Title:Protein Tyrosine Nitration: Role in Aging
Volume: 10
Issue: 4
Author(s): Bulbul Chakravarti and Deb N. Chakravarti*
Affiliation:
- Department of Chemistry, York College, The City University of New York, 94-20 Guy R. Brewer Boulevard, Jamaica, New York,United States
Keywords:
Protein modification, tyrosine nitration, aging, oxidative stress, aerobic metabolism, nitrosative stress.
Abstract: Background: Aging is the inevitable fate of all living organisms, but the molecular basis
of physiological aging is poorly understood. Oxidative stress is believed to play a key role in the
aging process. In addition to Reactive Oxygen Species (ROS), Reactive Nitrogen Species (RNS)
are generated during aerobic metabolism in living organisms. Although protein damage and functional
modification by ROS have been demonstrated in details, fewer studies have been reported on
protein damage by RNS and its implication in the aging process. Proteins undergoing tyrosine nitration
are associated with pathophysiology of several diseases, as well as physiological aging. The
purpose of the current review article is to provide a brief summary of the biochemical mechanisms
of tyrosine nitration, methodologies used for the detection of these modified proteins, effect of RNS
induced post translational modification on biological functions and the putative role of tyrosine nitrated
proteins in the aging process.
Methods: Published studies on the role of RNS in age related functional alteration of various organs/
tissues were critically reviewed and evaluated.
Results: Covalent modification of various proteins by tyrosine nitration is associated with modification
of biological functions of various organs/tissues such as skeletal muscle, heart, brain and liver
due to aging.
Conclusion: This information will be helpful to further investigate the interplay of different biochemical
pathways and networks involved in the tyrosine nitration of various proteins due to aging
with the ultimate goal to prevent the detrimental effects of RNS on the functional activities of these
proteins.
