Leptin is a peptide hormone that plays a crucial role in numerous physiological processes, including the regulation of metabolism, feeding, and energy homeostasis. The JAK/STAT signaling pathway plays a major role in signal transduction and activation of cellular responses, in which the transcription factor STAT3 is activated by phosphorylation and is subsequently involved in regulating the expression of genes that are essential for the action of leptin. However, the described mechanism of leptin in skeletal muscle culture has not yet been fully characterized. In this master thesis we examined the signaling response of skeletal muscle cells treated with leptin, focusing on measuring the phosphorylation of STAT1 and STAT3. We used primary human skeletal muscle cells and rat L6 skeletal muscle cells which were cultured to confluence and then differentiated into multinucleated myotubes.
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