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.
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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).
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Muscat, G., Dressel, U. Not a minute to waste. Nat Med 6, 1216–1217 (2000). https://doi.org/10.1038/81312
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DOI: https://doi.org/10.1038/81312
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