luis, and Ravinder Abrol. "Understanding G Protein Selectivity of Muscarinic Acetylcholine Receptors Using Computational Methods." International Journal of Molecular Sciences 20, no. 21 (October 24, 2019): 5290. http://dx.doi.org/10.3390/ijms20215290.

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The neurotransmitter molecule acetylcholine is capable of activating five muscarinic acetylcholine receptors, M1 through M5, which belong to the superfamily of G-protein-coupled receptors (GPCRs). These five receptors share high sequence and structure homology; however, the M1, M3, and M5 receptor subtypes signal preferentially through the Gαq/11 subset of G proteins, whereas the M2 and M4 receptor subtypes signal through the Gαi/o subset of G proteins, resulting in very different intracellular signaling cascades and physiological effects. The structural basis for this innate ability of the M1/M3/M5 set of receptors and the highly homologous M2/M4 set of receptors to couple to different G proteins is poorly understood. In this study, we used molecular dynamics (MD) simulations coupled with thermodynamic analyses of M1 and M2 receptors coupled to both Gαi and Gαq to understand the structural basis of the M1 receptor’s preference for the Gαq protein and the M2 receptor’s preference for the Gαi protein. The MD studies showed that the M1 and M2 receptors can couple to both Gα proteins such that the M1 receptor engages with the two Gα proteins in slightly different orientations and the M2 receptor engages with the two Gα proteins in the same orientation. Thermodynamic studies of the free energy of binding of the receptors to the Gα proteins showed that the M1 and M2 receptors bind more strongly to their cognate Gα proteins compared to their non-cognate ones, which is in line with previous experimental studies on the M3 receptor. A detailed analysis of receptor–G protein interactions showed some cognate-complex-specific interactions for the M2:Gαi complex; however, G protein selectivity determinants are spread over a large overlapping subset of residues. Conserved interaction between transmembrane helices 5 and 6 far away from the G-protein-binding receptor interface was found only in the two cognate complexes and not in the non-cognate complexes. An analysis of residues implicated previously in G protein selectivity, in light of the cognate and non-cognate structures, shaded a more nuanced role of those residues in affecting G protein selectivity. The simulation of both cognate and non-cognate receptor–G protein complexes fills a structural gap due to difficulties in determining non-cognate complex structures and provides an enhanced framework to probe the mechanisms of G protein selectivity exhibited by most GPCRs.
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Aihara, Takeshi, Yusuke Nakamura, Makoto M. Taketo, Minoru Matsui, and Susumu Okabe. "Cholinergically stimulated gastric acid secretion is mediated by M3 and M5 but not M1 muscarinic acetylcholine receptors in mice." American Journal of Physiology-Gastrointestinal and Liver Physiology 288, no. 6 (June 2005): G1199—G1207. http://dx.doi.org/10.1152/ajpgi.00514.2004.

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Muscarinic acetylcholine receptors play an important role in the regulation of gastric acid secretion stimulated by acetylcholine; nonetheless, the precise role of each receptor subtype (M1–M5) remains unclear. This study examined the involvement of M1, M3, and M5 receptors in cholinergic regulation of acid secretion using muscarinic receptor knockout (KO) mice. Gastric acid secretion was measured in both mice subjected to acute gastric fistula production under urethane anesthesia and conscious mice that had previously undergone pylorus ligation. M3 KO mice exhibited impaired gastric acid secretion in response to carbachol. Unexpectedly, M1 KO mice exhibited normal intragastric pH, serum gastrin and mucosal histamine levels, and gastric acid secretion stimulatied by carbachol, histamine, and gastrin. Pirenzepine, known as an M1-receptor antagonist, inhibited carbachol-stimulated gastric acid secretion in a dose-dependent manner in M1 KO mice as well as in wild-type (WT) mice, suggesting that the inhibitory effect of pirenzepine on gastric acid secretion is independent of M1-receptor antagonism. Notably, M5 KO mice exhibited both significantly lower carbachol-stimulated gastric acid secretion and histamine-secretory responses to carbachol compared with WT mice. RT-PCR analysis revealed M5-mRNA expression in the stomach, but not in either the fundic or antral mucosa. Consequently, cholinergic stimulation of gastric acid secretion is clearly mediated by M3 (on parietal cells) and M5 receptors (conceivably in the submucosal plexus), but not M1 receptors.
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Swaminathan, Meyyammai, Chin Chee, Sek Chin, Michael Buckle, Noorsaadah Rahman, Stephen Doughty, and Lip Chung. "Flavonoids with M1 Muscarinic Acetylcholine Receptor Binding Activity." Molecules 19, no. 7 (June 27, 2014): 8933–48. http://dx.doi.org/10.3390/molecules19078933.

