Abstract
Thioredoxin 1 (Trx1) is a key redox control system within the nucleus, yet little is known about the sensitivity of nuclear Trx1 to oxidative stress. The present study compared oxidant-induced changes in the redox states of nuclear Trx1, cytoplasmic Trx1, and cellular glutathione (GSH). Nuclear Trx1 was more reducing than cytoplasmic Trx1 and cellular GSH in proliferating cells. tert-Butylhydroperoxide caused an increase in the total amount of nuclear Trx1, but this was accompanied by a 60 mV oxidation. Thus, the increase in nuclear Trx1 levels did not correspond to an increase in the overall reducing capacity of Trx1 in the nucleus.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Active Transport, Cell Nucleus
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Cell Line
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Cell Nucleus / chemistry
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Cell Nucleus / metabolism
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Cytosol / chemistry
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Glutathione / chemistry
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Glutathione Disulfide / chemistry
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Humans
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Kinetics
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Membrane Proteins / chemistry*
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Membrane Proteins / metabolism
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Nuclear Proteins / chemistry*
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Nuclear Proteins / metabolism
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Oxidation-Reduction
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Oxidative Stress*
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Thioredoxins / chemistry*
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Thioredoxins / metabolism
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tert-Butylhydroperoxide / pharmacology
Substances
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Membrane Proteins
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Nuclear Proteins
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TXN protein, human
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Thioredoxins
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tert-Butylhydroperoxide
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Glutathione
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Glutathione Disulfide