Imaging α4β2 Nicotinic Acetylcholine Receptors (nAChRs) in Baboons with [18F]XTRA, a Radioligand with Improved Specific Binding in Extra-Thalamic Regions

2016 ◽  
Vol 19 (2) ◽  
pp. 280-288 ◽  
Author(s):  
Hiroto Kuwabara ◽  
Yongjun Gao ◽  
Michael Stabin ◽  
Jennifer Coughlin ◽  
Sridhar Nimmagadda ◽  
...  
1989 ◽  
Vol 238 (1291) ◽  
pp. 189-192 ◽  

A polyclonal, monospecific antiserum raised against a nicotinic acetylcholine receptor protein affinity-purified from insect nervous tissue, was employed to demonstrate the localization of antigenic sites in the neuropile of the terminal (sixth) abdominal ganglion of the cockroach Periplaneta americana . In agreement with previously published autoradiographic mapping of specific [ 125 I] α -bungarotoxin binding sites, specific areas of the central neuropile of this ganglion were densely stained, but not the cereal afferent axons. No staining was detected corresponding to the dense, peripheral, partly non-specific binding of α -bungarotoxin seen in autoradiographs of the same tissue. Certain peripherally located neuronal cell bodies, including the cell body of giant interneuron 2, contained intracellularly located antigenic sites.


2020 ◽  
Vol 5 (1) ◽  
pp. 54-61
Author(s):  
Angganararas Lungidningtyas ◽  
Arli Aditya Parikesit

Ethanol and nicotine are two common substances that are often linked to complications in alcoholic smokers. The high number of the co-consumptions in alcoholic smokers suggested a possible interaction between ethanol and nicotine in the central nervous system and a potential similar mechanism of action. Both ethanol and nicotine are shown to bind with neuronal nicotinic acetylcholine receptors (nAChRs), a ligand gated cation channel specifically targeted by the endogenous acetylcholine. Ethanol has a much less specific binding capability to modulate the receptors, however, emerging reports indicates that ethanol can interact with nAChRs both directly and indirectly. This study focuses on the analysis of ethanol binding sites with nAChRs using molecular docking techniques obtained from the Protein Data Bank. The obtained data showed a possible binding site for ethanol in nAChRs, however, upon validation, result is not substantial. Nevertheless, the obtained data should be useful for future reference for the basis of ethanol interactions with the human nAChRs proteins.


2005 ◽  
Vol 25 (1_suppl) ◽  
pp. S586-S586 ◽  
Author(s):  
Kazuo Hashikawa ◽  
Hidefumi Yoshida ◽  
Nobukatsu Sawamoto ◽  
Shigetoshi Takaya ◽  
Chihiro Namiki ◽  
...  

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