Abstract

Protein arginine methyltransferase 1 (PRMT1), PRMT4, and PRMT5 catalyze the methylation of arginine residues on target proteins. Previous work suggests that these enzymes regulate skeletal muscle plasticity. However, the function of PRMTs during disuse-induced muscle remodeling is unknown. The purpose of our study was to determine whether denervation-induced muscle disuse alters PRMT expression and activity in skeletal muscle, as well as to …

Authors

Stouth DW; Manta A; Ljubicic V

Journal

American Journal of Physiology - Cell Physiology, Vol. 314, No. 2, pp. c177–c190

Publisher

American Physiological Society

Publication Date

February 1, 2018

DOI

10.1152/ajpcell.00174.2017

ISSN

0363-6143

Associated Experts

Vladimir Ljubicic

Professor, Faculty of Science

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Fields of Research (FoR)

3101 Biochemistry and cell biology 3208 Medical physiology 32 Biomedical and Clinical Sciences 31 Biological Sciences

Medical Subject Headings (MeSH)

AMP-Activated Protein Kinases Animals Cell Plasticity Disease Models, Animal Male Mice, Inbred C57BL Muscle Denervation Muscle, Skeletal Muscular Atrophy Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha Phenotype Protein Binding Protein-Arginine N-Methyltransferases Signal Transduction Time Factors

Protein arginine methyltransferase expression, localization, and activity during disuse-induced skeletal muscle plasticity