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Role of the PLA 2 ‐independent peroxiredoxin VI activity in the survival of immortalized fibroblasts exposed to cytotoxic oxidative stress
Author(s) -
Salmon Michel,
Dedessus Le Moutier Jérémie,
Wenders Frédéric,
Chiarizia Sophie,
Eliaers François,
Remacle José,
Royer Véronique,
Pascal Thierry,
Toussaint Olivier
Publication year - 2004
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/s0014-5793(03)01437-6
Subject(s) - peroxiredoxin , cytotoxic t cell , oxidative stress , glutathione peroxidase , transfection , phospholipase , microbiology and biotechnology , glutathione , peroxidase , chemistry , phospholipase a2 , phospholipase a , cell culture , gpx1 , biochemistry , biology , enzyme , in vitro , gene , genetics
Peroxiredoxin VI (PrxVI) is a bifunctional enzyme with non‐selenium glutathione peroxidase and Ca 2+ ‐independent acidic phospholipase A 2 activities. We demonstrate that transfection‐mediated PrxVI overexpression protects immortalized human WI‐38 and murine NIH3T3 fibroblasts against cytotoxic doses of tert ‐butylhydroperoxide and H 2 O 2 . Mutants for either glutathione peroxidase or phospholipase A 2 activity show that glutathione peroxidase but not phospholipase A 2 activity is required to promote cell survival after stress. Also, ectopic PrxVI overexpression does not protect telomerase‐stabilized WI‐38 fibroblasts against stress‐induced premature senescence.