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Related Experiment Videos

Nitric oxide mediates iron release from ferritin.

D W Reif1, R D Simmons

  • 1Biology Department, Fisons Pharmaceuticals, Rochester, New York 14603.

Archives of Biochemistry and Biophysics
|December 1, 1990
PubMed
Summary

Nitric oxide (NO) can release iron from ferritin, a storage protein. This iron release may disrupt cellular iron balance and increase harmful reactive oxygen species, impacting tumor cells.

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Area of Science:

  • Biochemistry
  • Cellular Biology
  • Immunology

Background:

  • Activated macrophages synthesize nitric oxide (NO), potentially affecting tumor cells by depleting iron and inhibiting cellular functions.
  • The precise mechanism by which NO impacts iron metabolism and cellular respiration remains under investigation.

Purpose of the Study:

  • To investigate the role of nitric oxide (NO) in mobilizing iron from ferritin.
  • To determine if NO-induced iron release contributes to cellular damage via lipid peroxidation.

Main Methods:

  • Utilized sodium nitroprusside as an NO-generating agent.
  • Incubated NO donor with ferritin and measured iron release.
  • Assessed the role of hemoglobin and superoxide anion in modulating NO-dependent iron release.
  • Monitored lipid peroxidation as an indicator of oxidative damage.

Main Results:

  • Sodium nitroprusside induced the release of iron from ferritin.
  • Released iron catalyzed lipid peroxidation, indicating oxidative stress.
  • Hemoglobin and superoxide anion inhibited NO-mediated iron release from ferritin.
  • These findings provide evidence that NO mobilizes iron from ferritin.

Conclusions:

  • Nitric oxide (NO) can directly mobilize iron from the ferritin storage protein.
  • This mobilization disrupts intracellular iron homeostasis and promotes oxidative damage.
  • NO-induced iron release may contribute to the cytotoxic effects of activated macrophages on tumor cells.

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