Prolonged survival of the phosphorylated form of rhodopsin during dark adaptation of Royal College Surgeons rat

FEBS Letters

Ohguro, Hiroshi¹  Nakazawa, Mitsuru¹  Maeda, Tadao²  Mamiya, Kazuhisa¹  Ohguro, Ikuyo¹ 

[1] Department of Ophthalmology, Hirosaki University School of Medicine, 5 Zaifu-cho, Hirosaki, Aomori 036-8562, USA;Departments of Ophthalmology, University of Washington, School of Medicine, Seattle, WA 98195, USA

关键词: Rhodopsin;    Phosphorylation;    Retinal degeneration;    Immunocytochemistry;   

DOI  :  10.1016/S0014-5793(03)00908-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

To study rhodopsin (Rho) phosphorylation and dephosphorylation in Royal College of Surgeons (RCS) rat retina, specific antibodies toward major Rho phosphorylation sites in vivo, 334Ser or 338Ser, were prepared by immunization of authentic phosphorylated peptides in rabbit. Enzyme-linked immunosorbent assay identified that the raised antibodies exclusively recognized either the phosphorylated 334Ser or 338Ser site. In immunofluorescence labeling, both antibodies recognized photoreceptor outer segments in light-adapted retinas from Sprague–Dawley (SD), Brown–Norway (BN) and RCS rat. During dark adaptation, immunoreactivities toward phosphorylated 338Ser and 334Ser sites were diminished within several hours (0.2–2 h) in SD and BN rat retinas. However, those toward phosphorylated 338Ser and 334Ser sites were diminished within 4 to 7 days in RCS rat retinas. In vitro studies demonstrated decreased levels of both Rho phosphorylation and dephosphorylation reactions in RCS retinas. However, the dephosphorylation reaction was much more greatly affected than the phosphorylation reaction. Extremely prolonged survival of phosphorylated forms of Rho may contribute to persistent misregulation of phototransduction processes in retinal degeneration in RCS rat.

【 授权许可】

Unknown