TY - JOUR
T1 - Alterations in mitochondrial and cytosolic methionine sulfoxide reductase activity during cardiac ischemia and reperfusion
AU - Picot, Cédric R.
AU - Perichon, Martine
AU - Lundberg, Kathleen C.
AU - Friguet, Bertrand
AU - Szweda, Luke I.
AU - Petropoulos, Isabelle
N1 - Funding Information:
This work was supported by a grant from NIH/NIA (AG-19357-03). The authors thank Dr Anne-Laure Bulteau for helpful discussion.
PY - 2006/7
Y1 - 2006/7
N2 - During cardiac ischemia/reperfusion, proteins are targets of reactive oxygen species produced by the mitochondrial respiratory chain resulting in the accumulation of oxidatively modified protein. Sulfur-containing amino acids are among the most sensitive to oxidation. Certain cysteine and methionine oxidation products can be reversed back to their reduced form within proteins by specific repair enzymes. Oxidation of methionine in protein produces methionine-S-sulfoxide and methionine-R-sulfoxide that can be catalytically reduced by two stereospecific enzymes, methionine sulfoxide reductases A and B, respectively. Due to the importance of the methionine sulfoxide reductase system in the maintenance of protein structure and function during conditions of oxidative stress, the fate of this system during ischemia/reperfusion was investigated. Mitochondrial and cytosolic methionine sulfoxide reductase activities are decreased during ischemia and at early times of reperfusion, respectively. Partial recovery of enzyme activity was observed upon extended periods of reperfusion. Evidence indicates that loss in activity is not due to a decrease in the level of MsrA but may involve structural modification of the enzyme.
AB - During cardiac ischemia/reperfusion, proteins are targets of reactive oxygen species produced by the mitochondrial respiratory chain resulting in the accumulation of oxidatively modified protein. Sulfur-containing amino acids are among the most sensitive to oxidation. Certain cysteine and methionine oxidation products can be reversed back to their reduced form within proteins by specific repair enzymes. Oxidation of methionine in protein produces methionine-S-sulfoxide and methionine-R-sulfoxide that can be catalytically reduced by two stereospecific enzymes, methionine sulfoxide reductases A and B, respectively. Due to the importance of the methionine sulfoxide reductase system in the maintenance of protein structure and function during conditions of oxidative stress, the fate of this system during ischemia/reperfusion was investigated. Mitochondrial and cytosolic methionine sulfoxide reductase activities are decreased during ischemia and at early times of reperfusion, respectively. Partial recovery of enzyme activity was observed upon extended periods of reperfusion. Evidence indicates that loss in activity is not due to a decrease in the level of MsrA but may involve structural modification of the enzyme.
KW - Ischemia-reperfusion
KW - Methionine sulfoxide reductase
KW - Mitochondria
KW - MsrA
KW - Oxidized protein repair
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U2 - 10.1016/j.exger.2006.03.011
DO - 10.1016/j.exger.2006.03.011
M3 - Short survey
C2 - 16677789
AN - SCOPUS:33745060719
SN - 0531-5565
VL - 41
SP - 663
EP - 667
JO - Experimental Gerontology
JF - Experimental Gerontology
IS - 7
ER -