Published ahead of print on October 7, 2004, doi:10.1165/rcmb.2004-0021OC
© 2005 American Thoracic Society DOI: 10.1165/rcmb.2004-0021OC Protein Carbonyl Formation in the DiaphragmCritical Care and Respiratory Divisions, Royal Victoria Hospital, McGill University Health Centre, and Meakins-Christie Laboratories, McGill University; McGill University and Genome Quebec Innovation Centre, Montreal, Quebec, Canada; Muscle and Respiratory System Research Unit, IMIM, CEXS, Universitat Pompeu Fabra; and Respiratory Medicine Department, Hospital del Mar, Barcelona, Catalonia, Spain Correspondence and requests for reprints should be addressed to Dr. S. Hussain, Room L3.05, 687 Pine Ave. West, Montreal, PQ, H3A 1A1 Canada. 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 Escherichia coli lipopolysaccharides (LPS) and killed after various intervals. Diaphragm protein carbonylation increased significantly and peaked 12 h 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 3ß, mitochondrial and cytosolic creatine kinases,
Key Words: carbonyl formation • muscle contraction • nitric oxide • protein oxidation • sepsis This article has been cited by other articles:
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-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. 
