Petersen, Steen V.Olsen, Dorte Aa.Kenney, John M.Oury, Tim D.Valnickova, ZuzanaThogersen, Ida B.Crapo, James D.Enghild, Jan J.2011-04-282011-05-172011-04-282011-05-172005-01-15Biochemical Journal; 385:2 p. 427-432http://hdl.handle.net/10342/3380The 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 2005en-USAuthor notified of opt-out rights by Cammie Jennings prior to upload of this article.CollagenExtracellular superoxide dismutase (EC-SOD)Oxidative damageReduced afficityR213GStructuresArticlePMC113471310.1042/BJ20041218