We are finally beginning to unlock the mechanisms underlying Ca2+-stimulated muscle differentiation and cytokine-mediated muscle wasting. Gaining a better understanding of the signaling pathways that regulate muscle development and decay improves the prospects for repairing aged, injured and diseased muscle.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 12 print issues and online access
$209.00 per year
only $17.42 per issue
Rent or buy this article
Prices vary by article type
from$1.95
to$39.95
Prices may be subject to local taxes which are calculated during checkout
References
Nelson, K.A. The Cancer-Anorexia-Cachexia syndrome. Seminars in Oncology 27, 64–68 (2000).
Oliff, A. et al. Tumors secreting human TNF/cachetin induce cachexia in mice. Cell 50, 555–563 (1987).
Lecker, S.H., Solomon, V., Mitch, W.E., & Goldberg, A.L. Muscle protein breakdown and the critical role of the ubiquitin proteasome pathway in normal and diseased states. J. Nutr. 129, 227–237 (1999).
McKinsey, T.A., Zhang, C.-L., Lu, J. & Olson, E.N. Signal dependent nuclear export of a histone deacetylase regulates muscle differentiation. Nature (in the press).
Guttridge, D.C., Mayo, M.W., Madrid, L.V., Wang, C.-Y., & Baldwin, A.S. NF-κB-induced loss of MyoD mRNA: Possible role in muscle decay and cachexia. Science 289, 2363–2366 (2000).
Yaffe, D. & Saxel, O. Serial passaging and differentiation of myogenic cells isolated from mouse muscle. Nature 270, 725–727 (1977).
Black, B.L. & Olson, E.N. Transcriptional control of muscle development by myocyte enhancer factor-2 (MEF2) proteins. Ann. Rev. Cell Dev. Biol. 14, 167–196 (1998).
Archer, S. & Hodin, R. Histone acetylation and cancer. Curr. Opin. In Gen. and Dev. 9, 171–174 (1999).
Sartorelli, V., Huang, J., Hamamori, Y. & Kedes, L. Molecular mechanisms of myogenic coactivation by p300: Direct interaction with the activation domain of MyoD and with the MADS box of MEF2C. Mol. Cell Biol 17, 1010–1025 (1997).
Chen, S.L., Dowhan, D.H., Hosking, B.M. & Muscat, G.E. The steroid receptor coactivator, GRIP-1, is necessary for MEF-2C-dependent gene expression and skeletal muscle differentiation. Genes Dev. 14, 1209–1230 (2000).
Miska, E.A., Karlsson, C., Langley, E., Neilson, S., Pines, J. & Kouzarides, T. HDAC4 associates with and represses the MEF2 transcription factor. EMBO 18, 5099–5107 (1999)
Lu, J., McKinsey, T.A., Zhang, C.L. & Olson, E.N. Regulation of skeletal myogenesis by association of the MEF2 transcription factor with class II HDACs. Mol. Cell 6, 233–244 (2000).
Grozinger, C. & Schreiber, S. Regulation of HDAC 4 and 5 and transcriptional activity by 14-3-3 dependent cellular localisation. Proc. Natl. Acad. Sci. U S A 97, 7835–7840 (2000).
Olson, E.N. & Sanders Williams, R. Calcineurin signalling and muscle remodeling. Cell 101, 689–692 (2000).
Szalay, K., Razga, Z. & Duda, E. TNF inhibits myogenesis and downregulates the expression of myogenic regulatory factors, myoD and myogenin. Eur. J Cell Biol 74, 391–398 (1997).
Kawamura, I. et al. Intratumoral injection of oligonucleotides to the NF-κB binding site inhibits cachexia in a mouse tumor model. Gene Ther. 6, 91–95 (1999).
Megeney, L.A., Kablar, B., Garrett, K., Anderson, J.E. & Rudnicki, M.A. MyoD is required for myogenic stem cell function in adult skeletal muscle Genes Dev. 10, 1173–1183 (1996).
Guttridge, D.C., Albanese, C., Reuther, J.Y., Pestell, R.G. & Baldwin A.S. NF-κB control cell growth and differentiation through transcriptional regulation of cyclin D1. Mol. Cell. Biol. 19, 5785–5799 (1999).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Muscat, G., Dressel, U. Not a minute to waste. Nat Med 6, 1216–1217 (2000). https://doi.org/10.1038/81312
Issue Date:
DOI: https://doi.org/10.1038/81312
This article is cited by
-
Increased p70s6k phosphorylation during intake of a protein–carbohydrate drink following resistance exercise in the fasted state
European Journal of Applied Physiology (2010)