Skeletal muscle hypertrophy and atrophy signaling pathways.

By D. Glass. International Journal of Biochemistry and Cell Biology, 2005

1,138 citations recorded by the source corpus.

Subfields: Cellular and Molecular Neuroscience, Genetics, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/87ddaac8cab24f60d4962e048cbe390312369db8

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. J. Hawley
3. Vernon G. Coffey
4. A. Goldberg
5. D. Glass
6. S. Schiaffino
7. S. Lecker
8. B. Spiegelman

In Genetics

1. M. Sandri
2. J. Hawley
3. Vernon G. Coffey
4. A. Goldberg
5. B. Spiegelman
6. Christoph Handschin
7. D. Glass

In Molecular Biology

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

Citations in the corpus

• Reversal of cancer cachexia and muscle wasting by ActRIIB antagonism leads to prolonged survival. (2010, background): “While activation of the AKT pathway is associated with muscle growth, in atrophying muscles there is an activation of FOXO as well as NF-kB and possibly also Smad transcription factors, which promote protein degradation (Glass, 2005; Sandri et al., 2004).”
• The Molecular Bases of Training Adaptation (2007, methodology): “Cytokines are small polypeptides released at the site of inflammation in response to numerous factors including cachexia, sepsis, and exercise-induced muscle damage (Cannon and St. Pierre 1998; Jackman and Kandarian 2004; Glass 2005; Petersen and Pedersen 2005).”
• The role of exercise and PGC1α in inflammation and chronic disease (2008, background): “When stimulated by strength training, type IIB and type IIX muscle fibres can undergo substantial hypertroph”
• The E3 Ligase MuRF1 degrades myosin heavy chain protein in dexamethasone-treated skeletal muscle. (2007, background): “The E3 ubiquitin ligase MuRF1 has been shown to be transcriptionally induced in at least 13 models of muscle atrophy (Glass, 2005).”
• FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells. (2007, background): “Because of the importance of the ubiquitin-proteasome pathway in degrading myofibrillar proteins, there has been appreciable interest in developing inhibitors of the atro-phy-specific ubiquitin ligases or the proteasome to retard muscle atrophy and cachexia (Beehler et al., 2006; Glass, 2005).”
• Interleukin-6 is an essential regulator of satellite cell-mediated skeletal muscle hypertrophy. (2008, background): “Notably, autocrine/paracrine loops involving IGF-1 (insulin-like growth factor 1) are able to induce myofiber hypertrophy by activating PI3K (phosphatidylinositol 3-kinase)/ AKT-dependent pathways (Bodine et al., 2001; Glass, 2005).”
• An official American Thoracic Society/European Respiratory Society statement: update on limb muscle dysfunction in chronic obstructive pulmonary disease. (2014, background): “Disuse Associated with weakness, atrophy, changes in fiber type distribution and metabolic alterations (118, 120–123) Inflammation Triggering of the muscle proteolysis cascade (14, 15, 139, 140) Oxidative stress Triggering of the muscle proteolysis cascade (147, 149, 150) Associated with reduced mus”