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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Kawamura, Satoru Tachibanaki, Shuji Tomizuka, Junko |
| Description | Author Affiliation: Tomizuka J ( From the Graduate School of Frontier Biosciences.); Tachibanaki S ( From the Graduate School of Frontier Biosciences, Department of Biological Sciences, Graduate School of Science, Osaka University, Yamada-oka 1-3, Suita, Osaka 565-0871, Japan.); Kawamura S ( From the Graduate School of Frontier Biosciences, Department of Biological Sciences, Graduate School of Science, Osaka University, Yamada-oka 1-3, Suita, Osaka 565-0871, Japan kawamura@fbs.osaka-u.ac.jp.) |
| Abstract | Visual pigment in photoreceptors is activated by light. Activated visual pigment (R*) is believed to be inactivated by phosphorylation of R* with subsequent binding of arrestin. There are two types of photoreceptors, rods and cones, in the vertebrate retina, and they express different subtypes of arrestin, rod and cone type. To understand the difference in the function between rod- and cone-type arrestin, we first identified the subtype of arrestins expressed in rods and cones in carp retina. We found that two rod-type arrestins, rArr1 and rArr2, are co-expressed in a rod and that a cone-type arrestin, cArr1, is expressed in blue- and UV-sensitive cones; the other cone-type arrestin, cArr2, is expressed in red- and green-sensitive cones. We quantified each arrestin subtype and estimated its concentration in the outer segment of a rod or a cone in the dark; they were â ¼0.25 mm (rArr1 plus rArr2) in a rod and 0.6-0.8 mm (cArr1 or cArr2) in a cone. The effect of each arrestin was examined. In contrast to previous studies, both rod and cone arrestins suppressed the activation of transducin in the absence of visual pigment phosphorylation, and all of the arrestins examined (rArr1, rArr2, and cArr2) bound transiently to most probably nonphosphorylated R*. One rod arrestin, rArr2, bound firmly to phosphorylated pigment, and the other two, rArr1 and cArr2, once bound to phosphorylated R* but dissociated from it during incubation. Our results suggested a novel mechanism of arrestin effect on the suppression of the R* activity in both rods and cones. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 15 |
| Volume Number | 290 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2015-04-10 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Arrestin Metabolism Carps Fish Proteins Retinal Cone Photoreceptor Cells Retinal Pigments Retinal Rod Photoreceptor Cells Animals Genetics Guanosine 5'-O-(3-Thiotriphosphate) Immunoblotting Immunohistochemistry Phosphorylation Protein Binding Radiation Effects Transducin Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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