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Dissertations / Theses on the topic "M1 muscarinic acetylcholine receptor"

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Thomas, Rachel. "Investigating allosteric activation of the M1 muscarinic acetylcholine receptor." Thesis, University of Leicester, 2010. http://hdl.handle.net/2381/9298.

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Allosteric ligands of G protein-coupled receptors (GPCRs) bind to sites that are topographically distinct from the orthosteric site. AC-42 and 77-LH-28-1 are functionally selective M1 muscarinic acetylcholine (mACh) receptor allosteric agonists that are able to activate the M1 mACh receptor in the absence of an orthosteric ligand. In the present study, a variety of signalling pathways activated by AC-42 and 77-LH-28-1 have been investigated and compared with those activated by orthosteric agonists in Chinese hamster ovary (CHO) cells recombinantly expressing human M1 mACh receptors. Both orthosteric and allosteric agonists are able to activate Gαq/11-dependent signalling as demonstrated by concentration-dependent increases in [35S]-GTPγS binding to Gαq/11 subunits, [³H]-inositol phosphate accumulation and Ca²+ mobilisation. Both AC-42 and 77-LH-28-1 are also able to activate extracellular signal-regulated kinase 1/2 and cyclic AMP response-element binding protein (CREB). However, while all agonists enhance forskolin-stimulated cyclic AMP accumulation, only orthosteric agonists cause significant increases in [35S]-GTPγS binding to Gαi-proteins, suggesting that subtle differences may exist in the receptor conformations stabilised by orthosteric versus allosteric ligands. The effects of orthosteric and allosteric agonists on the regulation of the M1 mACh receptor expressed in CHO cells revealed that in contrast to orthosteric agonists, which cause significant internalisation and down-regulation, prolonged exposure to AC-42 does not significantly alter either cell-surface or total cellular M1 mACh receptor expression. 77-LH-28-1 does cause receptor internalisation, but not down-regulation. The apparent inability of AC-42 to cause M1 mACh receptor desensitisation is supported by the observation that arecoline was still able to stimulate a similar phosphoinositide hydrolysis response in CHO-hM1 cells incubated for 24 h with AC-42. These data indicate that AC -42 binding causes functional signalling in the absence of receptor regulatory mechanisms. These distinct pharmacological properties of allosteric agonists may provide therapeutic advantages additional to receptor subtype selectivity of action.
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Kim, Ju Young. "M1 muscarinic acetylcholine receptor regulation of endogenous transient receptor potential-canonical, subtype 6 (TRPC6) channels." Connect to resource, 2005. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1117570788.

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Thesis (Ph. D.)--Ohio State University, 2005.
Title from first page of PDF file. Document formatted into pages; contains xviii, 178 p.; also includes graphics. Includes bibliographical references (p. 163-178). Available online via OhioLINK's ETD Center
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Schroeder, Lee Frederick. "An in vivo biosensor for neurotransmitter release and In situ receptor activity acetylcholine and the M1 muscarinic receptor /." Diss., [La Jolla, Calif.] : University of California, San Diego, 2009. http://wwwlib.umi.com/cr/ucsd/fullcit?p3372798.

