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Striated muscle activator of Rho signaling is required for myotube survival but does not influence basal protein synthesis or degradation

Wallace, Marita A and Russell, Aaron P 2013, Striated muscle activator of Rho signaling is required for myotube survival but does not influence basal protein synthesis or degradation, American journal of physiology: cell physiology, vol. 305, no. 4, pp. C414-C426, doi: 10.1152/ajpcell.00421.2012.

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Title Striated muscle activator of Rho signaling is required for myotube survival but does not influence basal protein synthesis or degradation
Author(s) Wallace, Marita A
Russell, Aaron PORCID iD for Russell, Aaron P orcid.org/0000-0002-7323-9501
Journal name American journal of physiology: cell physiology
Volume number 305
Issue number 4
Start page C414
End page C426
Total pages 13
Publisher American Physiological Society
Place of publication Bethesda, Md.
Publication date 2013-08-15
ISSN 0363-6143
1522-1563
Keyword(s) STARS
disuse
exercise
sarcomere
skeletal muscle
Actins
Animals
Cell Line
Cell Survival
Gene Expression Regulation
Mice
Microfilament Proteins
Muscle Fibers, Skeletal
Muscle Proteins
Myoblasts, Skeletal
Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha
Phosphorylation
Polymerization
Proto-Oncogene Proteins c-akt
RNA Interference
RNA, Messenger
Receptors, Estrogen
Ribosomal Protein S6 Kinases, 70-kDa
Serum Response Factor
Signal Transduction
Trans-Activators
Transcription Factors
Transfection
Science & Technology
Life Sciences & Biomedicine
Cell Biology
Physiology
PALMITOYLTRANSFERASE-I-BETA
HUMAN SKELETAL-MUSCLE
RESISTANCE EXERCISE
OXIDATIVE CAPACITY
GENE-EXPRESSION
C2C12 MYOTUBES
TIME-COURSE
HYPERTROPHY
APOPTOSIS
Summary Skeletal muscle mass is regulated by sensing and transmitting extracellular mechanical stress signals to intracellular signaling pathways controlling protein synthesis and degradation. Striated muscle activator of Rho signaling (STARS) is a muscle-specific actin-binding protein that is sensitive to extracellular stress signals. STARS stimulates actin polymerization and influences serum response factor (SRF) and peroxisome proliferator-activated receptor-γ coactivator (PGC)-1α transcription of genes involved in muscle growth, structure, and contraction. The role of STARS in skeletal muscle cells is not well understood. This study investigated whether STARS influenced C2C12 myotube growth by regulating protein synthesis and degradation. The influence of STARS on Pgc-1α, Srf, and Errα mRNA levels, as well as several of their downstream targets involved in muscle cell growth, contraction, and metabolism, was also investigated. STARS overexpression increased actin polymerization, with no effect on protein synthesis, protein degradation, or Akt phosphorylation. STARS overexpression increased Pgc-1α, Srf, Ckmt2, Cpt-1β, and Mhc1 mRNA. STARS knockdown reduced actin polymerization and increased cell death and dead cell protease activity. It also increased markers of inflammation (Casp1, Il-1β, and Mcp-1), regeneration (Socs3 and Myh8), and fast myosin isoforms (Mhc2a and Mhc2x). We show for the first time in muscle cells that STARS overexpression increases actin polymerization and shifts the muscle cell to a more oxidative phenotype. The suppression of STARS causes cell death and increases markers of necrosis, inflammation, and regeneration. As STARS levels are suppressed in clinical models associated with increased necrosis and inflammation, such as aging and limb immobilization, rescuing STARS maybe a future therapeutic strategy to maintain skeletal muscle function and attenuate contraction-induced muscle damage.
Language eng
DOI 10.1152/ajpcell.00421.2012
Field of Research 111601 Cell Physiology
0601 Biochemistry And Cell Biology
0606 Physiology
1116 Medical Physiology
Socio Economic Objective 920116 Skeletal System and Disorders (incl. Arthritis)
HERDC Research category C1.1 Refereed article in a scholarly journal
ERA Research output type C Journal article
Copyright notice ©2013, the American Physiological Society
Persistent URL http://hdl.handle.net/10536/DRO/DU:30072208

Document type: Journal Article
Collections: Faculty of Health
School of Exercise and Nutrition Sciences
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