In vivoAND PHOTOPHYSICAL STUDIES ON PHOTOOXIDATIVE DAMAGE TO LENS PROTEINS AND THEIR PROTECTION BY RADIOPROTECTORS
作者:
JOAN E. ROBERTS,
JUDITH S. KINLEY,
ANTONY R. YOUNG,
GLORIA JENKINS,
STEPHEN J. ATHERTON,
JAMES DILLON,
期刊:
Photochemistry and Photobiology
(WILEY Available online 1991)
卷期:
Volume 53,
issue 1
页码: 33-38
ISSN:0031-8655
年代: 1991
DOI:10.1111/j.1751-1097.1991.tb08464.x
出版商: Blackwell Publishing Ltd
数据来源: WILEY
摘要:
Abstract—Photooxidation, whether initiated by an endogenous or exogenous sensitizer, is an important mechanism in light induced damage to the lens. One of the substrates for this damage is lens protein. A porphyrin sensitizer which binds to lens proteins [mesotetra(p‐sulfonatophenyl) porphyrin (TPPS)] was found to photooxidize Skh‐2 pigmented mice lens proteinin vivo.Uroporphyrin, a model for a non‐binding photosensitizer, did not induce photooxidative damage to the mouse lens.The radioprotector 3‐amino‐2‐hydroxypropyl phosphorothioate (WR‐77913) was investigated as an agent to retard or negatein vivophotooxidative damage to the lens. Intraperitoneal injections of WR‐77913 prior to irradiation reduced the TPPS induced photodestruction of lens protein in Skh‐2 pigmented mice.The mechanism of protection was also investigated. Thiols were found to quench both the triplet state of porphyrins and the reactive intermediate singlet oxygen on the order of 105and 106M‐1s1respectively. These are probably not fast enough to explain most of the protection afforded by thiols. An additional mechanism may be the accelerated photobleaching of porphyrins by thiols which protects tissue by reducing the absorptions
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