NDLI: In vitro selection of RNA molecules that displace cocaine from the membrane-bound nicotinic acetylcholine receptor

Content Provider	PubMed Central
Author	Ulrich, Henning Ippolito, Joseph E. Pagán, Oné R. Eterovic, Vesna A. Hann, Richard M. Shi, Hua Lis, John T. Eldefrawi, Mohyee E. Hess, George P.
Copyright Year	1998
Abstract	The nicotinic acetylcholine receptor (AChR) controls signal transmission between cells in the nervous system. Abused drugs such as cocaine inhibit this receptor. Transient kinetic investigations indicate that inhibitors decrease the channel-opening equilibrium constant [Hess, G. P. & Grewer, C. (1998) Methods Enzymol. 291, 443–473]. Can compounds be found that compete with inhibitors for their binding site but do not change the channel-opening equilibrium? The systematic evolution of RNA ligands by exponential enrichment methodology and the AChR in Torpedo californica electroplax membranes were used to find RNAs that can displace inhibitors from the receptor. The selection of RNA ligands was carried out in two consecutive steps: (i) a gel-shift selection of high-affinity ligands bound to the AChR in the electroplax membrane, and (ii) subsequent use of nitrocellulose filters to which both the membrane-bound receptor and RNAs bind strongly, but from which the desired RNA can be displaced from the receptor by a high-affinity AChR inhibitor, phencyclidine. After nine selection rounds, two classes of RNA molecules that bind to the AChR with nanomolar affinities were isolated and sequenced. Both classes of RNA molecules are displaced by phencyclidine and cocaine from their binding site on the AChR. Class I molecules are potent inhibitors of AChR activity in BC3H1 muscle cells, as determined by using the whole-cell current-recording technique. Class II molecules, although competing with AChR inhibitors, do not affect receptor activity in this assay; such compounds or derivatives may be useful for alleviating the toxicity experienced by millions of addicts.
Starting Page	14051
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	24
Volume Number	95
Language	English
Publisher	The National Academy of Sciences
Publisher Date	1998-11-24
Access Restriction	Open
Rights Holder	The National Academy of Sciences
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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Conformation of acetylcholine bound to the nicotinic acetylcholine receptor.

Mechanism-based discovery of ligands that counteract inhibition of the nicotinic acetylcholine receptor by cocaine and MK-801

Volatile anesthetic facilitation of in vitro desensitization of membrane-bound acetylcholine receptor from Torpedo californica

Volatile anesthetic facilitation of in vitro desensitization of membrane-bound acetylcholine receptor from Torpedo californica.

Structural details of membrane-bound acetylcholine receptor from Tropedo marmorata.

The conformation of acetylcholine at its target site in the membrane-embedded nicotinic acetylcholine receptor

Crystalline arrays of membrane-bound acetylcholine receptor.

Reconstitution of functional membrane-bound acetylcholine receptor from isolated Torpedo californica receptor protein and electroplax lipids.

Mechanism-based discovery of ligands that counteract inhibition of the nicotinic acetylcholine receptor by cocaine and MK-801.

In vitro selection of RNA molecules that displace cocaine from the membrane-bound nicotinic acetylcholine receptor

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Conformation of acetylcholine bound to the nicotinic acetylcholine receptor.

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Structural details of membrane-bound acetylcholine receptor from Tropedo marmorata.

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In vitro selection of RNA molecules that displace cocaine from the membrane-bound nicotinic acetylcholine receptor