Purification and characterization of extracellular superoxide dismutase in mouse lung

Biochem Biophys Res Commun. 2000 Aug 28;275(2):542-8. doi: 10.1006/bbrc.2000.3327.

Abstract

Extracellular superoxide dismutase (EC-SOD) is the major isozyme of SOD in arteries, but is also abundant in lungs. In particular, mouse lungs contain large amounts of EC-SOD compared to lungs in other mammals. This suggests that EC-SOD may have an amplified function in the mouse lung. This study describes the purification and characterization of mouse EC-SOD as well as its localization in mouse lung. Mouse EC-SOD exists primarily as a homotetramer composed of a pair of dimers linked through disulfide bonds present in the heparin-binding domains of each subunit. In addition, mouse EC-SOD can exist in active multimeric forms. We developed and utilized a polyclonal antibody to mouse EC-SOD to immunolocalize EC-SOD in mouse lung. EC-SOD labeling is strongest in the matrix of vessels, airways, and alveolar septa. This localization suggests that EC-SOD may have important functions in pulmonary biology, perhaps in the modulation of nitric oxide-dependent responses.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Chromatography, Gel
  • Electrophoresis, Polyacrylamide Gel
  • Immunohistochemistry
  • Lung / enzymology*
  • Mice
  • Molecular Sequence Data
  • Superoxide Dismutase / chemistry
  • Superoxide Dismutase / isolation & purification*
  • Superoxide Dismutase / metabolism

Substances

  • Superoxide Dismutase