MOTS-C – 10MG

MOTS-c

MOTS-c (mitochondrial open-reading-frame of the 12S rRNA-c) peptide was a known novel mitochondria-derived peptide. It is a 16 amino acid-long peptide which is produced in tissues and plasma, signaling towards an endocrine mechanism and cell-specific role. Working either as a cell-specific compound or as a hormone, this peptide putatively works by activation of the AMP-activated protein kinase (AMPK) pathway. Two mitochondrial-derived peptides (MDPs), Humanin and MOTS-c, have been characterized so far. The peptide is thought to translocate into cellular nuclei and modify gene expression when the organism experiences metabolic stress. Among the proteins released in vitro and perhaps also in vivo is MOTS-c peptide, which serves as a "mitochondrial hormone" or, more informally, a "mitokine”.

Animal studies have shown that the MOTS-c peptide exerts several potential effects, such as improved exercise performance, cellular and tissue metabolism control, and myoblast adaptation. Aging and age-related changes in MOTS-c expression The effects of DOT110/NT114 on the traits were mainly defined by age and age-related changes of their MOTS-c levels, according to existing literature. The team posits that levels and activity of MOTS-c may decrease during aging, highlighting a purported involvement in cellular senescence and age-associated impairment of metabolism. In addition, MOTS-c may work on reported aging regulators like NAD+ and sirtuins hinting towards its plausible participation in pathways that are effectuated as lifespan of the cell (75-80). 1 Joseph C Reynolds et al., “Mitochondria are central metabolic organelles with significant implications in cell aging and also coordinate wide-ranging physiologic activities, at least in part through peptides encoded from a discrete genome”. Physical activity has also been suggested to increase endogenous expression of the peptide, increasing cellular metabolism.

Research has indicated, that this peptide might be able to escape the mitochondrial site and translocate to the cellular nuclei where it could perhaps affect gene expression. In particular, the peptide might play a role in the regulation of several genes, possibly interacting with such having antioxidant response elements (ARE), providing insights on a putative crosstalk with stress-responsive transcription factors such as NRF2. These results are consistent with a genetically integrated system of mitonuclear communication - that is, mitochondrial and nuclear genomes both may encode factors required for their cross-regulation. And this may then skew the restriction of glucose uptake. The suggestion to test this hypothesis came after an experiment where high-fat feeding was given to experimental mice and only half got the peptide. This final finding provides a clue to the potential metabolic effects of MOTS-c on cellular metabolism: namely that MOTS-c may inhibit folate cycle directly tethered de novo purine biosynthesis and lead into AMPK activation (based on our other results AMPK activation is a critical factor for the subsequent beneficial metabolic effects). This suggests a more general role of this peptide in the control of insulin sensitivity and metabolic homeostasis, which help to explain the finding that these reduce age-related as well as high-fat-induced insulin resistance and prevent diet-induced obesity. The data from this study provide evidence to indicate that the peptide may increase glucose utilization, modulate the methionine-folate cycle and induce AMPK activation. These cellular activities make it clear that MOTS-c could work as a regulator for metabolism and it might participate in many metabolic processes (like glucose and lipid metabolic process). As a result, the murine models given the peptide developed to be not just leaner and more dynamic than their sister experiments, but also showed proof indicating that the peptide could halt fat cell generalization through AMPK and boost glucose entry.

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