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Thesis (Ph. D.)--University of California, San Diego, 2009.
Title from first page of PDF file (viewed October 20, 2009). Available via ProQuest Digital Dissertations. Vita. Includes bibliographical references (p. 100-120).
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Atkinson, Leone Sheila. "Development and characterization of herpes simplex virus type 1 vectors expressing m1 muscarinic acetylcholine receptors." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp04/nq25012.pdf.

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Prihandoko, Rudi. "An investigation into the pharmacology and regulation of the M1, M3 and M4 muscarinic acetylcholine receptors." Thesis, University of Leicester, 2013. http://hdl.handle.net/2381/28575.

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Functional selectivity, which highlights the ability of ligands to differentially activate the signalling pathways linked to G protein-couple receptors (GPCRs) has provided an avenue for developing ligands with greater safety profiles. Pilocarpine (Pilo), a non-selective muscarinic acetylcholine receptor (mAChR) agonist has been shown to differentially activate G protein subtypes linked to the M3 mAChR. In this study the pharmacology of Pilo was further investigated using a number of readouts. When compared to methacholine (MCh), a reference agonist, Pilo appeared to preferentially stimulate inositol phosphates production than global receptor phosphorylation. The ligand also appeared to preferentially promote phosphorylation of Ser412 at the third intracellular loop of the receptor than Ser577 at the C-terminal tail. This differential phosphorylation may be linked to the fact that these residues are phosphorylated by distinct protein kinases. However, such preferential phosphorylation was not evident at the mutant M3 RASSL receptor that was engineered to respond to Clozapine-N-oxide (CNO). This mutant receptor was phosphorylated in response to CNO stimulation in a similar manner as the wild-type M3 mAChR responding to ACh. Allosteric modulation has been considered an attractive approach to selectively target GPCR subtypes for multiple disease indications. BQCA and LY2033298 have been shown to act allosterically at the M1 and M4 mAChR, respectively. In this study, we provided evidence that BQCA is probe dependent and the compound is more potent as an affinity modulator of ACh than Pilo. However BQCA did not significantly potentiate the phosphorylation state of the M1 mAChR following stimulation with a sub-maximal concentration of ACh. Similar results were obtained for LY2033298 at the M4 mAChR which suggest that allosteric modulators do not promote a receptor conformation that increases the accessibility of phosphorylation sites to protein kinases.
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Ward, Stuart David Charles. "The role of residues Tyr381 to Val387, in transmembrane domain six of the rat M1 muscarinic acetylcholine receptor, in agonist binding and receptor activation." Thesis, University College London (University of London), 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.390625.

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Buffat, Maxine Guy Patrick. "Synthesis of selective M1 muscarinic receptor agonists." Thesis, University of Manchester, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.488787.

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Spalding, Tracy Anne. "Structural studies on the muscarinic acetylcholine receptor." Thesis, University College London (University of London), 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.315419.

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Madziva, Michael Taurai. "Mechanisms of M4 muscarinic acetylcholine receptor endocytosis." Thesis, University of Cambridge, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.619733.

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Aslanoglou, Despoina. "Ligand regulation of muscarinic acetylcholine receptor organisation." Thesis, University of Glasgow, 2016. http://theses.gla.ac.uk/7048/.

