Author | Petersen, Steen V. | en_US |
Author | Olsen, Dorte Aa. | en_US |
Author | Kenney, John M. | en_US |
Author | Oury, Tim D. | en_US |
Author | Valnickova, Zuzana | en_US |
Author | Thogersen, Ida B. | en_US |
Author | Crapo, James D. | en_US |
Author | Enghild, Jan J. | en_US |
Date Accessioned | 2011-04-28T14:44:00Z | en_US |
Date Accessioned | 2011-05-17T15:07:42Z | |
Date Available | 2011-04-28T14:44:00Z | en_US |
Date Available | 2011-05-17T15:07:42Z | |
Date of Issue | 2005-01-15 | en_US |
Identifier (Citation) | Biochemical Journal; 385:2 p. 427-432 | en_US |
Identifier (URI) | http://hdl.handle.net/10342/3380 | en_US |
Description | 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 | en_US |
Language | en_US | en_US |
Publisher | East Carolina University | en_US |
Related URI | http://www.biochemj.org/bj/default.htm | en_US |
Rights | Author notified of opt-out rights by Cammie Jennings prior to upload of this article. | en_US |
Subject | Collagen | en_US |
Subject | Extracellular superoxide dismutase (EC-SOD) | en_US |
Subject | Oxidative damage | en_US |
Subject | Reduced afficity | en_US |
Subject | R213G | en_US |
Subject | Structures | en_US |
Title | The high concentration of Arg213 → Gly extracellular superoxide dismutase (EC-SOD) in plasma is caused by a reduction of both heparin and collagen affinities | en_US |
Type | Article | en_US |
Identifier (PMID) | PMC1134713 | en_US |
Identifier (DOI) | 10.1042/BJ20041218 | |
Journal Name | Biochemical Journal | |
Journal Volume | 385 | |
Journal Issue | 2 | |
Article Pages | 427-432 | |