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¹ Department of Ophthalmology, Harvard Medical School and the Massachusetts Eye and Ear Infirmary, Boston, MA 02114
² Department of Neurobiology, Stanford University School of Medicine, Stanford, CA 94305
³ Zilkha Neurogenetic Institute, Beckman Macular Research Center, Doheny Eye Institute
⁴ Departments of Ophthalmology and Cell and Neurobiology, Keck School of Medicine of the University of Southern California, Los Angeles, CA 90089
⁵ Center for Neuroscience and Department of Psychiatry and Behavioral Sciences, University of California, Davis, CA 95616
⁶ Division of Biology, California Institute of Technology, Pasadena, CA 91125

Address correspondence to Clint L. Makino, Department of Ophthalmology, Harvard Medical School and the Massachusetts Eye and Ear Infirmary, 243 Charles Street, Boston, MA 02114. Fax: (617) 573-4290; email: cmakino{at}meei.harvard.edu

The Ca²⁺-binding protein recoverin may regulate visual transduction in retinal rods and cones, but its functional role and mechanism of action remain controversial. We compared the photoresponses of rods from control mice and from mice in which the recoverin gene was knocked out. Our analysis indicates that Ca²⁺-recoverin prolongs the dark-adapted flash response and increases the rod's sensitivity to dim steady light. Knockout rods had faster Ca²⁺ dynamics, indicating that recoverin is a significant Ca²⁺ buffer in the outer segment, but incorporation of exogenous buffer did not restore wild-type behavior. We infer that Ca²⁺-recoverin potentiates light-triggered phosphodiesterase activity, probably by effectively prolonging the catalytic activity of photoexcited rhodopsin.

Key Words: calcium-binding proteins • knockout mice • light adaptation • photoreceptors • phototransduction

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