scholarly journals M 1 muscarinic receptor activation decreases alcohol consumption via a reduction in consummatory behavior

2021 ◽  
Vol 10 (1) ◽  
Author(s):  
Leigh C. Walker ◽  
Erin J. Campbell ◽  
Kate L. Huckstep ◽  
Nicola A. Chen ◽  
Christopher J. Langmead ◽  
...  
Keyword(s):  
Alcohol Consumption ◽  
Muscarinic Receptor ◽  
Receptor Activation ◽  
Consummatory Behavior

scholarly journals Bedside to Bench: Role of Muscarinic Receptor Activation in Ultrarapid Growth of Colorectal Cancer in a Patient With Pheochromocytoma

2013 ◽  
Vol 88 (11) ◽  
pp. 1340-1346 ◽  
Author(s):  
Erik C. von Rosenvinge ◽  
Kunrong Cheng ◽  
Cinthia B. Drachenberg ◽  
Carol B. Fowler ◽  
David L. Evers ◽  
...  
Keyword(s):  
Colorectal Cancer ◽  
Muscarinic Receptor ◽  
Receptor Activation

Muscarinic receptor activation disrupts hippocampal sharp wave-ripples

2012 ◽  
Vol 1461 ◽  
pp. 1-9 ◽  
Author(s):  
Hiroaki Norimoto ◽  
Mika Mizunuma ◽  
Daisuke Ishikawa ◽  
Norio Matsuki ◽  
Yuji Ikegaya
Keyword(s):  
Muscarinic Receptor ◽  
Receptor Activation ◽  
Sharp Wave

scholarly journals Acetylcholine-induced neuronal differentiation: muscarinic receptor activation regulates EGR-1 and REST expression in neuroblastoma cells

2009 ◽  
Vol 108 (3) ◽  
pp. 821-834 ◽  
Author(s):  
Monica Salani ◽  
Tonino Anelli ◽  
Gabriella Augusti Tocco ◽  
Elena Lucarini ◽  
Chiara Mozzetta ◽  
...  
Keyword(s):  
Neuronal Differentiation ◽  
Muscarinic Receptor ◽  
Neuroblastoma Cells ◽  
Receptor Activation

CYCLIC GMP LEVELS IN NEUROBLASTOMA CELLS ARE INCREASED BY DEPOLARIZATION AND BY MUSCARINIC RECEPTOR ACTIVATION

Abstracts ◽  
1978 ◽  
pp. 40
Author(s):  
Robert Study ◽  
Xandra Breakefield ◽  
Tamas Bartfai ◽  
Paul Greengard
Keyword(s):  
Muscarinic Receptor ◽  
Cyclic Gmp ◽  
Neuroblastoma Cells ◽  
Receptor Activation

scholarly journals M4 Muscarinic Receptor Activation Modulates Calcium Channel Currents in Rat Intracardiac Neurons

1997 ◽  
Vol 78 (4) ◽  
pp. 1903-1912 ◽  
Author(s):  
J. Cuevas ◽  
D. J. Adams
Keyword(s):  
Calcium Channel ◽  
Muscarinic Receptor ◽  
High Voltage ◽  
Receptor Activation ◽  
Muscarinic Agonist ◽  
Muscarinic Agonists ◽  
Maximal Inhibition ◽  
Cell Recording ◽  
Channel Currents ◽  
Intracardiac Neurons

