Ruest et al, Feb 2002, Peptide elongation factor eEF1A-2/S1 expression in cultured differentiated myotubes and its protective effect against caspase-3-mediated apoptosis
Reference
Ruest, L. B.,
Marcotte, R.,
&
Wang, E.
Peptide elongation factor eEF1A-2/S1 expression in cultured differentiated myotubes and its protective effect against caspase-3-mediated apoptosis. J.Biol.Chem., 277(7): 5418-5425. (2002).
Abstract
Peptide elongation factor eEF1A-2/S1, which shares 92% homology with eEF1A-1/EF-1alpha, 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 because a transition from eEF1A-1/EF-1alpha 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 homolog eEF1A-1/EF-1alpha 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 resulting from adenoviral gene transfer protects differentiated myotubes from apoptosis by delaying their death, thus suggesting a prosurvival function for eEF1A-2/S1 in skeletal muscle. In contrast, myotube death is accelerated by the introduction of the homologous gene, eEF1A-1/EF-1alpha, whereas cells transfected with antisense eEF1A-1/EF-1alpha are protected from apoptosis. These results demonstrate that the two sister genes, eEF1A-1/EF-1alpha and eEF1A-2/S1, regulate myotube survival with the former exerting prodeath activity and the latter a prosurvival effectKeywords
- 06
- ACTIVATION
- activity
- Adenoviridae
- aging
- Animal
- Apoptosis
- beta-Galactosidase
- biosynthesis
- Blotting,Western
- brain
- Canada
- Caspases
- cell
- cell death
- Cell Differentiation
- Cell Survival
- CELL-DEATH
- CELLS
- Cells,Cultured
- chain
- chemistry
- cytology
- development
- differentiation
- DNA
- DNA Fragmentation
- effect
- EXPRESSION
- function
- GENE
- genetics
- heart
- In Situ Nick-End Labeling
- introduction
- jewish
- LA
- ME
- medical
- metabolism
- mice
- MUSCLE
- Muscle,Skeletal
- Myosin Heavy Chains
- Oligonucleotide
- oligonucleotides
- Oligonucleotides,Antisense
- Peptide Elongation Factor 1
- Peptide Elongation Factors
- pharmacology
- Poly(ADP-ribose) Polymerases
- Polymerase
- protein
- report
- research
- results
- SERUM
- SKELETAL-MUSCLE
- state
- Support,Non-U.S.Gov't
- Support,U.S.Gov't,P.H.S.
- Time Factors
- tissue
- Tissue Distribution
- TISSUES
- Transfection
- transition
- United States
- UNITED-STATES
- university
