Reversible oxidation of mitochondrial peroxiredoxin 3 in mouse heart subjected to ischemia and reperfusion

V Kumar; N KItaef; MB Hampton; MB Cannell; CC Winterbourn

doi:10.1016/j.febslet.2009.02.018

Reversible oxidation of mitochondrial peroxiredoxin 3 in mouse heart subjected to ischemia and reperfusion

V Kumar
, N KItaef
, MB Hampton
, MB Cannell
, CC Winterbourn

Research output: Contribution to journal › Article (Academic Journal) › peer-review

45 Citations (Scopus)

Abstract

Peroxiredoxins decompose peroxides through reversible oxidation of their active site cysteines. The redox state of the 2-Cys peroxiredoxins, 1, 2 and 3, was investigated in mouse hearts undergoing ischemia and reperfusion in a Langendorff system. The peroxiredoxins were predominantly reduced in control hearts. Mitochondrial peroxiredoxin 3 underwent significant oxidation to its disulfide-linked dimer during ischemia. Oxidation was largely reversed during reperfusion. No redox changes in cytoplasmic peroxiredoxins 1 and 2 were apparent. Peroxiredoxin 3 oxidation suggests localized mitochondrial generation of reactive oxidants during ischemia. This local antioxidant activity of peroxiredoxin 3 may have a role in maintaining cardiac function.

Translated title of the contribution	Reversible oxidation of mitochondrial peroxiredoxin 3 in mouse heart subjected to ischemia and reperfusion
Original language	English
Pages (from-to)	997 - 1000
Number of pages	3
Journal	FEBS Letters
Volume	583
DOIs	https://doi.org/10.1016/j.febslet.2009.02.018
Publication status	Published - Mar 2009

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title = "Reversible oxidation of mitochondrial peroxiredoxin 3 in mouse heart subjected to ischemia and reperfusion",

abstract = "Peroxiredoxins decompose peroxides through reversible oxidation of their active site cysteines. The redox state of the 2-Cys peroxiredoxins, 1, 2 and 3, was investigated in mouse hearts undergoing ischemia and reperfusion in a Langendorff system. The peroxiredoxins were predominantly reduced in control hearts. Mitochondrial peroxiredoxin 3 underwent significant oxidation to its disulfide-linked dimer during ischemia. Oxidation was largely reversed during reperfusion. No redox changes in cytoplasmic peroxiredoxins 1 and 2 were apparent. Peroxiredoxin 3 oxidation suggests localized mitochondrial generation of reactive oxidants during ischemia. This local antioxidant activity of peroxiredoxin 3 may have a role in maintaining cardiac function.",

author = "V Kumar and N KItaef and MB Hampton and MB Cannell and CC Winterbourn",

year = "2009",

month = mar,

doi = "10.1016/j.febslet.2009.02.018",

language = "English",

volume = "583",

pages = "997 -- 1000",

journal = "FEBS Letters",

issn = "1873-3468",

publisher = "John Wiley and Sons Inc",

}

TY - JOUR

T1 - Reversible oxidation of mitochondrial peroxiredoxin 3 in mouse heart subjected to ischemia and reperfusion

AU - Kumar, V

AU - KItaef, N

AU - Hampton, MB

AU - Cannell, MB

AU - Winterbourn, CC

PY - 2009/3

Y1 - 2009/3

N2 - Peroxiredoxins decompose peroxides through reversible oxidation of their active site cysteines. The redox state of the 2-Cys peroxiredoxins, 1, 2 and 3, was investigated in mouse hearts undergoing ischemia and reperfusion in a Langendorff system. The peroxiredoxins were predominantly reduced in control hearts. Mitochondrial peroxiredoxin 3 underwent significant oxidation to its disulfide-linked dimer during ischemia. Oxidation was largely reversed during reperfusion. No redox changes in cytoplasmic peroxiredoxins 1 and 2 were apparent. Peroxiredoxin 3 oxidation suggests localized mitochondrial generation of reactive oxidants during ischemia. This local antioxidant activity of peroxiredoxin 3 may have a role in maintaining cardiac function.

AB - Peroxiredoxins decompose peroxides through reversible oxidation of their active site cysteines. The redox state of the 2-Cys peroxiredoxins, 1, 2 and 3, was investigated in mouse hearts undergoing ischemia and reperfusion in a Langendorff system. The peroxiredoxins were predominantly reduced in control hearts. Mitochondrial peroxiredoxin 3 underwent significant oxidation to its disulfide-linked dimer during ischemia. Oxidation was largely reversed during reperfusion. No redox changes in cytoplasmic peroxiredoxins 1 and 2 were apparent. Peroxiredoxin 3 oxidation suggests localized mitochondrial generation of reactive oxidants during ischemia. This local antioxidant activity of peroxiredoxin 3 may have a role in maintaining cardiac function.

U2 - 10.1016/j.febslet.2009.02.018

DO - 10.1016/j.febslet.2009.02.018

M3 - Article (Academic Journal)

C2 - 19230834

SN - 1873-3468

VL - 583

SP - 997

EP - 1000

JO - FEBS Letters

JF - FEBS Letters

ER -

Reversible oxidation of mitochondrial peroxiredoxin 3 in mouse heart subjected to ischemia and reperfusion

Abstract

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