Published ahead of print on October 7, 2004, doi:10.1165/rcmb.2004-0021OC Am. J. Respir. Cell Mol. Biol., Volume 32, Number 1, January 2005, 9-17 A more recent version of this article appeared on January 1, 2005
Submitted on January 23, 2004 Protein carbonyl formation in the diaphragmEsther Barreiro1,1 Muscle and Respiratory System Research Unit, Universitat Pompeu Fabra, Barcelona, Catalonia, Spain, 2 Muscle and Respiratory System Research Unit, Universitat Pompeu Fabra, Barcelona, Catalonia, Spain; Respiratory Medicine Department, Hospital Del Mar, Barcelona, Catalonia, Spain, 3 Genome Quebec Innovation Centre, McGill University, Montreal, Quebec, Canada, 4 Critical Care and Respiratory Divisions, McGill University, Montreal, Quebec, Canada * To whom correspondence should be addressed. E-mail: sabah.hussain{at}muhc.mcgill.ca.
Although protein carbonyl formation is an index of oxidative stress in skeletal muscles, the exact proteins, which undergo oxidation in these muscles, remain unknown. We used 2D electrophoresis, immunoblotting and mass spectrometry to identify carbonylated proteins in the diaphragm in septic animals. Rats were injected with saline (control) or E. coli lipopolysaccharides (LPS) and sacrificed after various intervals. Diaphragm protein carbonylation increased significantly and peaked 12hrs after LPS injection and it was localized both inside muscle fibers and in blood vessels supplying muscle fibers. Aldolase A, glyceraldehyde 3-phosphate dehydrogenase, enolase 3
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, mitochondrial and cytosolic creatine kinases, 
-actin, carbonic anyhdrase III and ubiquinol-cytochrome c reductase were all carbonylated in septic rat diaphragms. In addition, we found significant negative correlations between the intensity of carbonylation and creatine kinase and aldolase activities. We conclude that glycolysis, ATP production, CO2 hydration and contractile proteins are targeted by oxygen radicals inside the diaphragm during sepsis.
