EPO-receptor is present in mouse C2C12 and human primary skeletal muscle cells but EPO does not influence myogenesis

Physiological Reports

Volumn 2, Issue 3, 2014, Pages

  Lamon, Séverine ^a   Zacharewicz, Evelyn ^a   Stephens, Andrew N ^b   Russell, Aaron P ^a  

^a DEAKIN UNIVERSITY   (Australia)

^b HUDSON INSTITUTE OF MEDICAL RESEARCH   (Australia)

Author keywords

Cytokine; Erythropoietin; Erythropoietinreceptor; Myogenesis; Skeletal muscle

Indexed keywords

ERYTHROPOIETIN RECEPTOR;

ANIMAL CELL; ARTICLE; CELL CULTURE; CELL PROLIFERATION; CONTROLLED STUDY; DNA SEQUENCE; ERYTHROPOIETIN RECEPTOR GENE; EXTRACELLULAR MATRIX; GENE; GENE EXPRESSION; GENETIC TRANSCRIPTION; HUMAN; HUMAN CELL; INTRACELLULAR SIGNALING; MOUSE; MUSCLE DEVELOPMENT; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN EXPRESSION; PROTEIN SYNTHESIS; REAL TIME POLYMERASE CHAIN REACTION; RNA EXTRACTION; SEQUENCE ANALYSIS; SKELETAL MUSCLE CELL; WESTERN BLOTTING;

EID: 85009069684     PISSN: None     EISSN: 2051817X     Source Type: Journal    
DOI: 10.1002/phy2.256     Document Type: Article

References (44)

