Open AccessIrreversible hyperoxidation of peroxiredoxin 2 is caused by tert‐ butyl hydroperoxide in human red blood cells
Author(s) -
Ishida Y.I.,
Takikawa M.,
Suzuki T.,
Nagahama M.,
Ogasawara Y.
Publication year - 2014
Publication title -
febs open bio
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.718
H-Index - 31
ISSN - 2211-5463
DOI - 10.1016/j.fob.2014.10.003
Subject(s) - peroxiredoxin , chemistry , tert butyl hydroperoxide , oxidative stress , biochemistry , microbiology and biotechnology , enzyme , biology , catalysis , peroxidase
Peroxiredoxin 2 (Prx2) is the third most abundant protein in red blood cells (RBCs). In this study, we have succeeded in implementing the rapid and simultaneous detection of the hyperoxidized (Prx2‐SO 2/3 ) and reduced (Prx2‐SH) forms of Prx2 in human RBCs using reverse phase high‐performance liquid chromatography. The detection of a peak corresponding to Prx2‐SO 2/3 was clearly observed following treatment of tert ‐butyl hydroperoxide ( t ‐BHP), but not H 2 O 2 , and was found to be dose‐dependent. The identity of the peak was confirmed as Prx2 by immunoblotting and mass spectrometry analysis. Our results suggest that t ‐BHP hyperoxidizes cysteine residues in Prx2 more readily than H 2 O 2 , and that accumulation of hyperoxidized Prx2 might reflect disruption of redox homeostasis in RBCs.