Inhibition of the Thiol-Specific Antioxidant Activity of Rat Liver MSP23 Protein by Hemin

Mouse stress-inducible 23-kDa protein (MSP23) belongs to a new type of antioxidative protein family and is highly expressed in livers. To examine its physiological role in the tissue, we have purified native MSP23 protein from the cytosolic fraction of rat liver. The purified protein showed the thio...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 1995-11, Vol.216 (3), p.970-975
Main Authors: Ishii, T., Kawane, T., Taketani, S., Bannai, S.
Format: Article
Language:English
Subjects:
Ammonium Sulfate
Animals
Antioxidants
Chemical Phenomena
Chemical Precipitation
Chemistry, Physical
Cytosol - chemistry
Dithiothreitol - pharmacology
Glutamate-Ammonia Ligase - antagonists & inhibitors
Heat-Shock Proteins - antagonists & inhibitors
Hemin - pharmacology
Liver - chemistry
Mercaptoethanol - pharmacology
Oxidation-Reduction
Peroxidases
Peroxiredoxins
Rats
Rats, Sprague-Dawley
Sulfhydryl Compounds - metabolism
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Summary:Mouse stress-inducible 23-kDa protein (MSP23) belongs to a new type of antioxidative protein family and is highly expressed in livers. To examine its physiological role in the tissue, we have purified native MSP23 protein from the cytosolic fraction of rat liver. The purified protein showed the thiol-specific antioxidant activity and protected glutamine synthetase from inactivation by a mixed metal-thiol oxidation. We examined the effect of hemin on that activity since it was recently shown by others that the rat liver MSP23 protein had a high binding affinity to heme. We have found that hemin at low concentrations inhibits the antioxidative activity of MSP23. This result suggests that one type of oxidant damage caused by hemin to cells is due to inactivation of the antioxidative protein, MSP23.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1995.2715