1. Christensen, B., C. Lundby, N. Jessen, T. S. Nielsen, P. F. Vestergaard, N. Moller, et al. 2012. Evaluation of functional erythropoietin receptor status in skeletal muscle in vivo: acute and prolonged studies in healthy human subjects. PLoS One 7: e31857.
2. Constantinescu, S. N., S. Ghaffari, and H. F. Lodish. 1999. The erythropoietin receptor: structure, activation and intracellular signal transduction. Trends Endocrinol. Metabol. 10: 18-23.
3. Czifra, G., I. B. Toth, R. Marincsak, I. Juhasz, I. Kovacs, P. Acs, et al. 2006. Insulin-like growth factor-I-coupled mitogenic signaling in primary cultured human skeletal muscle cells and in C2C12 myoblasts. A central role of protein kinase Cdelta. Cell. Signal. 18: 1461-1472.
4. Damen, J. E., A. L. Mui, L. Puil, T. Pawson, and G. Krystal. 1993. Phosphatidylinositol 3-kinase associates, via its Src homology 2 domains, with the activated erythropoietin receptor. Blood 81: 3204-3210.
5. D’Andrea, A. D., and L. I. Zon. 1990. Erythropoietin receptor. Subunit structure and activation. J. Clin. Invest. 86: 681-687.
6. Dogra, C., H. Changotra, S. Mohan, and A. Kumar. 2006. Tumor necrosis factor-like weak inducer of apoptosis inhibits skeletal myogenesis through sustained activation of nuclear factor-kappaB and degradation of MyoD protein. J. Biol. Chem. 281: 10327-10336.
7. Dogra, C., H. Changotra, N. Wedhas, X. Qin, J. E. Wergedal, and A. Kumar. 2007a. TNF-related weak inducer of apoptosis (TWEAK) is a potent skeletal muscle-wasting cytokine. Faseb J. 21: 1857-1869.
8. Dogra, C., S. L. Hall, N. Wedhas, T. A. Linkhart, and A. Kumar. 2007b. Fibroblast growth factor inducible 14 (Fn14) is required for the expression of myogenic regulatory factors and differentiation of myoblasts into myotubes. Evidence for TWEAK-independent functions of Fn14 during myogenesis. J. Biol. Chem. 282: 15000-15010.
9. Elliott, S., L. Busse, M. B. Bass, H. Lu, I. Sarosi, A. M. Sinclair, et al. 2006. Anti-Epo receptor antibodies do not predict Epo receptor expression. Blood 107: 1892-1895.
10. Elliott, S., S. Swift, L. Busse, S. Scully, G. Van, J. Rossi, et al. 2013. Epo receptors are not detectable in primary human tumor tissue samples. PLoS One 8: e68083.
11. Fisher, J. W. 2003. Erythropoietin: physiology and pharmacology update. Exp. Biol. Med. 228: 1-14.
12. Foletta, V. C., E. L. Brown, Y. Cho, R. J. Snow, A. Kralli, and A. P. Russell. 2013. Ndrg2 is a PGC-1alpha/ERRalpha target gene that controls protein synthesis and expression of contractile-type genes in C2C12 myotubes. Biochim. Biophys. Acta 1833: 3112-3123.
13. Hojman, P., C. Brolin, H. Gissel, C. Brandt, B. Zerahn, B. K. Pedersen, et al. 2009. Erythropoietin over-expression protects against diet-induced obesity in mice through increased fat oxidation in muscles. PLoS One 4: e5894.
14. Jia, Y., R. Warin, X. Yu, R. Epstein, and C. T. Noguchi. 2009. Erythropoietin signaling promotes transplanted progenitor cell survival. Faseb J. 23: 3089-3099.
15. Jia, Y., N. Suzuki, M. Yamamoto, M. Gassmann, and C. T. Noguchi. 2012. Endogenous erythropoietin signaling facilitates skeletal muscle repair and recovery following pharmacologically induced damage. Faseb J. 26: 2847-2858.
16. Klingmuller, U., S. Bergelson, J. G. Hsiao, and H. F. Lodish. 1996. Multiple tyrosine residues in the cytosolic domain of the erythropoietin receptor promote activation of STAT5. Proc. Natl. Acad. Sci. USA 93: 8324-8328.
17. Krantz, S. B. 1991. Erythropoietin. Blood 77: 419-434.
18. Lamon, S., and A. P. Russell. 2013. The role and regulation of erythropoietin (EPO) and its receptor in skeletal muscle: how much do we really know?. Front. Physiol. 4: 176.
19. Launay, T., L. Hagstrom, S. Lottin-Divoux, D. Marchant, P. Quidu, F. Favret, et al. 2010. Blunting effect of hypoxia on the proliferation and differentiation of human primary and rat L6 myoblasts is not counteracted by Epo. Cell Prolif. 43: 1-8.
20. LeBaron, M. J., T. J. Ahonen, M. T. Nevalainen, and H. Rui. 2007. In vivo response-based identification of direct hormone target cell populations using high-density tissue arrays. Endocrinology 148: 989-1008.
21. Lundby, C., Y. Hellsten, M. B. Jensen, A. S. Munch, and H. Pilegaard. 2008. Erythropoietin receptor in human skeletal muscle and the effects of acute and long-term injections with recombinant human erythropoietin on the skeletal muscle. J. Appl. Physiol. 104: 1154-1160.
22. Miura, Y., O. Miura, J. N. Ihle, and N. Aoki. 1994. Activation of the mitogen-activated protein kinase pathway by the erythropoietin receptor. J. Biol. Chem. 269: 29962-29969.
23. Noguchi, C. T., L. Wang, H. M. Rogers, R. Teng, and Y. Jia. 2008. Survival and proliferative roles of erythropoietin beyond the erythroid lineage. Expert Rev. Mol. Med. 10: e36.
