Selenoprotein expression and function-Selenoprotein W

被引:62
作者
Whanger, P. D. [1 ]
机构
[1] Oregon State Univ, Dept Environm & Mol Toxicol, Corvallis, OR 97330 USA
来源
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS | 2009年 / 1790卷 / 11期
关键词
Mammalian selenoprotein W; Amino acid sequence; Glutathione; Possible metabolic function; GLUTATHIONE-PEROXIDASE; DIETARY SELENIUM; SKELETAL-MUSCLE; MESSENGER-RNA; BRAIN; DISEASE; TISSUES; CELLS; SE;
D O I
10.1016/j.bbagen.2009.05.010
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Selenoprotein W (SeW) is a small selenoprotein (85 to 88 amino acids) first identified in sheep suffering from selenium deficiency. The levels are highest in muscle, heart (except rodents) spleen and brain. The deduced amino acid sequence has been obtained for mice, rats, monkeys, humans, sheep, pigs, fish and chickens. The sequences of Sew are identical in rats and mice as well as monkeys and humans. In all eight species of animals cysteine is present at residue number 9 and selenocysteine at residue number 13. Residue number 37 is cysteine in six species of animal with fish and chickens as the exceptions. Of those examined, the rodent Sew is the only one containing four cysteines whereas the others contain only two cysteines. Glutathionylaltion has been shown for Sew from rats and monkeys but has not been confirmed for this selenoprotein from the other six animals. The biological function of Sew has not been definitely identified. Evidence has been obtained that it can serve as an antioxidant, responds to stress, involved in cell immunity, specific target for methylmercury, and has thioredoxin-like function. (C) 2009 Published by Elsevier B.V.
引用
收藏
页码:1448 / 1452
页数:5
相关论文
共 43 条
[11]   SelT, SelW, SelH, and Rdx12: Genomics and molecular insights into the functions of selenoproteins of a novel thioredoxin-like family [J].
Dikiy, Alexander ;
Novoselov, Sergey V. ;
Fomenko, Dmitri E. ;
Sengupta, Aniruddha ;
Carlson, Bradley A. ;
Cerny, Ronald L. ;
Ginalski, Krzysztof ;
Grishin, Nick V. ;
Hatfield, Dolph L. ;
Gladyshev, Vadim N. .
BIOCHEMISTRY, 2007, 46 (23) :6871-6882
[12]  
Gladwin MT, 2006, NAT CHEM BIOL, V2, P110, DOI 10.1038/nchembio0206-110
[13]  
GU BQ, 1983, CHINESE MED J-PEKING, V96, P251
[14]   Selenoprotein W gene regulation by selenium in L8 cells [J].
Gu, QP ;
Ream, W ;
Whanger, PD .
BIOMETALS, 2002, 15 (04) :411-420
[15]   Purification, characterization, and glutathione binding to selenoprotein W from monkey muscle [J].
Gu, QP ;
Beilstein, MA ;
Barofsky, E ;
Ream, W ;
Whanger, PD .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1999, 361 (01) :25-33
[16]   Selenoprotein W accumulates primarily in primate skeletal muscle, heart, brain and tongue [J].
Gu, QP ;
Sun, Y ;
Ream, LW ;
Whanger, PD .
MOLECULAR AND CELLULAR BIOCHEMISTRY, 2000, 204 (1-2) :49-56
[17]   Deletion analysis of the rodent selenoprotein W promoter [J].
Hooven, LA ;
Vorachek, WR ;
Bauman, AB ;
Butler, JA ;
Ream, LW ;
Whanger, PD .
JOURNAL OF INORGANIC BIOCHEMISTRY, 2005, 99 (10) :2007-2012
[18]   Selenoprotein W is a glutathione-dependent antioxidant in vivo [J].
Jeong, DW ;
Kim, TS ;
Chung, YW ;
Lee, BJ ;
Kim, IY .
FEBS LETTERS, 2002, 517 (1-3) :225-228
[19]  
Jeong DW, 2004, MOL CELLS, V17, P156
[20]   Selenoprotein W as molecular target of methylmercury in human neuronal cells is down-regulated by GSH depletion [J].
Kim, YJ ;
Chai, YG ;
Ryu, JC .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2005, 330 (04) :1095-1102