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Science Forum Index » Life Extension Forum » Reversing Inactivation of peroxiredoxins.
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| Tim |
 Posted: Fri Jan 02, 2004 1:01 pm |
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Science. 2003 Apr 25;300(5619):653-6. Related Articles, Links
Comment in:
Science. 2003 Apr 25;300(5619):592-4.
Reversing the inactivation of peroxiredoxins caused by cysteine
sulfinic acid formation.
Woo HA, Chae HZ, Hwang SC, Yang KS, Kang SW, Kim K, Rhee SG.
Center for Cell Signaling Research and Division of Molecular Life
Sciences, Ewha Womans University, Seoul 120-750, Korea.
The active-site cysteine of peroxiredoxins is selectively oxidized to
cysteine sulfinic acid during catalysis, which leads to inactivation
of peroxidase activity. This oxidation was thought to be irreversible.
However, by metabolic labeling of mammalian cells with 35S, we show
that the sulfinic form of peroxiredoxin I, produced during the
exposure of cells to H2O2, is rapidly reduced to the catalytically
active thiol form. The mammalian cells' ability to reduce protein
sulfinic acid might serve as a mechanism to repair oxidatively damaged
proteins or represent a new type of cyclic modification by which the
function of various proteins is regulated.
PMID: 12714748 [PubMed - indexed for MEDLINE] |
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