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Muscarinic acetylcholine receptors (M1-M5) belong to the class A family of transmembrane G protein coupled receptors (GPCRs) and mediate various signalling processes. M1, M3 and M5 predominantly couple to Gq and promote intracellular calcium ion release from the endoplasmic reticulum. M2 and M4 preferentially couple Gi inhibiting adenylyl cyclase activity to thus decrease cAMP production and acting to regulate various ion channels. There is growing evidence that many GPCRs can exist as dimers or higher-order oligomers (Milligan, 2013) and muscarinic receptors are no exception (Alvarez-Curto et al., 2010). Herein, combinations of homomers and heteromers of co-expressed human M2 (hM2WT) and a RASSL (Receptor Activated Solely by Synthetic Ligand) form of the human M3 receptor (hM3RASSL) (Alvarez-Curto et al., 2011) were demonstrated to occur using N-terminal SNAP and CLIP tags in combination with homogeneous time resolved FRET (htrFRET). Stable Flp-In™ T-REx™ 293 cell lines able to inducibly express each of these receptor forms upon addition of doxycycline, and a cell line able to express both the hM3RASSL constitutively and hM2WT in a doxycycline inducible manner were generated. In these cells both hM3RASSL and hM2WT were detected after treatment with different concentrations of doxycycline via Western blots using tag-specific antibodies. Radioligand binding using [3H]-QNB indicated that similar amounts of hM2WT and hM3RASSL were expressed following induction with 5 ng.ml-1 doxycycline in the cells co-expressing the two receptors. Expression of the receptors was observed at the surface of live cells following labelling of the expressed receptors with SNAP and CLIP-specific cell impermeant substrates. Following induction with doxycycline each of hM2WT and hM3RASSL homomers and hM2WT-hM3RASSL heteromers were identified. Detection of oligomers was achieved following co-labelling with htrFRET-compatible substrates. Occupancy of hM2WT-hM3RASSL heteromers with the hM2WT agonist carbachol resulted in a marked, time and concentration-dependent decrease in detected heteromers and a concomitant, concentration-dependent increase in hM2WT homomers. The dynamics of interchange between heteromers and homomers was investigated by using a multiplex labelling approach and htrFRET. This method involved labelling with one energy donor and two energy acceptors capable of emitting at distinct wavelengths. Results confirmed the hM2WT-hM3RASSL heteromer to hM2WT homomer transition upon selective carbachol-mediated activation of hM2WT. A small increase in the hM3RASSL homomer was detected upon activation of the hM3RASSL with the selective agonist clozapine-N-oxide, but this was only observed in the absence of heteromers. Despite the presence of hM2WT-hM3RASSL heteromers the functional pharmacology of hM2WT and hM3RASSL receptor specific agonists was largely unaltered.
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Books on the topic "M1 muscarinic acetylcholine receptor"

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Molecular mechanisms of muscarinic acetylcholine receptor function. Austin, Tex: R.G. Landes Co., 1995.

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Rosenbaum, Larry C. Structural characterization of the cardiac muscarinic acetylcholine receptor. 1987.

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Tota, Michael R. Interaction of the muscarinic acetylcholine receptor with effector proteins. 1988.

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Vogel, Walter Kevin. Site-directed mutagenesis of the m2 muscarinic acetylcholine receptor. 1997.

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Vogel, Walter Kevin. Site-directed mutagenesis of the m2 muscarinic acetylcholine receptor. 1997.

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Mosser, Valerie A. Expression and G protein coupling of the M2 muscarinic acetylcholine receptor in Sf9 insect cells. 1999.

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Lambert, David G. Mechanisms and determinants of anaesthetic drug action. Edited by Michel M. R. F. Struys. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780199642045.003.0013.

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This chapter is broken into two main sections: a general description of the principles of ligand receptor interaction and a discussion of the main groups of ‘targets’; and explanation of some common pharmacological interactions in anaesthesia, critical care, and pain management. Agonists bind to and activate receptors while antagonists bind to receptors and block the effects of agonists. Antagonists can be competitive (most common) or non-competitive/irreversible. The main classes of drug target are enzymes, carriers, ion channels, and receptors with examples of anaesthetic relevance interacting with all classes. There are many examples in anaesthesia where multiple interacting drugs are co-administered—polypharmacology. To give an example: neuromuscular blockade. Rocuronium is a non-depolarizing neuromuscular blocker acting as a competitive antagonist at the nicotinic acetylcholine receptor. Rocuronium competes with endogenous acetylcholine to shift the concentration–response curve for contraction to the right. The degree of contractility is less for a given concentration of acetylcholine (agonist) in the presence of rocuronium. Using the same principle, the rightward shift can be compensated by increasing the amount of acetylcholine (as long as the amount of rocuronium presented to the receptor as an antagonist remains unchanged, its action can be overcome by increased agonist). Acetylcholine at the effect site is increased by acetylcholinesterase inhibition with neostigmine. One of the side-effects of neostigmine is that it acts as an indirect parasympathomimetic. In the cardiovascular system this would lead to muscarinic receptor-mediated bradycardia; these effects are routinely reversed by the competitive muscarinic antagonist glycopyrrolate.
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Mason, Peggy. Receiving the Synaptic Message. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780190237493.003.0013.

