Biochemistry (Moscow)

, Volume 73, Issue 2, pp 130–138

Light damaging action of all-trans-retinal and its derivatives on rhodopsin molecules in the photoreceptor membrane

  • M. Yu. Loginova
  • Ye. V. Rostovtseva
  • T. B. Feldman
  • M. A. Ostrovsky
Accelerated Publication

DOI: 10.1134/S000629790802003X

Cite this article as:
Loginova, M.Y., Rostovtseva, Y.V., Feldman, T.B. et al. Biochemistry Moscow (2008) 73: 130. doi:10.1134/S000629790802003X

Abstract

We have reproduced the model system containing A2-rhodopsin, NR-PE, A2-PE, and ATR-dimer-PE in order to study photosensitized damage of rhodopsin within photoreceptor membranes of rod outer segments. We have demonstrated that irradiation of such a system with visible light (400–700 nm) distorts the most important functional property of native visual pigment—its ability to regenerate after addition of 11-cis-retinal in the dark. We have also shown that all-trans-retinal bound to membrane phospholipids and rhodopsin has less photosensitizing activity that free all-trans-retinal.

Key words

visual pigment rhodopsinall-trans-retinalphotosensitizersphotodamage

Abbreviations

ABCR

ATP-binding cassette transporter

A2E

N-bis-retinylidene-ethanolamine

A2-PE

N-bis-retinylidene-phosphatidylethanolamine

A2-rhodopsin

rhodopsin which has each of its three lysine residues modified with two all-trans-retinal molecules

ATR

all-trans-retinal

ATR-dimer-PE

all-trans-retinal-dimer-phosphatidylethanolamine

NR-PE

N-retinylidene-phosphatidylethanolamine

ROS

rod outer segments

Copyright information

© Pleiades Publishing, Ltd. 2008

Authors and Affiliations

  • M. Yu. Loginova
    • 1
  • Ye. V. Rostovtseva
    • 1
  • T. B. Feldman
    • 1
  • M. A. Ostrovsky
    • 1
  1. 1.Emanuel’ Institute of Biochemical PhysicsRussian Academy of SciencesMoscowRussia