The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
Intracellular signaling during skeletal muscle atrophy
Abstract
A variety of conditions lead to skeletal muscle atrophy including muscle inactivity or disuse, multiple disease states (i.e., cachexia), fasting, and age‐associated atrophy (sarcopenia). Given the impact on mobility in the latter conditions, inactivity could contribute in a secondary manner to muscle atrophy. Because different events initiate atrophy in these different conditions, it seems that the regulation of protein loss may be unique in each case. In fact differences exist between the regulation of the various atrophy conditions, especially sarcopenia, as evidenced in part by comparisons of transcriptional profiles as well as by the unique triggering molecules found in each case. By contrast, recent studies have shown that many of the intracellular signaling molecules and target genes are similar, particularly among the atrophies related to inactivity and cachexia. This review focuses on the most recent findings related to intracellular signaling during muscle atrophy. Key findings are discussed that relate to signaling involving muscle ubiquitin ligases, the IGF/PI3K/Akt pathway, FOXO activity, caspase‐3 activity, and NF‐kappaB signaling, and an attempt is made to construct a unifying picture of how these data can be connected to better understand atrophy. Once more detailed cellular mechanisms of the atrophy process are understood, more specific interventions can be designed for the attenuation of protein loss. Muscle Nerve, 2006
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Cites
Identification of ubiquitin ligases required for skeletal muscle atrophy.
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Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression
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IKKβ/NF-κB Activation Causes Severe Muscle Wasting in Mice
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The Molecular Basis of Skeletal Muscle Atrophy
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Mono- Versus Polyubiquitination: Differential Control of p53 Fate by Mdm2
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Atrophy of the soleus muscle by hindlimb unweighting
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What do we really know about the ubiquitin-proteasome pathway in muscle atrophy?
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Cited by
Fielding, R. A., Vellas, B., Evans, W. J., Bhasin, S., Morley, J. E., Newman, A. B., Abellan van Kan, G., Andrieu, S., Bauer, J., Breuille, D., et al. (2011) · Journal of the American Medical Directors Association · doi:10.1016/j.jamda.2011.01.003 · Cited by 3,256
“Myostatin D inhibits cell cycling through SMAD3 and MyoD, thus inhibiting the production of satellite cells (52) while testosterone increases satellite cell production by stimulating β-catenin.”
BackgroundZhao, J., Brault, J. J., Schild, A., Cao, P., Sandri, M., Schiaffino, S., Lecker, S. H., & Goldberg, A. L. (2007) · Cell Metabolism · doi:10.1016/j.cmet.2007.11.004 · Cited by 1,489
The Molecular Basis of Skeletal Muscle Atrophy
Jackman, R. W., & Kandarian, S. C. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00579.2003 · Cited by 1,008
The Molecular Bases of Training Adaptation
Coffey, V. G., & Hawley, J. A. (2007) · Sports Medicine · doi:10.2165/00007256-200737090-00001 · Cited by 756
Salminen, A., Huuskonen, J., Ojala, J., Kauppinen, A., Kaarniranta, K., & Suuronen, T. (2008) · Ageing Research Reviews · doi:10.1016/j.arr.2007.09.002 · Cited by 581
Metadata
- Authors
- Kandarian, S. C., & Jackman, R. W.
- Venue
- Muscle & Nerve
- Publisher
- Wiley
- Published
- 2005-10-14
- Volume
- 33
- Issue
- 2
- Pages
- 155-165
- ISSN
- 0148-639X (ISSN-L)
- 1097-4598
- OpenAlex
- W2038996595
- Cited by
- 393
- References
- 12
- FWCI
- 8.30
- Type
- journal article
- Language
- en
- Open access
- closed
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