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Adaptation of the rat cardiac proteome in response to intensity‐controlled endurance exercise
Author(s) -
Burniston Jatin G.
Publication year - 2008
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200800268
Subject(s) - endurance training , heat shock protein , vo2 max , proteome , hsp70 , cardiac function curve , myosin , lactate dehydrogenase , chemistry , medicine , endocrinology , biology , biochemistry , heart rate , heart failure , gene , enzyme , blood pressure
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 ( $\ { \dot V} { O}_{ 2} { peak}$ ) and training was prescribed at 70–75% $\ { \dot V} { O}_{ 2} { peak}$ for 30 min, 4 days/wk. Hearts were isolated 4 h after a final $\ { \dot V} { O}_{ 2} { peak}$ 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 $\ { \dot V} { O}_{ 2} { peak}$ 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 . α‐myosin heavy chain and cardiac α‐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.