Post-translational modification (PTM) is one of the mechanisms by which
protein function is regulated by chronic
hypoxia. This article presents an overview of recent findings on PTM of
proteins induced by chronic intermittent
hypoxia (CIH) which is experienced by humans with
sleep disordered breathing resulting in autonomic abnormalities. The analysis of PTM of
proteins involves electrophoretic separation of tissue or cellular
proteins followed by immunolabeling using
antibodies specific to native and post-translationally modified forms. Recent results demonstrate that CIH, depending on the pattern, duration and severity of
hypoxia, alters the state of phosphorylation of a subset of
proteins associated with transcriptional factor activation, signaling pathways and
neurotransmitter synthesis via activation of appropriate enzymatic machinery that catalyzes specific phosphorylation reactions. Investigation pertaining to PTMs associated with CIH is at its infant stage and future application of high throughput proteomics techniques are necessary to unravel other important PTMs associated with various critical metabolic and signaling pathways that are activated by intermittent
hypoxia.