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Redox regulation of the tumor suppressor PTEN by glutathione
Author(s) -
Kim Yujeong,
Song Yong Bhum,
Kim Tae-Youl,
Kim Inyoung,
Han Seong-Jeong,
Ahn Younghee,
Cho Seung-Hyun,
Choi Cheol Yong,
Chay Kee-Oh,
Yang Sung Yeul,
Ahn Bong Whan,
Huh Won-Ki,
Lee Seung-Rock
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.07.006
Subject(s) - pten , tensin , gclc , glutathione , microbiology and biotechnology , phosphatase , glutathione reductase , biology , glutaredoxin , gene knockdown , biochemistry , pi3k/akt/mtor pathway , chemistry , phosphorylation , enzyme , signal transduction , glutathione peroxidase , gene
Phosphatase and tensin homolog deleted on chromosome 10 (PTEN) expressed in Saccharomyces cerevisiae was reversibly oxidized by hydrogen peroxide and reduced by cellular reductants. Reduction of hPTEN was delayed in each of S. cerevisiae gsh1Δ and gsh2Δ mutants. Expression of γ‐glutamylcysteine synthetase Gsh1 in the gsh1Δ mutant rescued regeneration rate of hPTEN. Oxidized hPTEN was reduced by glutathione in a concentration‐ and time‐dependent manner. Glutathionylated PTEN was detected. Incubation of 293T cells with BSO and knockdown expression of GCLc in HeLa cells by siRNA resulted in the delay of reduction of oxidized PTEN. Also, in HeLa cells transfected with GCLc siRNA, stimulation with epidermal growth factor resulted in the increase of oxidized PTEN and phosphorylation of Akt. These results suggest that the reduction of oxidized hPTEN is mediated by glutathione.