The high concentration of Arg213 → Gly extracellular superoxide dismutase (EC-SOD) in plasma is caused by a reduction of both heparin and collagen affinities

ECU Author/Contributor (non-ECU co-authors, if there are any, appear on document)

James D. Crapo (Creator)

Jan J. Enghild (Creator)

John M. Kenney (Creator)

Dorte Aa. Olsen (Creator)

Tim D. Oury (Creator)

Steen V. Petersen (Creator)

Ida B. Thogersen (Creator)

Zuzana Valnickova (Creator)

Institution

East Carolina University (ECU )

Web Site: http://www.ecu.edu/lib/

Abstract: The C-terminal region of EC-SOD (extracellular superoxide dismutase) mediates the binding to both heparin/heparan sulphate and type I collagen. A mutation (Arg213→Gly; R213G) within this extracellular matrix-binding region has recently been implicated in the development of heart disease. This relatively common mutation affects the heparin affinity and the concentration of EC-SOD in the plasma of R213G homozygous individuals is increased 10- to 30-fold. In the present study we confirm using R213G EC-SOD purified from a homozygous individual that the heparin affinity is reduced. Significantly the collagen affinity of the R213G EC-SOD variant was similarly affected and both the heparin and collagen affinitieswere reduced by 12-fold. Structural analysis of synthetic extracellularmatrix-binding regions suggests that the mutation alters the secondary structure.We conclude that the increased concentration of EC-SOD in the plasma of R213G carriers is caused by a reduction in both heparin and collagen affinities. Originally published Biochemical Journal Vol. 385 No. 2 Jan 2005

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Publication

Other

Biochemical Journal. 385:2(January 2005) p. 427-432.

Language: English

Date: 2011

Keywords

collagen, extracellular superoxide dismutase (EC-SOD), oxidative damage, reduced afficity, R213G, structure

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