Autor: |
Chen, Pu, Hao, Wenshan, Rife, Lawrence, Wang, Xiao Peng, Shen, Daiwei, Chen, Jeannie, Ogden, Thomas, Van Boemel, Gretchen B., Wu, Lanyin, Yang, Mao, Fong, Henry K.W. |
Předmět: |
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Zdroj: |
Nature Genetics; Jul2001, Vol. 28 Issue 3, p256, 5p |
Abstrakt: |
During visual excitation, rhodopsin undergoes photoactivation and bleaches to opsin and all-trans-retinal. To regenerate rhodopsin and maintain normal visual sensitivity, the all-trans isomer must be metabolized and reisomerized to produce the chromophore 11-cis-retinal in biochemical steps that constitute the visual cycle and involve the retinal pigment epithelium (RPE; refs. 3?8). A key step in the visual cycle is isomerization of an all-trans retinoid to 11-cis-retinol in the RPE (refs. 9?11). It could be that the retinochrome-like opsins, peropsin, or the retinal G protein-coupled receptor (RGR) opsin12?16 are isomerases in the RPE. In contrast to visual pigments, RGR is bound predominantly to endogenous all-trans-retinal, and irradiation of RGR in vitro results in stereospecific conversion of the bound all-trans isomer to 11-cis-retinal. Here we show that RGR is involved in the formation of 11-cis-retinal in mice and functions in a light-dependent pathway of the rod visual cycle. Mutations in the human gene encoding RGR are associated with retinitis pigmentosa. [ABSTRACT FROM AUTHOR] |
Databáze: |
Complementary Index |
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