ArticleMolecular and cellular biochemistry2011
Pharmacological inhibition of HSP90 activity negatively modulates myogenic differentiation and cell survival in C2C12 cells.
Article in Molecular and cellular biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 29 citations in OpenAlex.
- Sarcopenia and sepsis fuel a self-perpetuating cycle of immunometabolism decline.Frontiers in immunology · 2026Review
- Small Molecule Screening Identifies HSP90 as a Modifier of RNA Foci in Myotonic Dystrophy Type 1.Molecular and cellular biology · 2025Article
- Heat Shock Proteins: Important Helpers for the Development, Maintenance and Regeneration of Skeletal Muscles.Muscles (Basel, Switzerland) · 2023Review
- Heat shock protein 27 regulates myogenic and self-renewal potential of bovine satellite cells under heat stress.Journal of animal science · 2023Article
- Geldanamycin treatment does not result in anti-cancer activity in a preclinical model of orthotopic mesothelioma.PloS one · 2023Article
- Degradation of ribosomal and chaperone proteins is attenuated during the differentiation of replicatively aged C2C12 myoblasts.Journal of cachexia, sarcopenia and muscle · 2022Article
- Myoglobin maturation is driven by the hsp90 chaperone machinery and by soluble guanylyl cyclase.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- Expression and localization of heat-shock proteins during skeletal muscle cell proliferation and differentiation and the impact of heat stress.Cell stress & chaperones · 2019Article
- Pharmacological targeting of HSP90 with 17-AAG induces apoptosis of myogenic cells through activation of the intrinsic pathway.Molecular and cellular biochemistry · 2018Article
- Recurrent heat shock impairs the proliferation and differentiation of C2C12 myoblasts.Cell stress & chaperones · 2018Article
- BGP-15 improves contractile function of regenerating soleus muscle.Journal of muscle research and cell motility · 2018Article
- Therapeutic potential of heat shock protein induction for muscular dystrophy and other muscle wasting conditions.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- Article
- Utility of 17-(allylamino)-17-demethoxygeldanamycin treatment for skeletal muscle injury.Cell stress & chaperones · 2016Article
- A Remodeled Hsp90 Molecular Chaperone Ensemble with the Novel Cochaperone Aarsd1 Is Required for Muscle Differentiation.Molecular and cellular biology · 2016Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heat-shock protein90 (HSP90) plays an essential role in maintaining stability and activity of its clients. HSP90 is involved in cell differentiation and survival in a variety of cell types. To elucidate the possible role of HSP90 in myogenic differentiation and cell survival, we examined the time course of changes in the expression of myogenic regulatory factors, intracellular signaling molecules, and anti-/pro-apoptotic factors when C2C12 cells were cultured in differentiation condition in the presence of a HSP90-specific inhibitor, geldanamycin. Furthermore, we examined the effects of geldanamycin on muscle regeneration in vivo. Our results showed that geldanamycin inhibited myogenic differentiation with decreased expression of MyoD, myogenin and reduced phosphorylation levels of Akt1. Geldanamycin had little effect on the phosphorylation levels of p38MAPK and ERK1/2 but reduced the phosphorylation levels of JNK. Along with myogenic differentiation, geldanamycin increased apoptotic nuclei with decreased expression of Bcl-2. The skeletal muscles forced to regenerate in the presence of geldanamycin were of poor repair with small regenerating myofibers and increased connective tissues. Together, our findings suggest that HSP90 may modulate myogenic differentiation and may be involved in cell survival.
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