1 Section of Systems Biology Research, Department of Biomedical Sciences, Faculty of Health and Medical Sciences, Københavns Universitet2 Section of Social Medicine, Department of Public Health, Faculty of Health and Medical Sciences, Københavns Universitet3 unknown4 Section of Systems Biology Research, Department of Biomedical Sciences, Faculty of Health and Medical Sciences, Københavns Universitet5 Section of Social Medicine, Department of Public Health, Faculty of Health and Medical Sciences, Københavns Universitet
AIM: Exercise-induced adaptations of skeletal muscle are related to training mode and can be muscle fibre type specific. This study aimed to investigate heat shock protein expression in type I and type II muscle fibres in resting skeletal muscle of subjects with different training backgrounds. METHODS: Three groups of subjects were included: healthy active not engaged in any training programme (ACT, n = 12), resistance trained (RES, n = 6) and endurance trained (END, n = 8). Biopsies were obtained from vastus lateralis and immunohistochemistry was performed using monoclonal antibodies against myosin heavy chain I and IIA, αB-crystallin, HSP27, HSP60 and HSP70. RESULTS: In ACT and RES, but not in END, a fibre type specific expression with higher staining intensity in type I than type II fibres was seen for αB-crystallin. The opposite (II>I) was found for HSP27 in subjects from ACT (6 of 12 subjects) and RES (3 of 6), whereas all subjects from END displayed uniform staining. HSP60 showed no fibre specific expression. HSP70 displayed a fibre specific expression pattern (I>II) in ACT (4 of 12), but not in END or RES. CONCLUSION: This study shows that the level of expression of the different HSPs in human skeletal muscle is influenced by muscle fibre phenotype. The fibre type specific expression of HSP70 is influenced by resistance and endurance training whereas those of αB-crystallin and HSP27 are influenced only by endurance training suggesting the existence of a training-modality specific action on the adaptive processes including heat shock proteins in human skeletal muscle. This article is protected by copyright. All rights reserved.