Extracellular superoxide dismutase.

Published

Journal Article (Review)

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.

Full Text

Duke Authors

Cited Authors

  • Nozik-Grayck, E; Suliman, HB; Piantadosi, CA

Published Date

  • December 2005

Published In

Volume / Issue

  • 37 / 12

Start / End Page

  • 2466 - 2471

PubMed ID

  • 16087389

Pubmed Central ID

  • 16087389

International Standard Serial Number (ISSN)

  • 1357-2725

Digital Object Identifier (DOI)

  • 10.1016/j.biocel.2005.06.012

Language

  • eng

Conference Location

  • Netherlands