Neuronal nicotinic acetylcholine receptors: a new target site of ethanol
@article{Narahashi1999NeuronalNA, title={Neuronal nicotinic acetylcholine receptors: a new target site of ethanol}, author={Toshio Narahashi and Gary L. Aistrup and William Marszalec and Keiichi Nagata}, journal={Neurochemistry International}, year={1999}, volume={35}, pages={131-141} }
129 Citations
Dual action of n-alcohols on neuronal nicotinic acetylcholine receptors.
- Biology, ChemistryMolecular pharmacology
- 2001
It is found that n-alcohols, depending on the carbon chain length, exert a dual action, potentiation and inhibition, on nnAChRs in primary cultured rat cortical neurons, suggesting that potentiating and inhibitory actions are exerted through two different binding sites.
Alcohol modulation of neuronal nicotinic acetylcholine receptors is alpha subunit dependent.
- Medicine, BiologyAlcoholism, clinical and experimental research
- 2002
The alpha3beta2 AChRs are insensitive to ethanol because ethanol is at the transition point from potentiation to inhibition among n-alcohols with different carbon-chain lengths, which explains the differential action of ethanol on the central nervous system.
Effects of ethanol on excitatory and inhibitory synaptic transmission in rat cortical neurons.
- Biology, MedicineAlcoholism, clinical and experimental research
- 2007
It is concluded that ethanol stimulation of nAChRs modulates the activity of both glutamate and GABA receptors in rat cortical bipolar neurons.
Alcohol’s Actions on Neuronal Nicotinic Acetylcholine Receptors
- Medicine, BiologyAlcohol research & health : the journal of the National Institute on Alcohol Abuse and Alcoholism
- 2006
At least one subtype of nAChR may help protect cells against alcohol-induced neurotoxicity and natural variations in the genes encoding different nA ChR subunits may be associated with individual differences in the sensitivity to some of alcohol's and nicotine's effects.
Correlation between molecular volume and effects of n-alcohols on human neuronal nicotinic acetylcholine receptors expressed in Xenopus oocytes.
- Biology, ChemistryThe Journal of pharmacology and experimental therapeutics
- 2001
The hypothesis that molecular volume appears to be the most important determinant of both the potency as well as the direction of modulation of nAChR function by n-alcohols and related compounds is supported.
Neuronal Nicotinic Acetylcholine Receptors:Molecular Targets for Alcoholism andEthanol Reward: A Dissertation
- Biology, Medicine
- 2011
It is shown, for the first time, that a specific nAChR subtype, those that contain the α4 subunit (α4*), mediate voluntary ethanol consumption and reward and further supports the hypothesis that α4* nA ChRs are molecular targets for alcohol cessation therapies.
Nootropic drug modulation of neuronal nicotinic acetylcholine receptors in rat cortical neurons.
- BiologyMolecular pharmacology
- 2001
Nefiracetam potentiating action was not affected by 24-h pretreatment of neurons with pertussis toxin, but was abolished by cholera toxin, indicating that nnAChRs are an important site of action of nefiracetAM and G(s) proteins may be its crucial target.
Acute Alcohol Action and Desensitization of Ligand-Gated Ion Channels
- Biology, MedicinePharmacological Reviews
- 2009
Understanding interactions between ethanol and ionotropic receptor desensitization may help to explain different ethanol actions when ethanol is evaluated in vitro on cloned channel proteins, under physiological or pathological conditions or in distinct cell domains with modified ligand concentration and/or receptor conformation.
Basis of variable sensitivities of GABA(A) receptors to ethanol.
- Biology, MedicineAlcoholism, clinical and experimental research
- 2000
It was concluded that the GABA(A) receptors of these four cell types were basically sensitive to n-alcohols including ethanol but the sensitivity curve was shifted to the lower side in the order of decreasing sensitivity of DRG neurons > alpha1/beta2gamma2S > cortical neurons.
Unique general anesthetic binding sites within distinct conformational states of the nicotinic acetylcholine receptor.
- Biology, ChemistryInternational review of neurobiology
- 2003
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