Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression

By S. Lecker, R. Jagoe, A. Gilbert, Marcelo Gomes, Vickie E. Baracos, J. Bailey, S. Price, W. Mitch, A. Goldberg. The FASEB Journal, 2004

1,572 citations recorded by the source corpus.

Subfields: Cellular and Molecular Neuroscience, Genetics, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/c587a0897f0fa08e465daf59eabb1f564be5bebb

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cellular and Molecular Neuroscience

1. M. Sandri
2. A. Goldberg
3. J. Hawley
4. Vernon G. Coffey
5. D. Glass
6. S. Schiaffino
7. S. Lecker
8. J. Sacheck

In Genetics

1. M. Sandri
2. J. Hawley
3. A. Goldberg
4. Vernon G. Coffey
5. D. Glass
6. P. Bonaldo

In Molecular Biology

1. M. Sandri
2. S. Schiaffino
3. A. Goldberg
4. C. Mammucari
5. J. Hawley
6. Vernon G. Coffey
7. D. Glass
8. S. Lecker

Citations in the corpus

• Mitochondrial fission and remodelling contributes to muscle atrophy (2010, background): “Several metabolic adaptations occur in atrophying muscles (Lecker et al, 2004; Sandri et al, 2006).”
• The role of FoxO in the regulation of metabolism (2008, background): “Many of the transcripts whose expressions are altered in other models of atrophy such as diabetes, cancer and fasting are also altered following denervation (Lecker et al., 2004).”
• Cancer cachexia: mediators, signaling, and metabolic pathways. (2012, background): “Transcriptional activation of ubiquitin proteasome pathway (UPP) components has been found in the skeletal muscle of both rodent models (Lecker et al., 2004) and patients with pancreatic, upper gastrointestinal (UGI), or liver cancer (Williams et al., 1999; Bossola et al., 2003; Khal et al., 2005),…”
• The Molecular Bases of Training Adaptation (2007, background): “The evidence supporting their proposed role in muscle atrophy is compelling as the increase in gene expression of these ubiquitin proteins has been systematically induced with fasting, cachexia, diabetes, uremia, denervation, glucocorticoid release and disuse atrophy models (Bodine et al. 2001a; Jon”
• FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells. (2007, background): “Previously, we found that LC3 and Gabarapl1 are induced in muscles in diverse types of atrophy (Lecker et al., 2004).”
• Skeletal muscle hypertrophy and atrophy signaling pathways. (2005, background): “…(Tawa, Odessey, & Goldberg, 1997); the amount of polyubiquitin conjugation per total protein measured increases during atrophy (Lecker et al., 1999); mRNA levels of genes, which encode distinct components of the ubiquitin pathway increase during atrophy (Jagoe et al., 2002; Lecker et al., 2004).”
• Sarcopenia: an undiagnosed condition in older adults. Current consensus definition: prevalence, etiology, and consequences. International working group on sarcopenia. (2011, background): “Cytokines stimulate MURF 1 (muscle Ring finger), which, like atrogin, activates the ubiquitin-proteasome system (56).”
• Glucocorticoid-induced skeletal muscle atrophy. (2013, background): “…analyses of muscle atrophy due to a variety of wasting diseases are several genes (Atrogin-1, MuRF-1, Cathepsin-L, PDK4, p21, Gadd45, 4E-BP1) controlled by the FOXO transcription factors (Almon et al., 2007; Jagoe et al., 2002; Komamura et al., 2003; Lecker et al., 2004; Waddell et al., 2008).”
• Autophagy is required to maintain muscle mass. (2009, background): “Loss of muscle mass is controlled by a transcriptional program that requires activation of a subset of genes named atrophy-related genes or atrogenes (Lecker et al., 2004).”
• IGF-I stimulates muscle growth by suppressing protein breakdown and expression of atrophy-related ubiquitin ligases, atrogin-1 and MuRF1. (2004, background): “In various types of atrophy, including Cushing’s syndrome (22), diabetes (39), sepsis (50), cancer cachexia (2), and renal failure (41), muscles exhibit a common series of adaptations, including increased content of Ub-protein conjugates (55) and of mRNA encoding Ub (32), certain ubiquitination enzy”
• Rapid disuse and denervation atrophy involve transcriptional changes similar to those of muscle wasting during systemic diseases (2007, methodology): “After quality control tests from Incyte were applied to the data, data were imported into the Resolver software for further analysis (5) using a specific Rosetta error model generated for Incyte microarrays (46).”