scholarly journals Rat neuronal nicotinic acetylcholine receptors containing α7 subunit: pharmacological properties of ligand binding and function

2009 ◽  
Vol 30 (6) ◽  
pp. 842-850 ◽  
Author(s):  
Yingxian Xiao ◽  
Galya R Abdrakhmanova ◽  
Maryna Baydyuk ◽  
Susan Hernandez ◽  
Kenneth J Kellar
Keyword(s):  
Ligand Binding ◽  
Nicotinic Acetylcholine Receptors ◽  
Acetylcholine Receptors ◽  
Pharmacological Properties ◽  
Neuronal Nicotinic Acetylcholine Receptors ◽  
Nicotinic Acetylcholine ◽  
And Function ◽  
Α7 Subunit

scholarly journals Orthosteric and/or Allosteric Binding of α-Conotoxins to Nicotinic Acetylcholine Receptors and Their Models

Marine Drugs ◽  
2018 ◽  
Vol 16 (12) ◽  
pp. 460 ◽  
Author(s):  
Elena Kryukova ◽  
Igor Ivanov ◽  
Dmitry Lebedev ◽  
Ekaterina Spirova ◽  
Natalia Egorova ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Nicotinic Acetylcholine Receptors ◽  
Acetylcholine Receptors ◽  
Aplysia Californica ◽  
Neuronal Nicotinic Acetylcholine Receptors ◽  
Nonspecific Binding ◽  
Nicotinic Acetylcholine ◽  
X Ray ◽  
Ic50 Values ◽  
Micromolar Range

α-Conotoxins from Conus snails are capable of distinguishing muscle and neuronal nicotinic acetylcholine receptors (nAChRs). α-Conotoxin RgIA and αO-conotoxin GeXIVA, blocking neuronal α9α10 nAChR, are potential analgesics. Typically, α-conotoxins bind to the orthosteric sites for agonists/competitive antagonists, but αO-conotoxin GeXIVA was proposed to attach allosterically, judging by electrophysiological experiments on α9α10 nAChR. We decided to verify this conclusion by radioligand analysis in competition with α-bungarotoxin (αBgt) on the ligand-binding domain of the nAChR α9 subunit (α9 LBD), where, from the X-ray analysis, αBgt binds at the orthosteric site. A competition with αBgt was registered for GeXIVA and RgIA, IC50 values being in the micromolar range. However, high nonspecific binding of conotoxins (detected with their radioiodinated derivatives) to His6-resin attaching α9 LBD did not allow us to accurately measure IC50s. However, IC50s were measured for binding to Aplysia californica AChBP: the RgIA globular isomer, known to be active against α9α10 nAChR, was more efficient than the ribbon one, whereas all three GeXIVA isomers had similar potencies at low µM. Thus, radioligand analysis indicated that both conotoxins can attach to the orthosteric sites in these nAChR models, which should be taken into account in the design of analgesics on the basis of these conotoxins.

Potentiation and inhibition of subtypes of neuronal nicotinic acetylcholine receptors by Pb2+

1995 ◽  
Vol 291 (3) ◽  
pp. 399-406 ◽  
Author(s):  
Ruud Zwart ◽  
Regina G.D.M. Van Kleef ◽  
Jacob M. Milikan ◽  
Marga Oortgiesen ◽  
Henk P.M. Vijverberg
Keyword(s):  
Nicotinic Acetylcholine Receptors ◽  
Acetylcholine Receptors ◽  
Neuronal Nicotinic Acetylcholine Receptors ◽  
Nicotinic Acetylcholine
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