JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Originally published In Press as doi:10.1074/jbc.M110685200 on November 27, 2001

J. Biol. Chem., Vol. 277, Issue 7, 5418-5425, February 15, 2002
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
277/7/5418    most recent
M110685200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ruest, L.-B.
Right arrow Articles by Wang, E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ruest, L.-B.
Right arrow Articles by Wang, E.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Peptide Elongation Factor eEF1A-2/S1 Expression in Cultured Differentiated Myotubes and Its Protective Effect against Caspase- 3-mediated Apoptosis*

Louis-Bruno RuestDagger §, Richard MarcotteDagger , and Eugenia WangDagger §||

From the Dagger  Bloomfield Center for Research in Aging, Lady Davis Institute for Medical Research, Sir Mortimer B. Davis Jewish General Hospital, the Department of Medicine, McGill University, Montreal, Quebec H3T 1E2, Canada, and the § Department of Biochemistry and Molecular Biology, University of Louisville School of Medicine, Louisville, Kentucky 40202

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 effect.

* This work was supported in part by National Institutes of Health Research Operating Grant P01 AG 10821-06 (to E. W.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Recipient of a doctoral research award from the Medical Research Council of Canada (now Canadian Institute of Health Research).

|| To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, University of Louisville, 470 S. Preston St., Rm. 304, Louisville, KY 40202. Tel.: 502-852-2554; Fax: 502-852-2555; E-mail: Eugenia.wang@louisville.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
H. J. Newbery, D. H. Loh, J. E. O'Donoghue, V. A. L. Tomlinson, Y.-Y. Chau, J. A. Boyd, J. H. Bergmann, D. Brownstein, and C. M. Abbott
Translation Elongation Factor eEF1A2 Is Essential for Post-weaning Survival in Mice
J. Biol. Chem., September 28, 2007; 282(39): 28951 - 28959.
[Abstract] [Full Text] [PDF]

Home page
 Physiol. GenomicsHome page
J. C. Wu, J. M. Spin, F. Cao, S. Lin, X. Xie, O. Gheysens, I. Y. Chen, A. Y. Sheikh, R. C. Robbins, A. Tsalenko, et al.
Transcriptional profiling of reporter genes used for molecular imaging of embryonic stem cell transplantation
Physiol Genomics, March 13, 2006; 25(1): 29 - 38.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
N. M. Borradaile, K. K. Buhman, L. L. Listenberger, C. J. Magee, E. T.A. Morimoto, D. S. Ory, and J. E. Schaffer
A Critical Role for Eukaryotic Elongation Factor 1A-1 in Lipotoxic Cell Death
Mol. Biol. Cell, February 1, 2006; 17(2): 770 - 778.
[Abstract] [Full Text] [PDF]

Home page
 IOVSHome page
N. A. Whitlock, K. Lindsey, N. Agarwal, C. E. Crosson, and J.-X. Ma
Heat Shock Protein 27 Delays Ca2+-Induced Cell Death in a Caspase-Dependent and -Independent Manner in Rat Retinal Ganglion Cells
Invest. Ophthalmol. Vis. Sci., March 1, 2005; 46(3): 1085 - 1091.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J.-L. Lee, C.-T. Lin, L.-L. Chueh, and C.-J. Chang
Autocrine/Paracrine Secreted Frizzled-related Protein 2 Induces Cellular Resistance to Apoptosis: A POSSIBLE MECHANISM OF MAMMARY TUMORIGENESIS
J. Biol. Chem., April 9, 2004; 279(15): 14602 - 14609.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.