The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Hsp70 overexpression inhibits NF‐κB and Foxo3a transcriptional activities and prevents skeletal muscle atrophy
Open accessAbstract
Heat shock protein 70 (Hsp70) is a highly conserved and ubiquitous protein that is reported to provide cytoprotection in various cell types and tissues. However, the importance of Hsp70 expression during skeletal muscle atrophy, when Hsp70 levels are significantly decreased, is not known. The current study aimed to determine whether plasmid‐mediated overexpression of Hsp70, in the soleus muscle of rats, was sufficient to regulate specific atrophy signaling pathways and attenuate skeletal muscle disuse atrophy. We found that Hsp70 overexpression prevented disuse muscle fiber atrophy and inhibited the increased promoter activities of atrogin‐1 and MuRF1. Importantly, the transcriptional activities of Foxo3a and NF‐κB, which are implicated in the regulation of atrogin‐1 and MuRF1, were abolished by Hsp70. These data suggest that Hsp70 may regulate key atrophy genes through inhibiting Foxo3a and NF‐κB activities during disuse. Indeed, we show that specific inhibition of Foxo3a prevented the increases in both atrogin‐1 and MuRF1 promoter activities during disuse. However, inhibition of NF‐κB did not affect the activation of either promoter, suggesting its requirement for disuse atrophy is through its regulation of other atrophy genes. We conclude that overexpression of Hsp70 is sufficient to inhibit key atrophy signaling pathways and prevent skeletal muscle atrophy.— Senf, S. M., Dodd, S. L., McClung, J. M., Judge, A. R. Hsp70 overexpression inhibits NF‐κB and Foxo3a transcriptional activities and prevents skeletal muscle atrophy. FASEB J. 22, 3836–3845 (2008)
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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 E3 Ligase MuRF1 Degrades Myosin Heavy Chain Protein in Dexamethasone-Treated Skeletal Muscle
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What do we really know about the ubiquitin-proteasome pathway in muscle atrophy?
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Valenzuela, P. L., Castillo‐García, A., Morales, J. S., Izquierdo, M., Serra‐Rexach, J. A., Santos‐Lozano, A., & Lucia, A. (2019) · Comprehensive Physiology · doi:10.1002/cphy.c190002 · Cited by 152
Metadata
- Authors
- Senf, S. M., Dodd, S. L., McClung, J. M., & Judge, A. R.
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 2008-07-21
- Volume
- 22
- Issue
- 11
- Pages
- 3836-3845
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- OpenAlex
- W2170722828
- Cited by
- 287
- References
- 7
- FWCI
- 6.70
- Type
- journal article
- Language
- en
- Open access
- green
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