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.
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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
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Original Russian Text © M. Yu. Loginova, Ye. V. Rostovtseva, T. B. Feldman, M. A. Ostrovsky, 2008, published in Biokhimiya, 2008, Vol. 73, No. 2, pp. 162–172.
Originally published in Biochemistry (Moscow) On-Line Papers in Press, as Manuscript BM07-249, December 16, 2007.
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Loginova, M.Y., Rostovtseva, Y.V., Feldman, T.B. et al. Light damaging action of all-trans-retinal and its derivatives on rhodopsin molecules in the photoreceptor membrane. Biochemistry Moscow 73, 130–138 (2008). https://doi.org/10.1134/S000629790802003X
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DOI: https://doi.org/10.1134/S000629790802003X