Mitochondrial-Derived Peptides
Mitochondrial-derived peptides are discussed in relation to short coding regions associated with mitochondrial DNA. MOTS-c is a specific reference peptide within that research area. A mitochondrial association does not make every material used in metabolism research a mitochondrial-derived peptide.
Discovery and cellular context
Lee and colleagues described MOTS-c as a 16-residue peptide associated with a short open reading frame in the mitochondrial 12S rRNA region. Their work examined metabolic pathways and mouse outcomes. [1]
Kim and colleagues later investigated stress-related movement of MOTS-c to the nucleus and gene-expression responses. Those localisation and pathway findings do not establish a single settled direct receptor mechanism. [2]
Keep the experiment type visible
| Research question | Evidence type |
|---|---|
| Where is the reference sequence associated? | Genomic and molecular characterisation |
| What changes during cellular stress? | Cell localisation and pathway experiments |
| What follows an experimental intervention? | The particular animal or cell model tested |
| What changes during human exercise? | Endogenous peptide measurement, unless administration was actually studied |
Reynolds and colleagues combined mouse interventions with human exercise-related measurements. The human component measured endogenous MOTS-c; it was not a human administration trial. [3]
Ramanjaneya and colleagues reported no change in circulating MOTS-c after their moderate exercise-training programme. Different exercise and measurement designs should not be compressed into a universal “exercise increases MOTS-c” rule. [4]
Newer mechanistic work remains model-specific
Gudiksen and colleagues used transgenic mouse models to examine mitochondrial bioenergetic responses and included a human arterial–venous measurement. The authors' interpretation of the circulating peptide's source remains an interpretation of that design. [5]
For the material identity and preparation questions, use the MOTS-c profile. For the chemical distinction from a dinucleotide and a redox tripeptide, see NAD+, MOTS-c and glutathione. Neither a pathway association nor an endogenous measurement verifies the identity or performance of a purchased container.
Explore the related evidence
| Resource | Why open it |
|---|---|
| Longevity and Mitochondrial Research Compounds | Browse the ageing, mitochondrial and redox research category. |
| MOTS-c 10 mg | Open the product record for its nominal presentation and current purchasing information. |
| What Are Peptides? | Start with peptide bonds, residues and sequence. |
| NAD+ Metabolism and Its Precursors | Distinguish NAD pool size, redox state and metabolic flux. |
| Guides & Resources | Choose another scientific, analytical or procurement guide. |
Sources and scope
- Lee et al. (2015). MOTS-c and metabolic homeostasis. Cell Metabolism.12S-rRNA-region sORF, 16-amino-acid reference; folate/purine and AMPK pathway findings; mouse results, not human administration. Access: Original article abstract opened through the official Europe PMC core record; not merely a search snippet
- Kim et al. (2018). MOTS-c nuclear translocation under metabolic stress. Cell Metabolism.AMPK-dependent stress localisation and gene-expression response; no claim of a settled direct receptor. Access: Original article abstract opened through the official Europe PMC core record; not merely a search snippet
- Reynolds et al. (2021). MOTS-c, exercise and muscle homeostasis. Nature Communications.Mouse administration and human endogenous measurement kept separate; no human administration inferred. Access: Original abstract plus complete publisher article and Europe PMC full text
- Ramanjaneya et al. (2019). Lipids, insulin and circulating MOTS-c. Clinical Endocrinology.Exercise-training null circulating finding in controls and women with PCOS; not equivalent to every acute-exercise endpoint. Access: Original article abstract opened through the official Europe PMC core record; not merely a search snippet
- Gudiksen et al. (2026). MOTS-c and muscle mitochondrial bioenergetics. Free Radical Biology and Medicine.AMPK/PGC-1α dependence and functional mitochondrial changes; human source-of-circulating-peptide inference remains the authors’ interpretation. Access: Original article abstract opened through the official Europe PMC core record; not merely a search snippet