Proteomic analysis of global changes induced by deep hypothermia in both protein synthesis and phosphorylation.

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Hypothermia is utilized with increasing frequency to protect organs such as the brain against ischemic injury. Though a principal mechanism of hypothermic protection would be suppression of metabolism, its pleiotropic effects are as yet incompletely understood. To analyze hypothermia-induced proteomic changes, we employed fluorescence-based two-dimensional(2-D) difference gel electrophoresis(DIGE) and matrix-assisted laser desorption/ionization-time-of-flight(MALDI-TOF/TOF) tandem mass spectrometry. Deep hypothermia produced significant down-regulation of the proteins that regulates ATP synthesis or muscle contraction in rat heart muscle. Hypothermia also produced significant down-regulation of the following cellular components and biological processes or pathways in rat livers : endoplasmic reticulum(ER), mitochondria, ATP binding, amino acid metabolism, urea cycle, response to oxidative stress, anti-apoptosis, negative regulation of apoptosis. These changes were similar to those in hibernating animals except for both ER and apoptosis-related pathways, which are conversely up-regulated in hibernating mammals. This discrepancy needs to be investigated further in future research.