Selenophosphate synthetase 1 is an essential protein with roles in regulation of redox homoeostasis in mammals

被引:33
|
作者
Tobe, Ryuta [1 ]
Carlson, Bradley A. [1 ]
Huh, Jang Hoe [2 ]
Castro, Nadia P. [3 ]
Xu, Xue-Ming [1 ,10 ]
Tsuji, Petra A. [4 ]
Lee, Sang-Goo [5 ]
Bang, Jeyoung [2 ]
Na, Ji-Woon [2 ]
Kong, Young-Yun [2 ]
Beaglehole, Daniel [1 ]
Southon, Eileen [6 ]
Seifried, Harold [7 ]
Tessarollo, Lino [8 ]
Salomon, David S. [3 ]
Schweizer, Ulrich [9 ]
Gladyshev, Vadim N. [5 ]
Hatfield, Dolph L. [1 ]
Lee, Byeong Jae [2 ]
机构
[1] NIH, Mol Biol Selenium, Mouse Canc Genet Program, Ctr Canc Res, Bldg 10, Bethesda, MD 20892 USA
[2] Seoul Natl Univ, Sch Biol Sci, Seoul 151742, South Korea
[3] NIH, Tumor Growth Factor Sect, Mouse Canc Genet Program, Ctr Canc Res, Bldg 10, Bethesda, MD 20892 USA
[4] Towson Univ, Dept Biol Sci, Towson, MD 21252 USA
[5] Harvard Med Sch, Brigham & Womens Hosp, Div Genet, Boston, MA 02115 USA
[6] NCI Frederick, Basic Sci Program, SAIC Frederick, Frederick, MD 21702 USA
[7] NCI, Nutr Sci Res Grp, Bethesda, MD 20892 USA
[8] NIH, Neural Dev Sect, Mouse Canc Genet Program, Ctr Canc Res, Bldg 10, Bethesda, MD 20892 USA
[9] Rhein Friedrich Wilhelms Univ Bonn, Inst Biochem & Mol Biol, D-53115 Bonn, Germany
[10] Genecopoeia Inc, 9620 Med Ctr Dr 101, Rockville, MD 20850 USA
基金
美国国家卫生研究院; 新加坡国家研究基金会;
关键词
cancer; reactive oxygen species (ROS); redox regulation; selenium; selenocysteine; selenophosphate synthetase 1; SELENOPROTEIN BIOSYNTHESIS; GLUTATHIONE TRANSFERASE; THIOREDOXIN REDUCTASE; GENETIC-CODE; SELENOCYSTEINE; SELENIUM; METABOLISM; EXPRESSION; DROSOPHILA; CELLS;
D O I
10.1042/BCJ20160393
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
Selenophosphate synthetase (SPS) was initially detected in bacteria and was shown to synthesize selenophosphate, the active selenium donor. However, mammals have two SPS paralogues, which are designated SPS1 and SPS2. Although it is known that SPS2 catalyses the synthesis of selenophosphate, the function of SPS1 remains largely unclear. To examine the role of SPS1 in mammals, we generated a Sps1-knockout mouse and found that systemic SPS1 deficiency led to embryos that were clearly underdeveloped by embryonic day (E)8.5 and virtually resorbed by E14.5. The knockout of Sps1 in the liver preserved viability, but significantly affected the expression of a large number of mRNAs involved in cancer, embryonic development and the glutathione system. Particularly notable was the extreme deficiency of glutaredoxin 1 (GLRX1) and glutathione transferase Omega 1 (GSTO1). To assess these phenotypes at the cellular level, we targeted the removal of SPS1 in F9 cells, a mouse embryonal carcinoma (EC) cell line, which affected the glutathione system proteins and accordingly led to the accumulation of hydrogen peroxide in the cell. Furthermore, we found that several malignant characteristics of SPS1-deficient F9 cells were reversed, suggesting that SPS1 played a role in supporting and/or sustaining cancer. In addition, the overexpression of mouse or human GLRX1 led to a reversal of observed increases in reactive oxygen species (ROS) in the F9 SPS1/GLRX1-deficient cells and resulted in levels that were similar to those in F9 SPS1-sufficient cells. The results suggested that SPS1 is an essential mammalian enzyme with roles in regulating redox homoeostasis and controlling cell growth.
