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Differential epigenetic modifications of histones at the myosin heavy chain genes in fast and slow skeletal muscle fibers and in response to muscle unloading.
Am J Physiol Cell Physiol. 2009 Jul; 297(1):C6-16.AJ

Abstract

Recent advances in chromatin biology have enhanced our understanding of gene regulation. It is now widely appreciated that gene regulation is dependent upon post-translational modifications to the histones which package genes in the nucleus of cells. Active genes are known to be associated with acetylation of histones (H3ac) and trimethylation of lysine 4 in histone H3 (H3K4me3). Using chromatin immunoprecipitation (ChIP), we examined histone modifications at the myosin heavy chain (MHC) genes expressed in fast vs. slow fiber-type skeletal muscle, and in a model of muscle unloading, which results in a shift to fast MHC gene expression in slow muscles. Both H3ac and H3K4me3 varied directly with the transcriptional activity of the MHC genes in fast fiber-type plantaris and slow fiber-type soleus. During MHC transitions with muscle unloading, histone H3 at the type I MHC becomes de-acetylated in correspondence with down-regulation of that gene, while upregulation of the fast type IIx and IIb MHCs occurs in conjunction with enhanced H3ac in those MHCs. Enrichment of H3K4me3 is also increased at the type IIx and IIb MHCs when these genes are induced with muscle unloading. Downregulation of IIa MHC, however, was not associated with corresponding loss of H3ac or H3K4me3. These observations demonstrate the feasibility of using the ChIP assay to understand the native chromatin environment in adult skeletal muscle, and also suggest that the transcriptional state of types I, IIx and IIb MHC genes are sensitive to histone modifications both in different muscle fiber-types and in response to altered loading states.

Authors+Show Affiliations

Dept. of Physiology and Biophysics, Univ. of California, Irvine, CA 92697, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Research Support, N.I.H., Extramural

Language

eng

PubMed ID

19369448

Citation

Pandorf, Clay E., et al. "Differential Epigenetic Modifications of Histones at the Myosin Heavy Chain Genes in Fast and Slow Skeletal Muscle Fibers and in Response to Muscle Unloading." American Journal of Physiology. Cell Physiology, vol. 297, no. 1, 2009, pp. C6-16.
Pandorf CE, Haddad F, Wright C, et al. Differential epigenetic modifications of histones at the myosin heavy chain genes in fast and slow skeletal muscle fibers and in response to muscle unloading. Am J Physiol Cell Physiol. 2009;297(1):C6-16.
Pandorf, C. E., Haddad, F., Wright, C., Bodell, P. W., & Baldwin, K. M. (2009). Differential epigenetic modifications of histones at the myosin heavy chain genes in fast and slow skeletal muscle fibers and in response to muscle unloading. American Journal of Physiology. Cell Physiology, 297(1), C6-16. https://doi.org/10.1152/ajpcell.00075.2009
Pandorf CE, et al. Differential Epigenetic Modifications of Histones at the Myosin Heavy Chain Genes in Fast and Slow Skeletal Muscle Fibers and in Response to Muscle Unloading. Am J Physiol Cell Physiol. 2009;297(1):C6-16. PubMed PMID: 19369448.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Differential epigenetic modifications of histones at the myosin heavy chain genes in fast and slow skeletal muscle fibers and in response to muscle unloading. AU - Pandorf,Clay E, AU - Haddad,Fadia, AU - Wright,Carola, AU - Bodell,Paul W, AU - Baldwin,Kenneth M, Y1 - 2009/04/15/ PY - 2009/4/17/entrez PY - 2009/4/17/pubmed PY - 2009/8/18/medline SP - C6 EP - 16 JF - American journal of physiology. Cell physiology JO - Am J Physiol Cell Physiol VL - 297 IS - 1 N2 - Recent advances in chromatin biology have enhanced our understanding of gene regulation. It is now widely appreciated that gene regulation is dependent upon post-translational modifications to the histones which package genes in the nucleus of cells. Active genes are known to be associated with acetylation of histones (H3ac) and trimethylation of lysine 4 in histone H3 (H3K4me3). Using chromatin immunoprecipitation (ChIP), we examined histone modifications at the myosin heavy chain (MHC) genes expressed in fast vs. slow fiber-type skeletal muscle, and in a model of muscle unloading, which results in a shift to fast MHC gene expression in slow muscles. Both H3ac and H3K4me3 varied directly with the transcriptional activity of the MHC genes in fast fiber-type plantaris and slow fiber-type soleus. During MHC transitions with muscle unloading, histone H3 at the type I MHC becomes de-acetylated in correspondence with down-regulation of that gene, while upregulation of the fast type IIx and IIb MHCs occurs in conjunction with enhanced H3ac in those MHCs. Enrichment of H3K4me3 is also increased at the type IIx and IIb MHCs when these genes are induced with muscle unloading. Downregulation of IIa MHC, however, was not associated with corresponding loss of H3ac or H3K4me3. These observations demonstrate the feasibility of using the ChIP assay to understand the native chromatin environment in adult skeletal muscle, and also suggest that the transcriptional state of types I, IIx and IIb MHC genes are sensitive to histone modifications both in different muscle fiber-types and in response to altered loading states. SN - 1522-1563 UR - https://www.unboundmedicine.com/medline/citation/19369448/Differential_epigenetic_modifications_of_histones_at_the_myosin_heavy_chain_genes_in_fast_and_slow_skeletal_muscle_fibers_and_in_response_to_muscle_unloading_ L2 - https://journals.physiology.org/doi/10.1152/ajpcell.00075.2009?url_ver=Z39.88-2003&rfr_id=ori:rid:crossref.org&rfr_dat=cr_pub=pubmed DB - PRIME DP - Unbound Medicine ER -