24. Ogilvie, M., X. Yu, V. Nicolas-Metral, S. M. Pulido, C. Liu, U. T. Ruegg, et al. 2000. Erythropoietin stimulates proliferation and interferes with differentiation of myoblasts. J. Biol. Chem. 275: 39754-39761.
25. Owens, J., K. Moreira, and G. Bain. 2013. Characterization of primary human skeletal muscle cells from multiple commercial sources. In Vitro Cell. Dev. Biol. Anim. 49: 695-705.
26. Pallard, C., F. Gouilleux, M. Charon, B. Groner, S. Gisselbrecht, and I. Dusanter-Fourt. 1995. Interleukin-3, erythropoietin, and prolactin activate a STAT5-like factor in lymphoid cells. J. Biol. Chem. 270: 15942-15945.
27. Penta, K., and S. T. Sawyer. 1995. Erythropoietin induces the tyrosine phosphorylation, nuclear translocation, and DNA binding of STAT1 and STAT5 in erythroid cells. J. Biol. Chem. 270: 31282-31287.
28. Plaisance, I., C. Morandi, C. Murigande, and M. Brink. 2008. TNF-alpha increases protein content in C2C12 and primary myotubes by enhancing protein translation via the TNF-R1, PI3K, and MEK. Am. J. Physiol. Endocrinol. Metab. 294: E241-E250.
29. Quelle, F. W., D. Wang, T. Nosaka, W. E. Thierfelder, D. Stravopodis, Y. Weinstein, et al. 1996. Erythropoietin induces activation of Stat5 through association with specific tyrosines on the receptor that are not required for a mitogenic response. Mol. Cell. Biol. 16: 1622-1631.
30. Rainczuk, A., J. R. Rao, J. L. Gathercole, N. J. Fairweather, S. Chu, R. Masadah, et al. 2014. Evidence for the antagonistic form of CXC-motif chemokine CXCL10 in serous epithelial ovarian tumours. Int. J. Cancer 134: 530-541
31. Rasmussen, P., E. M. Foged, R. Krogh-Madsen, J. Nielsen, T. R. Nielsen, N. V. Olsen, et al. 2010. Effects of erythropoietin administration on cerebral metabolism and exercise capacity in men. J. Appl. Physiol. 109: 476-483.
32. Remy, I., I. A. Wilson, and S. W. Michnick. 1999. Erythropoietin receptor activation by a ligand-induced conformation change. Science 283: 990-993.
33. Rommel, C., S. C. Bodine, B. A. Clarke, R. Rossman, L. Nunez, T. N. Stitt, et al. 2001. Mediation of IGF-1-induced skeletal myotube hypertrophy by PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways. Nat. Cell Biol. 3: 1009-1013.
34. Rotter, R., M. Menshykova, T. Winkler, G. Matziolis, I. Stratos, M. Schoen, et al. 2008. Erythropoietin improves functional and histological recovery of traumatized skeletal muscle tissue. J. Orthop. Res. 26: 1618-1626.
35. Rundqvist, H., E. Rullman, C. J. Sundberg, H. Fischer, K. Eisleitner, M. Stahlberg, et al. 2009. Activation of the erythropoietin receptor in human skeletal muscle. Eur. J. Endocrinol. 161: 427-434.
36. Schuler, B., J. Vogel, B. Grenacher, R. A. Jacobs, M. Arras, and M. Gassmann. 2012. Acute and chronic elevation of erythropoietin in the brain improves exercise performance in mice without inducing erythropoiesis. Faseb J. 26: 3884-3890.
37. Sharma, V., N. Harafuji, A. Belayew, and Y. W. Chen. 2013. DUX4 differentially regulates transcriptomes of human rhabdomyosarcoma and mouse C2C12 cells. PLoS One 8: e64691.
38. Sinclair, A. M., A. Coxon, I. McCaffery, S. Kaufman, K. Paweletz, L. Liu, et al. 2010. Functional erythropoietin receptor is undetectable in endothelial, cardiac, neuronal, and renal cells. Blood 115: 4264-4272.
39. Stephens, A. N., N. J. Hannan, A. Rainczuk, K. L. Meehan, J. Chen, P. K. Nicholls, et al. 2010. Post-translational modifications and protein-specific isoforms in endometriosis revealed by 2D DIGE. J. Proteome Res. 9: 2438-2449.
40. Tada, H., Y. Kagaya, M. Takeda, J. Ohta, Y. Asaumi, K. Satoh, et al. 2006. Endogenous erythropoietin system in non-hematopoietic lineage cells plays a protective role in myocardial ischemia/reperfusion. Cardiovasc. Res. 71: 466-477.
41. Vandenburgh, H. H., S. Hatfaludy, P. Karlisch, and J. Shansky. 1989. Skeletal muscle growth is stimulated by intermittent stretch-relaxation in tissue culture. Am. J. Physiol. 256: C674-C682.
42. Yasuda, Y., S. Masuda, M. Chikuma, K. Inoue, M. Nagao, and R. Sasaki. 1998. Estrogen-dependent production of erythropoietin in uterus and its implication in uterine angiogenesis. J. Biol. Chem. 273: 25381-25387.
43. Youssoufian, H., G. Longmore, D. Neumann, A. Yoshimura, and H. F. Lodish. 1993. Structure, function, and activation of the erythropoietin receptor. Blood 81: 2223-2236.
44. Zaman, K., H. Ryu, D. Hall, K. O’Donovan, K. I. Lin, M. P. Miller, et al. 1999. Protection from oxidative stress-induced apoptosis in cortical neuronal cultures by iron chelators is associated with enhanced DNA binding of hypoxia-inducible factor-1 and ATF-1/CREB and increased expression of glycolytic enzymes, p21(waf1/cip1), and erythropoietin. J. Neurosci. 19: 9821-9830.