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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2011.1
- 수록면
- 40 - 45 (6page)
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Extracellular superoxide dismutase (EC-SOD) is an antioxidant enzyme that protects cells and tissues from extracellular damage by eliminating superoxide anion radicals produced during metabolism. Two different forms of EC-SOD exist, and their different enzyme activities are a result of different disulfide bond patterns. Although only two folding variants have been discovered so far, five folding variants are theoretically possible.
Therefore, we constructed five different mutant EC-SOD expression vectors by substituting cysteine residues with serine residues and evaluated their expression levels and enzyme activities.
The mutant EC-SODs were expressed at lower levels than that of wild-type EC-SOD, and all of the mutants exhibited inhibited extracellular secretion, except for C195S ECSOD.
Finally, we demonstrated that co-expression of wild-type EC-SOD and any one of the mutant EC-SODs resulted in reduced secretion of wild-type EC-SOD. We speculate that mutant EC-SOD causes malfunctions in systems such as antioxidant systems and sensitizes tissues to ROS-mediated diseases.
[BMB reports 2011; 44(1): 40-45]
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참고문헌 (23)
참고문헌 신청
Antonyuk, S. V / 2009 / The structure of human extracellular Copper-Zinc superoxide dismutase at 1.7 A Resolution: Insights into Heparin and Collagen Binding / J. Mol. Biol
Carlsson, L. M / 1996 / The rat extracellular superoxide dismutase dimer is converted to a tetramer by the exchange of a single amino acid / Proc. Natl. Acad. Sci. U.S.A 93
Chen, V. M / 2006 / Evidence for activation of tissue factor by an allosteric disulfide bond / Biochemistry 45 : 12020 ~ 12028
Ellgaard, L / 2005 / The human protein disulphide isomerase family: substrate interactions and functional properties / EMBO Rep 6 : 28 ~ 32
Enghild, J. J / 1999 / The heparin-binding domain of extracellular superoxide dismutase is proteolytically processed intracellularly during biosynthesis / J. Biol. Chem 274
Carlsson, L. M / 1996 / The rat extracellular superoxide dismutase dimer is converted to a tetramer by the exchange of a single amino acid / Proc. Natl. Acad. Sci. U.S.A 93
Chen, V. M / 2006 / Evidence for activation of tissue factor by an allosteric disulfide bond / Biochemistry 45 : 12020 ~ 12028
Ellgaard, L / 2005 / The human protein disulphide isomerase family: substrate interactions and functional properties / EMBO Rep 6 : 28 ~ 32
Enghild, J. J / 1999 / The heparin-binding domain of extracellular superoxide dismutase is proteolytically processed intracellularly during biosynthesis / J. Biol. Chem 274
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