TY - JOUR
T1 - Nicotinic acetylcholine receptors at the single-channel level
AU - Bouzat, Cecilia
AU - Sine, Steven M.
N1 - Funding Information:
This work was supported by grants from Agencia Nacional de Promoción Científica y Tecnológica de Argentina, Consejo Nacional de Investigaciones Científicas y Técnicas Argentina (CONICET), Universidad Nacional del Sur, and Bill and Melinda Gates Foundation to CB. Research in the Sine laboratory is supported in part by NIH grants NS31744 and NS94124. We are grateful to Dr. Corradi and Mr. Lasala for the help with the figures.
Funding Information:
This work was supported by grants from Agencia Nacional de Promoci?n Cient?fica y Tecnol?gica de Argentina, Consejo Nacional de Investigaciones Cient?ficas y T?cnicas Argentina (CONICET), Universidad Nacional del Sur, and Bill and Melinda Gates Foundation to CB. Research in the Sine laboratory is supported in part by NIH grants NS31744 and NS94124. We are grateful to Dr. Corradi and Mr. Lasala for the help with the figures.
Publisher Copyright:
© 2017 The British Pharmacological Society
PY - 2018/6
Y1 - 2018/6
N2 - Over the past four decades, the patch clamp technique and nicotinic ACh (nACh) receptors have established an enduring partnership. Like all good partnerships, each partner has proven significant in its own right, while their union has spurred innumerable advances in life science research. A member and prototype of the superfamily of pentameric ligand-gated ion channels, the nACh receptor is a chemo-electric transducer, binding ACh released from nerves and rapidly opening its channel to cation flow to elicit cellular excitation. A subject of a Nobel Prize in Physiology or Medicine, the patch clamp technique provides unprecedented resolution of currents through single ion channels in their native cellular environments. Here, focusing on muscle and α7 nACh receptors, we describe the extraordinary contribution of the patch clamp technique towards understanding how they activate in response to neurotransmitter, how subtle structural and mechanistic differences among nACh receptor subtypes translate into significant physiological differences, and how nACh receptors are being exploited as therapeutic drug targets. Linked Articles: This article is part of a themed section on Nicotinic Acetylcholine Receptors. To view the other articles in this section visit http://onlinelibrary.wiley.com/doi/10.1111/bph.v175.11/issuetoc/.
AB - Over the past four decades, the patch clamp technique and nicotinic ACh (nACh) receptors have established an enduring partnership. Like all good partnerships, each partner has proven significant in its own right, while their union has spurred innumerable advances in life science research. A member and prototype of the superfamily of pentameric ligand-gated ion channels, the nACh receptor is a chemo-electric transducer, binding ACh released from nerves and rapidly opening its channel to cation flow to elicit cellular excitation. A subject of a Nobel Prize in Physiology or Medicine, the patch clamp technique provides unprecedented resolution of currents through single ion channels in their native cellular environments. Here, focusing on muscle and α7 nACh receptors, we describe the extraordinary contribution of the patch clamp technique towards understanding how they activate in response to neurotransmitter, how subtle structural and mechanistic differences among nACh receptor subtypes translate into significant physiological differences, and how nACh receptors are being exploited as therapeutic drug targets. Linked Articles: This article is part of a themed section on Nicotinic Acetylcholine Receptors. To view the other articles in this section visit http://onlinelibrary.wiley.com/doi/10.1111/bph.v175.11/issuetoc/.
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U2 - 10.1111/bph.13770
DO - 10.1111/bph.13770
M3 - Review article
C2 - 28261794
AN - SCOPUS:85017449622
SN - 0007-1188
VL - 175
SP - 1789
EP - 1804
JO - British Journal of Pharmacology
JF - British Journal of Pharmacology
IS - 11
ER -