Cuevas, J. and Adams, D. J. M4 muscarinic receptor activation modulates calcium channel currents in rat intracardiac neurons. J. Neurophysiol. 78: 1903–1912, 1997. Modulation of high-voltage–activated Ca2+ channels by muscarinic receptor agonists was investigated in isolated parasympathetic neurons of neonatal rat intracardiac ganglia using the amphotericin B perforated-patch whole cell recording configuration of the patch-clamp technique. Focal application of the muscarinic agonists acetylcholine (ACh), muscarine, and oxotremorine-M to the voltage-clamped soma membrane reversibly depressed peak Ca2+ channel current amplitude. The dose-reponse relationship obtained for ACh-induced inhibition of Ba2+ current ( I Ba) exhibited a half-maximal inhibition at 6 nM. Maximal inhibition of I Ba amplitude obtained with 100 μM ACh was ∼75% compared with control at +10 mV. Muscarinic agonist-induced attenuation of Ca2+ channel currents was inhibited by the muscarinic receptor antagonists pirenzepine (≤300 nM) and m4-toxin (≤100 nM), but not by AF-DX 116 (300 nM) or m1-toxin (60 nM). The dose-response relationship obtained for antagonism of muscarine-induced inhibition of I Ba by m4-toxin gave an IC50 of 11 nM. These results suggest that muscarinic agonist-induced inhibition of high-voltage–activated Ca2+ channels in rat intracardiac neurons is mediated by the M4 muscarinic receptor. M4 receptor activation shifted the voltage dependence and depressed maximal activation of Ca2+ channels but had no effect on the steady-state inactivation of Ca2+ channels. Peak Ca2+ channel tail current amplitude was reduced ≥30% at +90 mV in the presence of ACh, indicating a voltage-independent component to the muscarinicreceptor-mediated inhibition. Both dihydropyridine- and ω-conotoxin GVIA–sensitive and -insensitive Ca2+ channels were inhibited by ACh, suggesting that the M4 muscarinic receptor is coupled to multiple Ca2+ channel subtypes in these neurons. Inhibition of I Ba amplitude by muscarinic agonists was also observed after cell dialysis using the conventional whole cell recording configuration. However, internal perfusion of the cell with 100 μM guanosine 5′-O-(2-thiodiphosphate) trilithium salt (GDP-β-S) or incubation of the neurons in Pertussis toxin (PTX) abolished the modulation of I Ba by muscarinic receptor agonists, suggesting the involvement of a PTX-sensitive G-protein in the signal transduction pathway. Given that ACh is the principal neurotransmitter mediating vagal innervation of the heart, the presence of this inhibitory mechanism in postganglionic intracardiac neurons suggests that it may serve for negative feedback regulation.

Receptor phosphorylation does not mediate cross talk between muscarinic M3 and bradykinin B2 receptors

1999 ◽  
Vol 277 (5) ◽  
pp. C859-C869 ◽  
Author(s):  
Gary B. Willars ◽  
Werner Müller-Esterl ◽  
Stefan R. Nahorski
Keyword(s):  
Protein Kinase C ◽  
Muscarinic Receptor ◽  
Cross Talk ◽  
Chinese Hamster ◽  
Receptor Activation ◽  
Receptor Phosphorylation ◽  
Phosphoinositide Signaling ◽  
Kinase C ◽  
Heterologous Desensitization ◽  
B2 Receptors

This study examined cross talk between phospholipase C-coupled muscarinic M3 and bradykinin B2 receptors coexpressed in Chinese hamster ovary (CHO) cells. Agonists of either receptor enhanced phosphoinositide signaling (which rapidly desensitized) and caused protein kinase C (PKC)-independent, homologous receptor phosphorylation. Muscarinic M3 but not bradykinin B2 receptors were also phosphorylated after phorbol ester activation of PKC. Consistent with this, muscarinic M3 receptors were phosphorylated in a PKC-dependent fashion after bradykinin B2 receptor activation, but muscarinic M3 receptor activation did not influence bradykinin B2receptor phosphorylation. Despite heterologous phosphorylation of muscarinic M3 receptors, phosphoinositide and Ca2+signaling were unaffected. In contrast, marked heterologous desensitization of bradykinin-mediated responses occurred despite no receptor phosphorylation. This desensitization was associated with a sustained component of muscarinic receptor-mediated signaling, whereas bradykinin's inability to influence muscarinic receptor-mediated responses was associated with rapid and full desensitization of bradykinin responses. Thus the mechanism of functional cross talk most likely involves depletion of a shared signaling component. These data demonstrate that receptor phosphorylation is not a prerequisite for heterologous desensitization and that such desensitization is not obligatory after heterologous receptor phosphorylation.

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