skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Desensitization of membrane-bound Torpedo acetylcholine receptor by amine noncompetitive antagonists and aliphatic alcohols: studies of (/sup 3/H)acetylcholine binding and /sup 22/Na/sup +/ ion fluxes

Journal Article · · Biochemistry; (United States)
OSTI ID:5779430

Measurements of the kinetics of binding of (/sup 3/H)acetylcholine ((/sup 3/H)AcCh) to membrane-bound nicotinic AcCh receptors from Torpedo electric tissue have been used to characterize the effects of amine and alcohol noncompetitive antagonists on receptor conformational equilibria. The receptor exists in interconvertible conformations distinguished by agonist binding affinity. The high-affinity receptor conformation stabilized by noncompetitive antagonists was characterized by (1) the rate constant (k/sub rec/) for receptor reisomerization upon removal of stabilizing ligand and (2) the rate constant (k/sub dis/) for dissociation of (/sup 3/H)AcCh-receptor complexes. On the basis of these criteria, the high-affinity receptor conformation stabilized by amine and alcohol noncompetitive blockers is the same as that stabilized by agonist. Histrionicotoxin (HTX) and adiphenine antagonized the conformational perturbation caused by proadifen, while mixtures of HTX and 2-propanol produced additive effects. Exposure to proadifen in the absence of agonist produced a reversible inhibition (desensitization) of the flux response, and recovery from desensitization occurred at the same rate as the reisomerization from the high-affinity receptor state. HTX, which did not cause desensitization of the flux response, reduced the desensitization by proadifen. These results are compatible with the hypothesis that certain noncompetitive antagonists modify receptor function by stabilizing the same high-affinity (desensitized) conformation that is stabilized by agonists, either as a consequence of binding to the allosteric site or by an alternate mechanism.

Research Organization:
Harvard Medical School, Boston, MA
OSTI ID:
5779430
Journal Information:
Biochemistry; (United States), Vol. 23:18
Country of Publication:
United States
Language:
English

Similar Records

Reaction of (3H)meproadifen mustard with membrane-bound Torpedo acetylcholine receptor
Journal Article · Wed Oct 15 00:00:00 EDT 1986 · J. Biol. Chem.; (United States) · OSTI ID:5779430

Calcium-dependent effect of the thymic polypeptide thymopoietin on the desensitization of the nicotinic acetylcholine receptor
Journal Article · Fri May 01 00:00:00 EDT 1987 · Proc. Natl. Acad. Sci. U.S.A.; (United States) · OSTI ID:5779430

Conformational states of the nicotinic acetylcholine receptor from Torpedo californica induced by the binding of agonists, antagonists, and local anesthetics. Equilibrium measurements using tritium-hydrogen exchange
Journal Article · Tue Jan 10 00:00:00 EST 1989 · Biochemistry; (United States) · OSTI ID:5779430