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Ionotropic and metabotropic receptors differ in their speed of action, the variety of effects produced after ligand-binding, and in the number of types present in the nervous system. The participation of two ionotropic glutamate receptors in synaptic plasticity is thought to be the cellular basis of learning. The actions of acetylcholine on nicotinic acetylcholine receptors present at the neuromuscular junction are described. The pharmacological profile of the GABAA receptor, central to most neural functions, is introduced. The properties of metabotropic receptors that are coupled to G proteins, termed G protein-coupled receptors (GPCRs), are detailed. Three canonical second-messenger systems through which GPCRs act are briefly described. An introduction to clinical pharmacology focused on how drugs acting on muscarinic and adrenergic receptors produce peripheral and central psychotropic effects is provided. Finally, the role of connexins and gap junctions in myelination and hearing is introduced.
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Marques, Tiago Reis, and Shitij Kapur. Novel Approaches for Treating Psychotic Disorders. Edited by Dennis S. Charney, Eric J. Nestler, Pamela Sklar, and Joseph D. Buxbaum. Oxford University Press, 2017. http://dx.doi.org/10.1093/med/9780190681425.003.0021.

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Current antipsychotic medications have been the mainstay in the treatment of schizophrenia since chlorpromazine was introduced in 1952. However, all antipsychotics share the same mechanism of action, which involves a blockade of the dopamine D2-receptor. This chapter covers recent attempts to develop new treatments for psychotic disorders. These include new approaches to the delivery of existing antipsychotic medications and the most recent and promising mechanisms of action that are distinct from existing antipsychotics. Some of the new mechanisms of action include drugs targeting the glutamatergic system, the alpha7 nicotinic acetylcholine receptor, the phosphodiesterase 10A enzyme, or the muscarinic and serotoninergic system. Finally, we have reviewed a number of alternative nonpharmacological pathways, such as avatar therapy, repetitive transcranial magnetic stimulation, or cognitive remediation. The chapter ends by discussing some of the major challenges facing the development of new treatments for psychotic disorders.
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Book chapters on the topic "M1 muscarinic acetylcholine receptor"

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Ichiyama, S., and T. Haga. "Muscarinic Acetylcholine Receptor." In Handbook of Neurochemistry and Molecular Neurobiology, 418–39. Boston, MA: Springer US, 2009. http://dx.doi.org/10.1007/978-0-387-30370-3_23.

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Sumiyoshi, Takaaki, and Takeshi Enomoto. "Muscarinic Acetylcholine Receptor Activators." In Small Molecule Therapeutics for Schizophrenia, 183–211. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/7355_2014_47.

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Wess, J., W. Zhang, A. Duttaroy, T. Miyakawa, J. Gomeza, Y. Cui, A. S. Basile, et al. "Muscarinic Acetylcholine Receptor Knockout Mice." In Transgenic Models in Pharmacology, 65–93. Berlin, Heidelberg: Springer Berlin Heidelberg, 2004. http://dx.doi.org/10.1007/978-3-642-18934-0_3.

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Skok, V. I., A. A. Selyanko, and V. A. Derkach. "Recognition Center of Muscarinic Acetylcholine Receptor." In Neuronal Acetylcholine Receptors, 179–92. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4684-1668-8_8.

