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Molecular cloning and localization of rhodopsin kinase in the mammalian pineal

Published online by Cambridge University Press:  02 June 2009

Xinyu Zhao
Affiliation:
Department of Ophthalmology, University of Washington, Seattle Department of Pharmacology, University of Washington, Seattle
Françoise Haeseleer
Affiliation:
Department of Ophthalmology, University of Washington, Seattle
Robert N. Fariss
Affiliation:
Department of Ophthalmology, University of Washington, Seattle
Jing Huang
Affiliation:
Department of Ophthalmology, University of Washington, Seattle
Wolfgang Baehr
Affiliation:
Department of Ophthalmology, University of Utah, Health Sciences Center, Salt Lake City
Ann H. Milam
Affiliation:
Department of Ophthalmology, University of Washington, Seattle
Krzysztof Palczewski
Affiliation:
Department of Ophthalmology, University of Washington, Seattle Department of Pharmacology, University of Washington, Seattle

Abstract

Several retinal photoreceptor proteins involved in phototransduction have also been found in the mammalian pineal. This study demonstrates that rat and human pineals express protein kinases that are identical to the corresponding rod photoreceptor rhodopsin kinases. The deduced amino acid sequence of rat and human rhodopsin kinases have 84% sequence similarity to the earlier reported sequence of the bovine retinal enzyme, with complete conservation of the topological regions containing the position of the catalytic domain and sites of posttranslational modifications. Rat pineal also expresses rod opsin and putative blue cone opsin. Using immunocytochemistry, rod opsin and rhodopsin kinase were found to be co-localized in pinealocytes in the human tissue. These data demonstrate that the mammalian pineal contains light-sensitive opsins and a kinase involved in their inactivation. These findings correlate with an earlier report that neonatal rats show extraretinal light sensitivity, and suggest that a functional photoreceptive system may be present in the adult mammalian pineal.

Type
Research Articles
Copyright
Copyright © Cambridge University Press 1997

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