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Pathophysiological functions of nitric oxide-mediated protein modifications
Harry Ischiropoulos1, Andrew Gow
1Stokes Research Institute, Children's Hospital of Philadelphia, University of Pennsylvania, Abramson Research Center, Rm. 416, 34th Street, Civic Center Building, Philadelphia, PA 19104, USA. ischirop@mail.med.upenn.edu
Toxicology
|February 5, 2005
Summary
Nitric oxide (NO) modifies proteins through reactions like metal binding and nitrosation, impacting biological systems. These modifications integrate physiological balance and may mediate disease.
Area of Science:
- Biochemistry
- Molecular Biology
- Physiology
Background:
- Nitric oxide (NO) exhibits diverse biological effects.
- Protein modifications by NO are key to its functions.
Purpose of the Study:
- To review the chemistry of nitric oxide.
- To elucidate the biological functions and significance of NO-mediated protein modifications.
Main Methods:
- Review of chemical reactions of nitric oxide with proteins.
- Analysis of nitric oxide-derived reactive nitrogen species.
- Examination of protein binding to metal centers.
- Investigation of nitrosation and nitration reactions.
Main Results:
- NO reacts with proteins via metal center binding, nitrosation, and nitration.
- These reactions are central to NO's biological reactivity.
- NO acts as an integrator of physiological homeostasis.
Conclusions:
- Post-translational modifications by NO explain its pleiotropic effects.
- NO can mediate physiological homeostasis and pathological phenotypes.