The metabolic response to injury includes major alterations in protein metabolism; however, little is known about alterations in the synthesis of individual proteins and their role in the stress response. Our aim was to study how individual proteins in liver and muscle are altered by abdominal surgery. Changes produced in mRNA and proteins by abdominal surgery were studied in rats using RAP (random arbitrary priming)-PCR, to investigate mRNA alterations, and standard or isotopic (with in vivo radioactive labelling of proteins) two-dimensional electrophoresis/MS proteomic analyses, to study differential expression of proteins. Many of the differentially expressed proteins identified in blood were specifically synthesized by the liver to participate in the stress response. The hepatic proteins (antioxidant proteins, serine protease inhibitors, acute-phase proteins and transport proteins) were secreted into the bloodstream to produce a systemic action, indicating the central role of the liver in the stress response. Overexpressed proteins identified in liver were associated with the glycolytic processes and the folding of nascent proteins, confirming the high metabolic activity of the liver after surgery. The role of skeletal muscle protein as an amino acid donor to fuel the processes involved in the stress response was shown by the decrease in high-molecular-mass myofibrillar proteins. Combined use of the three techniques studied, differential RAP-PCR and standard and isotopic proteome analysis, provided complementary information on the differentially expressed proteins in a rat model of surgical stress.
Transcriptomic and proteomic analysis of liver and muscle alterations caused by surgical stress in rats
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Joan LÓPEZ-HELLÍN, Ricardo GONZALO, Mónica TEJEDA, Montserrat CARRASCAL, Maya R. VILÀ, Joaquín ABIÁN, Elena GARCÍA-ARUMÍ; Transcriptomic and proteomic analysis of liver and muscle alterations caused by surgical stress in rats. Clin Sci (Lond) 1 February 2005; 108 (2): 167–178. doi: https://doi.org/10.1042/CS20040144
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