Extracellular superoxide dismutase.
The extracellular space is protected from oxidant stress by the antioxidant enzyme extracellular superoxide dismutase (EC-SOD), which is highly expressed in selected tissues including blood vessels, heart, lungs, kidney and placenta. EC-SOD contains a unique heparin-binding domain at its carboxy-terminus that establishes localization to the extracellular matrix where the enzyme scavenges superoxide anion. The EC-SOD heparin-binding domain can be removed by proteolytic cleavage, releasing active enzyme into the extracellular fluid. In addition to protecting against extracellular oxidative damage, EC-SOD, by scavenging superoxide, preserves nitric oxide bioactivity and facilitates hypoxia-induced gene expression. Loss of EC-SOD activity contributes to the pathogenesis of a number of diseases involving tissues with high levels of constitutive extracellular superoxide dismutase expression. A thorough understanding of the biological role of EC-SOD will be invaluable for developing novel therapies to prevent stress by extracellular oxidants.
Nozik-Grayck
Eva
E
Pediatric Critical Care, Department of Pediatrics, University of Colorado School of Medicine, 4200 E 9th Ave B131, Denver, CO 80262, USA. Eva.Grayck@uchsc.edu
Suliman
Hagir B
HB
Piantadosi
Claude A
CA
D000818:Animals; D005110:Extracellular Space / Q000201:enzymology*; D015971:Gene Expression Regulation, Enzymologic; D006801:Humans; D020836:Protein Structure, Quaternary; D013482:Superoxide Dismutase / Q000096:biosynthesis / Q000502:physiology*; D014158:Transcription, Genetic
D013482:Superoxide Dismutase