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Nitric oxide and its decomposed derivatives decrease the binding of extracellular-superoxide dismutase to the

M Yamamoto1, H Hara, T Adachi

  • 1Laboratory of Clinical Pharmaceutics, Gifu Pharmaceutical University, 5-6-1 Mitahora-higashi, Gifu 502-8585, Japan.

FEBS Letters
|September 22, 2001
PubMed
Summary
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Excess nitric oxide (NO) reduces extracellular-superoxide dismutase (EC-SOD) binding to endothelial cells. This impairs the cell

Area of Science:

  • Biochemistry
  • Cell Biology
  • Physiology

Background:

  • Extracellular-superoxide dismutase (EC-SOD) is crucial for protecting vascular endothelial cells from oxidative stress.
  • EC-SOD binds to the endothelial cell surface via heparan sulfate proteoglycans.

Purpose of the Study:

  • To investigate the effect of nitric oxide (NO) on the binding of EC-SOD to endothelial cells.
  • To understand how inflammatory conditions might affect EC-SOD's protective function.

Main Methods:

  • Incubation of endothelial cells (HUVEC, bovine aortic) with NO donors (SNAP, NOR4) and lipopolysaccharide-stimulated cells.
  • Assessing EC-SOD binding to cell surfaces and immobilized heparin.
  • Utilizing a nitric oxide synthase inhibitor (N(G)-nitro-L-arginine).

Related Experiment Videos

Main Results:

  • Potent NO donors significantly decreased EC-SOD binding to endothelial cell proteoglycans.
  • NO from stimulated cells also reduced EC-SOD binding, an effect blocked by a nitric oxide synthase inhibitor.
  • NO donors and their decomposition products reduced EC-SOD binding to heparin.

Conclusions:

  • Excessive NO, as seen in inflammation, diminishes EC-SOD's attachment to the vascular endothelial cell surface.
  • This reduction in binding compromises the endothelial cells' defense against oxidative stress.