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Papers In Press, published online ahead of print November 27, 2001
Biochemistry & Molecular Biology, University of Louisville, Louisville, Ky 40223
Corresponding Author: eugenia.wang{at}louisville.edu
Peptide elongation factor eEF1A-2/S1, which shares 92% homology with its sister gene eEF1A-1/EF-1a, is exclusively expressed in brain, heart and skeletal muscle. In these tissues, eEF1A-2/S1 is the only type 1A elongation factor expressed in adulthood, since a transition from eEF1A-1/EF-1a to eEF1A-2/S1 occurs in early postnatal development. In this article, we report that the expression of eEF1A-2/S1 protein is activated upon myogenic differentiation. Furthermore, we show that upon serum deprivation-induced apoptosis, eEF1A-2/S1 protein disappears and is replaced by its homologue eEF1A-1/EF-1a in dying myotubes; cell death is characterized by the activation of caspase-3. In addition, we show that the continuous expression of eEF1A-2/S1 due to adenoviral gene transfer protects differentiated myotubes from apoptosis by delaying their death, thus suggesting a pro-survival function for eEF1A-2/S1 in skeletal muscle. In contrast, myotube death is accelerated by the introduction of the homologous gene, eEF1A-1/EF-1a, while cells transfected with antisense eEF1A-1/EF-1a are protected from apoptosis. These results demonstrate that the two sister genes, eEF1A-1/EF-1a and eEF1A-2/S1, regulate myotube survival with the former exerting pro-death activity and the latter a pro-survival effect.
J. Biol. Chem, 10.1074/jbc.M110685200
Submitted on November 7, 2001
Revised on November 21, 2001
Accepted on November 27, 2001
Peptide elongation factor eEF1A-2/S1 expression in cultured differentiated myotubes, and its protective effect against caspase-3-mediated apoptosis
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