MOTS-c 10mg

MOTS-c is a fascinating mitochondrial-derived peptide that has garnered significant attention in the scientific community for its potential roles in metabolic regulation and cellular function. This 16-amino acid peptide is encoded within the mitochondrial 12S rRNA gene and has been shown to act as a mitochondrial signal that can influence various physiological processes17.

Discovery and Structure

MOTS-c was first identified through an in silico search for potential small open reading frames within the human 12S rRNA. The peptide consists of 16 amino acids and is highly conserved across species, particularly in its first 11 residues7. This conservation suggests that MOTS-c may play a crucial role in cellular function that has been maintained throughout evolution.

Metabolic Regulation

Research has indicated that MOTS-c may be a key player in metabolic homeostasis. Studies have shown that MOTS-c can influence several metabolic pathways:

• Glucose Metabolism: MOTS-c has been observed to enhance insulin sensitivity in skeletal muscle and improve glucose utilization2.

• Lipid Metabolism: Treatment with MOTS-c has been associated with reduced fat accumulation in diet-induced obese animal models4.

• Mitochondrial Function: As a mitochondrial-derived peptide, MOTS-c appears to regulate mitochondrial function and cellular energy metabolism1.

Cellular Signaling

MOTS-c has been found to interact with various cellular signaling pathways:

• AMPK Activation: Research suggests that MOTS-c can activate the AMP-activated protein kinase (AMPK) pathway, which is crucial for energy homeostasis7.

• Folate-Methionine Cycle: MOTS-c has been shown to target the folate-methionine cycle and influence de novo purine biosynthesis7.

• Gene Expression: Studies have demonstrated that MOTS-c can regulate gene expression, particularly genes associated with cellular metabolism and inflammation7.

Potential Areas of Interest

Scientific research has explored the potential roles of MOTS-c in various physiological processes:

1. Muscle Function: MOTS-c has been studied for its potential to reduce myostatin signaling and muscle atrophy1.

2. Exercise Performance: Research has investigated MOTS-c as an exercise-induced regulator of physical performance and muscle homeostasis4.

3. Aging: Some studies have explored the potential role of MOTS-c in age-related processes and longevity2.

4. Bone Metabolism: Emerging research has begun to investigate the potential involvement of MOTS-c in bone metabolism and osteoblast function8.

5. Cardiovascular Function: Some studies have examined the potential effects of MOTS-c on cardiovascular health2.

6. Inflammation: Research has explored the potential anti-inflammatory properties of MOTS-c5.

Molecular Mechanisms

At the molecular level, MOTS-c has been observed to:

• Translocate to the nucleus, suggesting a direct role in gene regulation4.

• Influence protein homeostasis (proteostasis) processes4.

• Affect heat-shock responses, including regulation of heat-shock proteins4.

• Modulate oxidative stress responses4.

Conclusion

MOTS-c represents an exciting area of scientific research in the field of cellular metabolism and mitochondrial biology. As a mitochondrial-derived peptide, it offers unique insights into the complex communication between mitochondria and the rest of the cell. Ongoing research continues to uncover the multifaceted roles of MOTS-c in cellular function and metabolism.

It’s important to note that while MOTS-c shows promise in various areas of research, much work remains to be done to fully understand its functions and potential applications. As with all peptides, MOTS-c should only be used for legitimate scientific research purposes by qualified professionals in appropriate laboratory settings.

References:1 https://journals.physiology.org/doi/full/10.1152/ajpendo.00275.20202 https://pmc.ncbi.nlm.nih.gov/articles/PMC9905433/4 https://www.nature.com/articles/s41467-020-20790-05 https://pmc.ncbi.nlm.nih.gov/articles/PMC9570330/7 https://pmc.ncbi.nlm.nih.gov/articles/PMC4350682/8 https://www.frontiersin.org/journals/physiology/articles/10.3389/fphys.2023.1149120/full