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Activation of ERK by sodium tungstate induces protein synthesis and prevents protein degradation in rat L6 myotubes
Author(s) -
Salto Rafael,
Vílchez José D.,
Cabrera Elena,
Guinovart Joan J.,
Girón María D.
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.05.004
Subject(s) - protein kinase b , mapk/erk pathway , phosphorylation , pi3k/akt/mtor pathway , myogenesis , chemistry , sodium tungstate , protein degradation , skeletal muscle , tungstate , microbiology and biotechnology , protein kinase a , medicine , endocrinology , biochemistry , signal transduction , biology , organic chemistry , tungsten
The balance between the rates of protein synthesis and degradation in muscle is regulated by PI3K/Akt signaling. Here we addressed the effect of ERK activation by sodium tungstate on protein turnover in rat L6 myotubes. Phosphorylation of ERK by this compound increased protein synthesis by activating MTOR and prevented dexamethasone‐induced protein degradation by blocking FoxO3a activity, but it did not alter Akt phosphorylation. Thus, activation of ERK by tungstate improves protein turnover in dexamethasone‐treated cells. On the basis of our results, we propose that tungstate be considered an alternative to IGF‐I and its analogs in the prevention of skeletal muscle atrophy.