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Haga, T., G. Berstein, T. Nishiyama, H. Uchiyama, K. Ohara, and K. Haga. "Biochemical Studies on the Muscarinic Acetylcholine Receptor." In Neuroreceptors and Signal Transduction, 239–54. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4757-5971-6_19.

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Lederer, P. C., R. Thiemann, A. Ellermann, J. Radeck, and G. Lux. "Muscarinic M1-Receptor-Antagonists in Health and Disease." In Muscarinic Receptor Subtypes in the GI Tract, 59–66. Berlin, Heidelberg: Springer Berlin Heidelberg, 1985. http://dx.doi.org/10.1007/978-3-642-70668-4_9.

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Schwarz, Roy D., Michael J. Callahan, Robert E. Davis, Mark R. Emmerling, Juan C. Jaen, William Lipinski, Thomas A. Pugsley, et al. "Pharmacological Characterization of PD151832, an M1 Muscarinic Receptor Agonist." In Alzheimer Disease, 311–15. Boston, MA: Birkhäuser Boston, 1997. http://dx.doi.org/10.1007/978-1-4612-4116-4_46.

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Järv, J. "Neurotoxic Agents Interacting with the Muscarinic Acetylcholine Receptor." In Selective Neurotoxicity, 659–80. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-85117-9_18.

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Rattan, S. "M1 and M2 Muscarinic Receptor Subtypes in the Lower Esophageal Sphincter." In Muscarinic Receptor Subtypes in the GI Tract, 43–51. Berlin, Heidelberg: Springer Berlin Heidelberg, 1985. http://dx.doi.org/10.1007/978-3-642-70668-4_7.

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Fox, J. E. T., E. E. Daniel, and T. J. McDonald. "Peptidergic Activation of Muscarinic M1 Inhibition in the Canine Small Intestine in Vivo." In Muscarinic Receptor Subtypes in the GI Tract, 67–74. Berlin, Heidelberg: Springer Berlin Heidelberg, 1985. http://dx.doi.org/10.1007/978-3-642-70668-4_10.

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Conference papers on the topic "M1 muscarinic acetylcholine receptor"

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Gross, Aaron D. "The muscarinic acetylcholine receptor: An important and underexplored component of the cholinergic system in arthropods." In 2016 International Congress of Entomology. Entomological Society of America, 2016. http://dx.doi.org/10.1603/ice.2016.94275.

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Fanelli, F., M. C. Menziani, M. Cocchi, A. Carotti, and P. G. De Benedetti. "Theoretical approaches to quantitative structure-activity relationship (QSAR) analysis of M1-muscarinic receptor-ligand complexes." In The first European conference on computational chemistry (E.C.C.C.1). AIP, 1995. http://dx.doi.org/10.1063/1.47825.

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Hayakawa, Yoku, Mitsuru Konishi, Kosuke Sakitani, Kazuhiko Koike, and Timothy Wang. "Abstract 3339: Muscarinic acetylcholine receptor subtype 3 regulates gastric stem cell expansion and gastric cancer progression by controlling YAP activation." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-3339.

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Mergenthal, Adam R., Jean-Marie C. Bouteiller, and Theodore W. Berger. "Cholinergic Modulation of CA1 Pyramidal Cells via M1 Muscarinic Receptor Activation: A Computational Study at Physiological and Supraphysiological Levels." In 2018 40th Annual International Conference of the IEEE Engineering in Medicine and Biology Society (EMBC). IEEE, 2018. http://dx.doi.org/10.1109/embc.2018.8512574.

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Reports on the topic "M1 muscarinic acetylcholine receptor"

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Miller, Steven L. The Efficacy of LY293558 in Blocking Seizures and Associated Morphological, and Behavioral Alterations Induced by Soman in Immature Male Rats and the Role of the M1 Muscarinic Acetylcholine Receptor in Organophosphate Induced Seizures. Fort Belvoir, VA: Defense Technical Information Center, January 2015. http://dx.doi.org/10.21236/ad1012848.

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