Note: The nomenclature of antioxidant protein 2 is currently undergoing reconsideration. This protein is currently named antioxidant protein 2 in humans and peroxiredoxin 5 in mice. However, peroxiredoxin 5 in humans refers to a different protein (named peroxiredoxin 6 in mouse). As the same protein is supposed to have the same name in different species, we will use the old name of antioxidant protein 2 until this nomenclature issue is resolved by the human and mouse nomenclature committees.
Antioxidant protein 2 prevents methemoglobin formation in erythrocyte hemolysates
Article first published online: 7 JAN 2003
European Journal of Biochemistry
Volume 270, Issue 2, pages 334–341, January 2003
How to Cite
Stuhlmeier, K. M., Kao, J. J., Wallbrandt, P., Lindberg, M., Hammarström, B., Broell, H. and Paigen, B. (2003), Antioxidant protein 2 prevents methemoglobin formation in erythrocyte hemolysates. European Journal of Biochemistry, 270: 334–341. doi: 10.1046/j.1432-1033.2003.03393.x
- Issue published online: 7 JAN 2003
- Article first published online: 7 JAN 2003
- (Received 11 June 2002, revised 13 October 2002, accepted 26 November 2002)
- reactive oxygen species;
- antioxidant protein 2
Antioxidant protein 2 (AOP2) is a member of a family of thiol-specific antioxidants, recently renamed peroxiredoxins, that evolved as part of an elaborate system to counteract and control detrimental effects of oxygen radicals. AOP2 is found in endothelial cells, erythrocytes, monocytes, T and B cells, but not in granulocytes. AOP2 was found solely in the cytoplasm and was not associated with the nuclear or membrane fractions; neither was it detectable in plasma. Further experiments focused on the function of AOP2 in erythrocytes where it is closely associated with the hemoglobin complex, particularly with the heme. An investigation of the mechanism of this interaction demonstrated that the conserved cysteine-47 in AOP2 seems to play a role in AOP2-heme interactions. Recombinant AOP2 prevented induced as well as noninduced methemoglobin formation in erythrocyte hemolysates, indicating its antioxidant properties. We conclude that AOP2 is part of a sophisticated system developed to protect and support erythrocytes in their many physiological functions.