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Article Abstract
The aim of the present study was to investigate the effects of Oncostatin M receptor (OSMR) subunit gp130 knockdown on insulin-stimulated glucose metabolism-related signaling pathways and glucose uptake in skeletal muscle cells. siRNA-mediated gp130 knockdown was conducted in C2C12 muscle cells, and insulin was added and incubated for 1 h. The cells were cultivated to analyze the mRNA levels of gp130, phosphorylation of STAT3, and glucose metabolism-regulated signaling pathways, and OSM levels in the culture medium were analyzed. The phosphorylation of STAT 3 was significantly decreased in gp130 cell. The insulin stimulation was significantly increased in both gp130 and gp130 and the phosphorylation of IRS-1 Ser 1101 was significantly decreased in gp130. PI3-kinase activity and Akt Thr 308 phosphorylation were significantly decreased in gp130. The insulin-stimulated increase in glucose uptake rate was significantly attenuated in gp130. In the culture medium, OSM levels were significantly lower in gp130compared to gp130 cell. In conclusion, the knockdown of gp130 caused a decrease in STAT 3 phosphorylation and resulted in the attenuation of insulin-mediated glucose metabolism signaling in skeletal muscle cells. Thus, an excessive increase in extracellular OSM may induce blunted insulin action in skeletal muscle cells.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11289081 | PMC |
| http://dx.doi.org/10.1038/s41598-024-68613-2 | DOI Listing |
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