Exercise-induced histone modifications in human skeletal muscle

McGee, Sean L., Fairlie, Erin, Garnham, Andrew P. and Hargreaves, Mark 2009, Exercise-induced histone modifications in human skeletal muscle, Journal of physiology, vol. 587, no. 24, pp. 5951-5958, doi: 10.1113/jphysiol.2009.181065.

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Title Exercise-induced histone modifications in human skeletal muscle
Author(s) McGee, Sean L.ORCID iD for McGee, Sean L. orcid.org/0000-0001-6953-106X
Fairlie, Erin
Garnham, Andrew P.
Hargreaves, Mark
Journal name Journal of physiology
Volume number 587
Issue number 24
Start page 5951
End page 5958
Total pages 8
Publisher Wiley
Place of publication Oxford, England
Publication date 2009-12-15
ISSN 0022-3751
Summary Skeletal muscle adaptations to exercise confer many of the health benefits of physical activity and occur partly through alterations in skeletal muscle gene expression. The exact mechanisms mediating altered skeletal muscle gene expression in response to exercise are unknown. However, in recent years, chromatin remodelling through epigenetic histone modifications has emerged as a key regulatory mechanism controlling gene expression in general. The purpose of this study was to examine the effect of exercise on global histone modifications that mediate chromatin remodelling and transcriptional activation in human skeletal muscle in response to exercise. In addition, we sought to examine the signalling mechanisms regulating these processes. Following 60 min of cycling, global histone 3 acetylation at lysine 9 and 14, a modification associated with transcriptional initiation, was unchanged from basal levels, but was increased at lysine 36, a site associated with transcriptional elongation. We examined the regulation of the class IIa histone deacetylases (HDACs), which are enzymes that suppress histone acetylation and have been implicated in the adaptations to exercise. While we found no evidence of proteasomal degradation of the class IIa HDACs, we found that HDAC4 and 5 were exported from the nucleus during exercise, thereby removing their transcriptional repressive function. We also observed activation of the AMP-activated protein kinase (AMPK) and the calcium–calmodulin-dependent protein kinase II (CaMKII) in response to exercise, which are two kinases that induce phosphorylation-dependent class IIa HDAC nuclear export. These data delineate a signalling pathway that might mediate skeletal muscle adaptations in response to exercise.
Language eng
DOI 10.1113/jphysiol.2009.181065
Field of Research 060114 Systems Biology
Socio Economic Objective 970106 Expanding Knowledge in the Biological Sciences
HERDC Research category C1 Refereed article in a scholarly journal
Copyright notice ©2009, Wiley
Persistent URL http://hdl.handle.net/10536/DRO/DU:30025035

Document type: Journal Article
Collection: School of Medicine
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Created: Fri, 12 Mar 2010, 11:59:42 EST by Sean McGee

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