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Am J Physiol Lung Cell Mol Physiol 284: L917-L925, 2003. First published January 10, 2003; doi:10.1152/ajplung.00374.2002
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Vol. 284, Issue 6, L917-L925, June 2003

EDITORIAL FOCUS
Synthesis and anti-inflammatory activity of a chimeric recombinant superoxide dismutase: SOD2/3

Bifeng Gao, Sonia C. Flores, Jonathan A. Leff, Swapan K. Bose, and Joe M. McCord

Webb-Waring Institute, University of Colorado Health Sciences Center, Denver, Colorado 80262

External surfaces of cells are normally protected by extracellular superoxide dismutase, SOD3, which binds to polyanions such as heparan sulfate. We constructed a fusion gene encoding a chimeric SOD consisting of the mature human mitochondrial SOD2 plus the COOH-terminal 26-amino acid heparin-binding "tail" from SOD3. This tail is responsible for the enzyme's affinity for endothelial surfaces. The fusion gene was expressed in Escherichia coli, and the fully active enzyme SOD2/3 was purified. Although native SOD2 has no affinity for heparin, SOD2/3 binds to a heparin-agarose column. In a rat model of acute lung injury induced by intratracheal instillation of IL-1, SOD2/3, SOD2, and denatured SOD2/3 showed 92%, 13.8%, and 0% reduction of lung leak, respectively. Only SOD2/3 prevented neutrophil accumulation. In the carrageenan-induced foot edema model in the rat, SOD2/3 reduced edema by 62% (P < 0.003) at a dose in which native SOD2 produced no significant effect. Thus SOD2/3 appears to have properties as a therapeutic anti-inflammatory agent that are greatly superior to other available forms of the enzyme.

inflammation; lung injury; interleukin-1; free radicals; oxidative injury


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