Reactive Oxygen Species and Cellular Function Switch.
10.7599/hmr.2013.33.2.104
- Author:
Seong Eon RYU
1
Author Information
1. Department of Bioengineering, College of Engineering, Hanyang University, Seoul, Korea. ryuse@hanyang.ac.kr
- Publication Type:Review
- Keywords:
Reactive Oxygen Species;
OxyR;
Hsp33;
Protein Tyrosine Phosphatase;
Protein Structure
- MeSH:
Aging;
DNA;
Electrons;
Heat-Shock Proteins;
Protein Tyrosine Phosphatases;
Proteins;
Reactive Oxygen Species
- From:Hanyang Medical Reviews
2013;33(2):104-109
- CountryRepublic of Korea
- Language:Korean
-
Abstract:
Reactive oxygen species (ROS) are harmful to cellular components such as proteins, DNA and lipids. The continuous production of ROS during the respiratory electron transfer process has been regarded as the major cause of aging. However, the discoveries of proteins whose structure and function switch with cellular ROS suggest that ROS are active players in cellular regulation. OxyR is the first protein whose ROS-regulated mechanism was revealed by the atomic structure studies. The distantly-located two cysteines in OxyR form a disulfide bond by reaction with ROS, resulting in conformational and functional switches in the protein. The heat shock protein 33 is another protein that is activated by increased level of cellular ROS. Many other cellular proteins including protein tyrosine phosphatases are also regulated by ROS. This review focuses on the structure and function of the ROS-regulated proteins and their implications on the ROS's cellular roles. Detailed studies on the ROS-generating protein machinery and the ROS-regulated proteins should contribute to the therapeutic control of ROS-related diseases and aging processes.
