A common polymorphism in extracellular superoxide dismutase affects cardiopulmonary disease risk by altering protein distribution.

ABSTRACT:

Background

The enzyme extracellular superoxide dismutase (EC-SOD; SOD3) is a major antioxidant defense in lung and vasculature. A nonsynonomous single-nucleotide polymorphism in EC-SOD (rs1799895) leads to an arginine to glycine amino acid substitution at position 213 (R213G) in the heparin-binding domain. In recent human genetic association studies, this single-nucleotide polymorphism attenuates the risk of lung disease, yet paradoxically increases the risk of cardiovascular disease.

Methods and results

Capitalizing on the complete sequence homology between human and mouse in the heparin-binding domain, we created an analogous R213G single-nucleotide polymorphism knockin mouse. The R213G single-nucleotide polymorphism did not change enzyme activity, but shifted the distribu

SUBMITTER: Hartney JM 

PROVIDER: S-EPMC4270938 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature