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Review
. 2005 Dec;37(12):2466-71.
doi: 10.1016/j.biocel.2005.06.012. Epub 2005 Jul 21.

Extracellular superoxide dismutase

Eva Nozik-Grayck  1 , Hagir B Suliman, Claude A Piantadosi
Affiliations
Review

Extracellular superoxide dismutase

Eva Nozik-Grayck et al. Int J Biochem Cell Biol. 2005 Dec.

Abstract

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.

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