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Published online 10 November 2003 doi:10.1085/jgp.200308938
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© Rockefeller University Press, 0022-1295/2003/12/703/ $5.00
Journal of General Physiology, Volume 122, Number 6, December 2003 703-712

Novel Form of Adaptation in Mouse Retinal Rods Speeds Recovery of Phototransduction

Claudia M. Krispel1, Ching-Kang Chen2, Melvin I. Simon3 and Marie E. Burns1

1 Center for Neuroscience and Department of Psychiatry and Behavioral Sciences, University of California, Davis, Davis, CA 95616
2 Department of Ophthalmology and Visual Sciences, University of Utah, Salt Lake City, UT 84112
3 Division of Biology, 147-75, California Institute of Technology, Pasadena, CA 91125

Address correspondence to Marie E. Burns, Center for Neuroscience, University of California, Davis, 1544 Newton Court, Davis, CA 95616. Fax: (530) 754-7382; email: meburns{at}ucdavis.edu

Photoreceptors of the retina adapt to ambient light in a manner that allows them to detect changes in illumination over an enormous range of intensities. We have discovered a novel form of adaptation in mouse rods that persists long after the light has been extinguished and the rod's circulating dark current has returned. Electrophysiological recordings from individual rods showed that the time that a bright flash response remained in saturation was significantly shorter if the rod had been previously exposed to bright light. This persistent adaptation did not decrease the rate of rise of the response and therefore cannot be attributed to a decrease in the gain of transduction. Instead, this adaptation was accompanied by a marked speeding of the recovery of the response, suggesting that the step that rate-limits recovery had been accelerated. Experiments on knockout rods in which the identity of the rate-limiting step is known suggest that this adaptive acceleration results from a speeding of G protein/effector deactivation.

Key Words: photoreceptors • GTP-binding proteins • kinetics • phototransduction • knock-out mice


Abbreviation used in this paper: PDE, phosphodiesterase.


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