Covalent modification of sulfur-containing amino acids in proteins by reactive oxygen species (ROS) has been attracting attention
as a major post-translational modification regulating intracellular signal transduction pathways. Angiotensin II (Ang II), a major
physiologically active substrate in renin-angiotensin (RAS) system, plays a central role in the pathophysiology of cardiovascular systems.
Many evidences show that Ang II activates several signaling pathways via an oxidative modification of proteins by Ang II-induced ROS.
Ang II induced ROS production is predominantly regulated by three enzymes: NADPH oxidase, mitochondrial respiratory complex, and
nitric oxide synthase (NOS), and each enzyme-generating ROS are found to activate appropriate signaling pathways via selective oxidation
of specific proteins. These reactions are negatively regulated by ROS-scavenging enzymes or disulfide bridge reducing enzymes, and
functional disorders of these enzymes are found to cause cardiovascular dysfunctions. Thus, the spatial and temporal regulation of oxidative
modification of signaling proteins by ROS is essential to maintain cardiovascular homeostasis by Ang II. This review brings in the
new aspect in understanding ROS-mediated regulation of cardiovascular homeostasis by Ang II, and provides the possible mechanisms
underlying metamorphosis of cardiovascular homeostasis by ROS.
Keywords: Reactive oxygen species, nitric oxide, cysteine modification, receptor, senescence.
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