MOTS-c (20mg – 100mg)

MOTS-c

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Peptide Partners Manufacturer Id: WF03

Batch Id: MC202512

Research Studies

(for educational purposes only)

Study 1: MOTS-c promotes muscle differentiation in vitro

Authors: Sandra García-Benlloch, Francisco Revert-Ros, Jose Rafael Blesa, Rafael Alis

Source: https://www.sciencedirect.com/science/article/pii/S0196978122001061

Scientific Findings

The study investigated the effect of MOTS-c on myogenesis in human (LHCN-M2) and murine (C2C12) myoblasts. The findings indicate that wild-type MOTS-c peptide enhances myotube formation, whereas a variant with a substitution at tyrosine 8 (Y8F) does not. Furthermore, wild-type MOTS-c, but not the Y8F peptide, was shown to counteract the interleukin-6 (IL-6)-induced reduction of nuclear myogenin. The proposed mechanism is that MOTS-c interacts with the STAT3 transcription factor via its putative SH2 binding motif (YIFY region), thereby reducing STAT3’s transcriptional activity and promoting myotube formation.

Plain English Interpretation

This research explored how a naturally occurring peptide called MOTS-c affects muscle cell development. Using muscle cells from both humans and mice, the scientists found that MOTS-c helps these cells to mature and form muscle fibers. They also discovered that a specific part of the MOTS-c molecule is crucial for this process. When this part was altered, the beneficial effect was lost. The study suggests that MOTS-c works by influencing a key protein (STAT3) involved in cell growth, which in turn enhances the formation of new muscle tissue. This could have implications for understanding and potentially treating muscle-related conditions.

Study 2: The mitochondrial genome-encoded peptide MOTS-c interacts with Bcl-2 to alleviate nonalcoholic steatohepatitis progression

Authors: Huanyu Lu, Linni Fan, Wenli Zhang, Guo Chen, An Xiang, Li Wang, Zifan Lu, Yue Zhai

Source: https://www.sciencedirect.com/science/article/pii/S2211124723015991

Scientific Findings

This study elucidates the molecular mechanism by which MOTS-c ameliorates nonalcoholic steatohepatitis (NASH). The research demonstrates that MOTS-c directly interacts with the BH3 domain of the antiapoptotic protein B-cell lymphoma-2 (Bcl-2). This interaction enhances Bcl-2 protein stability by suppressing its ubiquitination. In vitro experiments using a Bcl-2 inhibitor and adeno-associated virus (AAV)-mediated Bcl-2 knockdown confirmed that the protective effects of MOTS-c against NASH-induced mitochondrial dysfunction, inflammation, and fibrosis are dependent on Bcl-2 function. Metabolomic analysis further revealed that MOTS-c reverses NASH-induced mitochondrial metabolic deficiencies.

Plain English Interpretation

This research uncovers how a natural peptide called MOTS-c can help protect the liver from a serious condition called nonalcoholic steatohepatitis (NASH), which is a severe form of fatty liver disease. The scientists discovered that MOTS-c works by interacting with a protein called Bcl-2, which is known to prevent cell death. By binding to Bcl-2, MOTS-c makes it more stable and prevents it from being broken down by the cell. This action helps to restore normal function to the mitochondria, the powerhouses of the cells, and reduces the inflammation and scarring associated with NASH. In essence, MOTS-c acts as a guardian for liver cells, protecting them from the damage caused by this disease.

Study 3: MOTS-c modulates skeletal muscle function by directly binding and activating CK2

Authors: Hiroshi Kumagai, Su-Jeong Kim, Brendan Miller, et al.

Source: https://www.cell.com/iscience/fulltext/S2589-0042(24)02437-4

Scientific Findings

This study identifies protein kinase CK2 as a direct and functional target of MOTS-c. In vitro, cell-free systems demonstrated that MOTS-c directly binds to and activates CK2. This interaction is crucial for the metabolic effects of MOTS-c. The study also investigated a naturally occurring variant, K14Q MOTS-c, which showed reduced binding to CK2 and a concomitant lack of activation. This provides a molecular basis for the observed physiological effects, linking the in vitro findings to in vivo and clinical observations.

Plain English Interpretation

This research discovered that a small protein called MOTS-c works by directly switching on an enzyme called CK2. Using experiments in a test tube, the scientists showed that MOTS-c binds to CK2 and activates it. This is like a key fitting into a lock to turn on a machine. They also found that a common variation of the MOTS-c ‘key’ doesn’t fit the CK2 ‘lock’ as well, and so it can’t turn on the machine. This discovery helps to explain how MOTS-c affects our bodies at a molecular level, and why some people might be more prone to certain health issues.