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

Biochemistry (Mosc). 2008 Feb;73(2):130-8. 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Isomerism
  • Light
  • Membrane Lipids / chemistry
  • Phosphatidylethanolamines / chemistry
  • Pyridinium Compounds / chemistry
  • Retinaldehyde / analogs & derivatives
  • Retinaldehyde / chemistry*
  • Retinaldehyde / radiation effects*
  • Retinoids / chemistry
  • Rhodopsin / chemistry*
  • Rhodopsin / metabolism
  • Rod Cell Outer Segment / chemistry*
  • Rod Cell Outer Segment / metabolism
  • Spectrometry, Fluorescence
  • Spectrophotometry, Ultraviolet

Substances

  • A2-PE compound
  • A2-rhodopsin
  • Membrane Lipids
  • N-retinylidene-phosphatidylethanolamine
  • Phosphatidylethanolamines
  • Pyridinium Compounds
  • Retinoids
  • retinal dimer phosphatidylethanolamine
  • Rhodopsin
  • Retinaldehyde