Age-related changes in histone modification in rat gastrocnemius muscle

Changes in histone acetylation and methylation status with aging affect gene expression and phenotype in several tissues; however, age-related changes in histone modification in the skeletal muscle have not been elucidated yet. This study investigated age-related global changes in histone modificati...

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Bibliographic Details
Published in:Experimental gerontology 2019-10, Vol.125, p.110658-110658, Article 110658
Main Authors: Yoshihara, Toshinori, Machida, Shuichi, Tsuzuki, Takamasa, Kakigi, Ryo, Chang, Shuo-wen, Sugiura, Takao, Naito, Hisashi
Format: Article
Language:English
Subjects:
Histone acetylation
Histone tri-methylation
Histone-modifying enzyme
Sarcopenia
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Summary:Changes in histone acetylation and methylation status with aging affect gene expression and phenotype in several tissues; however, age-related changes in histone modification in the skeletal muscle have not been elucidated yet. This study investigated age-related global changes in histone modification in rat gastrocnemius muscle. Male Wistar rats (n = 28) were assigned to one of four age groups (n = 7 per group) corresponding to different life stages: 3 months old (3-mo; young), 6 months old (adult), 12 months old (12-mo; middle-aged), and 24 months old (24-mo; old). The gastrocnemius muscle was removed and global histone modification (acetylation and tri-methylation) at K9 and K27 was evaluated by western blotting. Relative muscle mass decreased in the 12- and 24-mo rats accompanied with reduction in type IIb myosin heavy chain isoforms and Myh4 (MHC IIB) mRNA expression. Histone H3 acetylation decreased in an age-dependent manner, with lower levels in 12- and 24-mo groups than in the 3-mo group. K9 and K27 acetylation decreased with age. Although there was no significant change in K27 tri-methylation, K9 tri-methylation showed an age-dependent decline. Histone modification status (acetylation at K9 and K27 and tri-methylation at K9) was positively associated with relative gastrocnemius muscle weight, the percentage of type IIb myosin heavy chain isoform, myosin heavy chain type IIb protein expression, and the level of Myh4 mRNA. Thus, global histone H3 methylation and acetylation decrease with age, and the latter might be associated with age-related muscle atrophy of rat gastrocnemius muscle. •Global histone H3 methylation and acetylation decrease with age.•SIRT1 accumulation in nuclei presumably could induce H3K9 and H3K27 deacetylation.•Changes may be linked to age-related type IIb fiber atrophy in rat skeletal muscle.
ISSN:0531-5565
1873-6815
DOI:10.1016/j.exger.2019.110658