Key result
Serum deprivation upregulates ubiquitin, proteasome, and calpain mRNA expression in chick myotubes.
Why the study?
Serum deprivation was previously shown to stimulate myofibrillar proteolysis in chick myotubes, but its effect on proteolytic-related gene expression was unclear.
Serum deprivation stimulates ubiquitin-proteasome and calpain proteolytic pathways in chick myotubes, increasing myofibrillar proteolysis.
Answers are grounded in this paper and cite their sources.
Serum deprivation activates ubiquitin-proteasome and calpain pathways in myotubes; leaves open their role in clinical muscle wasting.
We previously reported that serum deprivation stimulates myofibrillar proteolysis in chick myotubes. In the present study, we examined the effect of serum deprivation on expression of the proteolytic-related genes (ubiquitin, proteasome, calpains, and cathepsin B) by real-time PCR of cDNA in chick myotubes. Myotubes were incubated with serum-free medium for 24 h. Ubiquitin and proteasome subunits (C1 and C2) and calpains (m-, mu-, and p94/calpain-3) but not cathepsin B mRNA expression were increased by serum deprivation. These results indicate that serum deprivation stimulates ubiquitin-proteasome and calpain proteolytic pathways, resulting in an increase in myofibrillar proteolysis in chick myotubes.
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Nakashima et al. (2005) studied this question. Serum deprivation was evaluated on Expression of proteolytic-related genes (ubiquitin, proteasome, calpains, and cathepsin B). Serum deprivation for 24 hours increased the mRNA expression of ubiquitin, proteasome subunits, and calpains, but not cathepsin B, in chick myotubes.
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