Protein-protein interactions and lens transparency

被引:69
作者
Takemoto, Larry [1 ]
Sorensen, Christopher M. [2 ]
机构
[1] Kansas State Univ, Div Biol, Manhattan, KS 66506 USA
[2] Kansas State Univ, Dept Phys, Manhattan, KS 66506 USA
基金
美国国家卫生研究院;
关键词
lens transparency; cataract;
D O I
10.1016/j.exer.2008.08.018
中图分类号
R77 [眼科学];
学科分类号
100212 ;
摘要
Past studies have identified posttranslational modifications of human lens proteins occurring during cataract formation, and have also demonstrated that protein-protein interactions exist between different lens crystallins. Based upon current theories of lens transparency, these posttranslational modifications and their possible effects upon crystallin interactions may be the key to understanding why the lens is able to transmit light, and why transmission is decreased during cataractogenesis. This review will summarize current knowledge of posttranslational modifications during human cataractogenesis, and will propose their possible role in protein-protein interactions that are thought to be necessary for lens transparency. Based upon this premise, model systems will be described that will test the validity of the theory. (C) 2008 Elsevier Ltd. All rights reserved.
引用
收藏
页码:496 / 501
页数:6
相关论文
共 64 条
[1]  
ANDLEY UP, 2008, KNOCK MOUSE MODEL R1
[2]   THEORY OF TRANSPARENCY OF EYE [J].
BENEDEK, GB .
APPLIED OPTICS, 1971, 10 (03) :459-&
[3]   Alpha-b crystallin gene (CRYAB) mutation causes dominant congenital posterior polar cataract in humans [J].
Berry, V ;
Francis, P ;
Reddy, MA ;
Collyer, D ;
Vithana, E ;
MacKay, I ;
Dawson, G ;
Carey, AH ;
Moore, A ;
Bhattacharya, SS ;
Quinlan, RA .
AMERICAN JOURNAL OF HUMAN GENETICS, 2001, 69 (05) :1141-1145
[4]   TOPOGRAPHIC CORRESPONDENCE BETWEEN TOTAL AND NONFREEZABLE WATER-CONTENT AND THE APPEARANCE OF CATARACT IN HUMAN LENSES [J].
BETTELHEIM, FA ;
CASTORO, JA ;
WHITE, O ;
CHYLACK, LT .
CURRENT EYE RESEARCH, 1986, 5 (12) :925-932
[5]  
BETTELHEIM FA, 1986, INVEST OPHTH VIS SCI, V27, P122
[6]   Thermodynamic stability of bovine α-crystallin in its interactions with other bovine crystallins [J].
Bettelheim, FA ;
Chen, A .
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 1998, 22 (3-4) :247-252
[7]   Role of ATP on the interaction of α-crystallin with its substrates and its implications for the molecular chaperone function [J].
Biswas, A ;
Das, KP .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (41) :42648-42657
[8]   VERTEBRATE EYE LENS [J].
BLOEMENDAL, H .
SCIENCE, 1977, 197 (4299) :127-138
[9]  
BOYLE DL, 2003, BMC OPHTHALMOL, V3, P1
[10]   The ageing lens [J].
Bron, AJ ;
Vrensen, GFJM ;
Koretz, J ;
Maraini, G ;
Harding, JJ .
OPHTHALMOLOGICA, 2000, 214 (01) :86-104