Journal
PROTEOMICS
Volume 9, Issue 1, Pages 106-115Publisher
WILEY
DOI: 10.1002/pmic.200800268
Keywords
2-D gel electrophoresis; Animal model; Exercise; Heart; HSP20 heat shock proteins
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Endurance training improves cardiac function and protects against heart disease. The rodent intensity-controlled running model replicates endurance exercise in humans and can be used to investigate molecular adaptations in the heart. Rats (n = 6, 280 +/- 3 g) performed exercise tests to measure their peak oxygen uptake ((V) over dotO(2)peak) and training was prescribed at 70-75% (V) over dotO(2)peak for 30 min, 4 days/wk. Hearts were isolated 4 h after a final (V) over dotO(2)peak test and left ventricle proteomes compared to weight-matched control animals (n = 6, 330 +/- 2 g) using differential analysis of 2-D gels. Proteins were identified by searching MS and MS/MS spectra against Swiss-Prot using MASCOT (www.matrixscience.com). Average (V) over dotO(2)peak increased 23% (p = 0.008) over the 6-week regimen and 23 gel spots differed (p<0.05) between exercised and control hearts. Expression of myofibrillar proteins (e.g. alpha-myosin heavy chain and cardiac alpha-actin) and proteins associated with fatty acid metabolism (e.g. heart fatty acid binding protein, acetyl coenzyme A dehydrogenase and mitochondrial thioesterase-1) increased. in addition, this work discovered a novel increase in phosphorylation of heat shock protein 20 at serine 16. Previously this modification has been associated with improved cardiomyocyte contractility and protection against apoptosis.
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