引用
收藏
页码:2141 / 2154
页数:14
相关论文
共 50 条
  • [31] Redox regulation of the tumor suppressor protein p27kip1
    Bedford, Rebecca M.
    Sheaff, Robert J.
    ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 2009, 237
  • [32] Protective roles of redox-active protein thioredoxin-1 for severe acute pancreatitis
    Ohashi, S
    Nishio, A
    Nakamura, H
    Kido, M
    Ueno, S
    Uza, N
    Inoue, S
    Kitamura, H
    Kiriya, K
    Asada, M
    Tamaki, H
    Matsuura, M
    Kawasaki, K
    Fukui, T
    Watanabe, N
    Nakase, H
    Yodoi, J
    Okazaki, K
    Chiba, T
    AMERICAN JOURNAL OF PHYSIOLOGY-GASTROINTESTINAL AND LIVER PHYSIOLOGY, 2006, 290 (04): : G772 - G781
  • [33] Emergence of hormonal and redox regulation of galectin-1 in placental mammals: Implication in maternal-fetal immune tolerance
    Than, Nanclor Gabor
    Romero, Roberto
    Erez, Offer
    Weckle, Amy
    Tarca, Adi L.
    Hotra, John
    Abbas, Asad
    Han, Yu Mi
    Kim, Sung-Su
    Kusanovic, Juan Pedro
    Gotsch, Francesca
    Hou, Zhuocheng
    Santolaya-Forgas, Joaquin
    Benirschke, Kurt
    Papp, Zoltan
    Grossman, Lawrence I.
    Goodman, Morris
    Wildman, Derek E.
    PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2008, 105 (41) : 15819 - 15824
  • [34] The redox/DNA repair protein, Ref-1, is essential for early embryonic development in mice
    Xanthoudakis, S
    Smeyne, RJ
    Wallace, JD
    Curran, T
    PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (17) : 8919 - 8923
  • [35] The redox/DNA repair protein, Ref-1, is essential for early embryonic development in mice
    Xanthoudakis, S.
    Smeyne, R. J.
    Wallace, J. D.
    Curran, T.
    Proceedings of the National Academy of Sciences of the United States of America, 93 (17):
  • [36] Redox-dependent regulation of end-binding protein 1 activity by glutathionylation
    Miao Chen
    Jian Wang
    Yang Yang
    Tao Zhong
    Peng Zhou
    Huixian Ma
    Jingrui Li
    Dengwen Li
    Jun Zhou
    Songbo Xie
    Min Liu
    Science China(Life Sciences) , 2021, (04) : 575 - 583
  • [37] Protein Disulfide Isomerase A1 is a Central Hub for Redox Regulation of VSMC Phenotype
    Wosniak, Joao
    Goncalves, Renata C.
    Tanaka, Leonardo Y.
    Zanatta, Daniela B.
    Strauss, Bryan E.
    Laurindo, Francisco R.
    Fernandes, Denise C.
    ARTERIOSCLEROSIS THROMBOSIS AND VASCULAR BIOLOGY, 2017, 37
  • [38] Redox-dependent regulation of end-binding protein 1 activity by glutathionylation
    Miao Chen
    Jian Wang
    Yang Yang
    Tao Zhong
    Peng Zhou
    Huixian Ma
    Jingrui Li
    Dengwen Li
    Jun Zhou
    Songbo Xie
    Min Liu
    Science China Life Sciences, 2021, 64 : 575 - 583
  • [39] Redox regulation of SurR by protein disulfide oxidoreductase in Thermococcus onnurineus NA1
    Lim, Jae Kyu
    Jung, Hae-Chang
    Kang, Sung Gyun
    Lee, Hyun Sook
    EXTREMOPHILES, 2017, 21 (03) : 491 - 498
  • [40] Redox regulation of protein tyrosine phosphatase 1B function by an organic peroxide
    Bhattacharyya, Sanjib
    Gates, Kent S.
    ABSTRACTS OF PAPERS OF THE AMERICAN CHEMICAL SOCIETY, 2007, 234