IGF-I stimulates muscle growth by suppressing protein breakdown and expression of atrophy-related ubiquitin ligases, atrogin-1 and MuRF1.

By J. Sacheck, A. Ohtsuka, S. C. McLary, A. Goldberg. American Journal of Physiology. Endocrinology and Metabolism, 2004

651 citations recorded by the source corpus.

Subfields: Cell Biology, Cellular and Molecular Neuroscience, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/c36ef9be8d1fdc872d072c30af54b45388f88fa0

How researchers see this paper

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

In Cell Biology

1. S. Schiaffino
2. M. Sandri
3. C. Mammucari
4. S. Lecker
5. P. Delafontaine
6. Tadashi Yoshida
7. W. Mitch
8. A. Goldberg

In Cellular and Molecular Neuroscience

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

In Molecular Biology

1. M. Sandri
2. S. Schiaffino
3. A. Goldberg
4. C. Mammucari
5. D. Glass
6. S. Lecker
7. E. Masiero
8. P. Delafontaine

Citations in the corpus

• Mechanisms of IGF-1-Mediated Regulation of Skeletal Muscle Hypertrophy and Atrophy (2020, background): “In myofibers, IGF-1 rapidly and strongly reduced Dex-induced Atrogin-1 expression (~80% reduction after 6 h), whereas MuRF-1 mRNA reduction occurred more slowly (~30% reduction after 18 h) [38].”
• The E3 Ligase MuRF1 degrades myosin heavy chain protein in dexamethasone-treated skeletal muscle. (2007, background): “…it has previously been shown that DEX treatment can induce atrophy and the upregulation of MuRF1 and MAFbx in myotubes (Latres et al., 2005; Sacheck et al., 2004) and the selective loss of MYH by increasing protein 382 Cell Metabolism 6, 376–385, November 2007 ª2007 Elsev turnover…”
• FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells. (2007, methodology): “…that IGF-1 or insulin can reduce protein degradation rapidly by sup-pressingautophagyviamTORactivationandwithtimecan also suppress this process by inactivating FoxOs, which also inhibits proteasomal degradation through the reduction of atrogin-1 and MuRF1 transcription (Sacheck et al., 2004).”
• FoxO3 controls autophagy in skeletal muscle in vivo. (2007, methodology): “1 mM) was added, and proteolysis was measured starting 1 hr later (Sacheck et al., 2004).”
• Protein degradation by the ubiquitin-proteasome pathway in normal and disease states. (2006, background): “Administration of high doses of these hormones to rodents, like Cushing’s syndrome in humans, stimulates protein degradation in muscle via atrogin-1, and this response requires FoxO activation (77,106,107).”
• Cellular and molecular mechanisms of muscle atrophy (2013, neutral): “…experiments (including diabetes, cancer cachexia, chronic renal failure, fasting and denervation) have muscle atrophy in common, the commonly up- or downregulated genes are believed to regulate the loss of muscle components and are called atrophy-related genes or ‘atrogenes’ (Sacheck et al., 2007).”