MOTS-c 10mg· 10mg

MOTS-c has been proposed to act primarily through activation of AMP-activated protein kinase (AMPK), the central cellular energy sensor. In skeletal muscle and adipose tissue preparations, the peptide elevates phosphorylated AMPK and downstream phospho-ACC, mimicking aspects of caloric restriction and exercise signaling. The upstream mechanism is thought to involve modulation of folate-methionine metabolism: MOTS-c has been observed to inhibit the AICAR-to-IMP conversion catalyzed by AICAR transformylase, elevating intracellular AICAR and thereby activating AMPK.

Under metabolic stress, MOTS-c translocates to the nucleus where it co-occupies stress-responsive promoter regions with nuclear factor erythroid 2-related factor 2 (NRF2) and other transcription factors, modulating expression of antioxidant and metabolic genes. The peptide has also been reported to engage cell-surface signaling through unidentified receptors, with effects on insulin sensitivity in hepatocyte and adipocyte preparations.