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Mechanical stretch induces activation of eukaryotic elongation factor 2 in C2C12 myoblast
Author(s) -
Nakai Naoya,
Kawano Fuminori,
Oke Yoshihiko,
Nomura Sachiko,
Terada Masahiro,
Ohira Takashi,
Ohira Yoshinobu
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.601.8
Subject(s) - c2c12 , microbiology and biotechnology , protein kinase a , elongation , elongation factor , mapk/erk pathway , kinase , chemistry , myocyte , p38 mitogen activated protein kinases , phosphorylation , biochemistry , materials science , biology , ultimate tensile strength , rna , myogenesis , gene , metallurgy , ribosome
It has been proposed that mechanically‐induced tension was the critical event for initiating muscle hypertrophy. However, the molecular mechanisms involved in this process are still under investigation. In the present study, effect of mechanical stretch on the protein translation initiation is studied in C2C12 myoblast. C2C12 cells were plated on fibronectin‐coated silicone elastomer chamber in DMEM containing 10% fetal bovine serum. Cells were grown in CO 2 incubator and subjected to 30 min of cyclic 15% biaxial stretch at a frequency of 1Hz. 30 min of cyclic stretch increased the phosphorylation levels of p38 mitogen activated protein kinase (MAPK) and extracellular‐regulated kinase 1 and 2 (ERK1/2). Eukaryotic elongation factor 2 (eEF2), a marker for peptide chain elongation process, was also activated (dephosphorylated) by cyclic stretch. These results suggest that p38 MAPK and/or ERK1/2 pathway may be involved in stretch‐induced activation of protein translation elongation process. This study is supported by Grant‐in‐Aid for Scientific Research C (20500577 to N.N.) from the Ministry of Education, Culture, Sports, Science and Technology, Japan.