While inhibiting lipogenesis, AOD9604 may potentially stimulate and improve lipolysis (fat disintegration or breakdown). The peptide does not appear to affect IGF-1 or insulin levels and may not have any association in diabetes or glucose intolerance.^[1] Researchers comment that “chronic [exposure to] AOD9604 showed no adverse effect on insulin sensitivity of the animals, as [seen] with euglycemic clamp techniques.” There is also no data to suggest that the peptide leads to the formation of antibodies. ^[2]

AOD9604 and General Research

The peptide appears to stimulate the pituitary gland by acting directly on it. This appears to be the same mechanism of action as GH, as it mimics the actions of the natural growth hormone on body fat metabolism. AOD9604 has been suggested by researchers to accelerate fat-burning processes and restore anabolism by acting on the pituitary gland. The compound has not been implicated in appetite alteration or blood sugar levels.

AOD9604 research in mice suggested that the peptide may impact more than the beta-3-adrenergic receptors on white fat.^[4] The scientists suggested that “both hGH and AOD9604 are capable of increasing the repressed levels of beta(3)-AR RNA in obese mice to levels comparable with those in lean mice.” Initially, it was assumed that AOD9604 may increase the metabolic rate in fat cells by binding to these receptors and switching them from storage to user mode. However, even mice lacking these receptors appeared to have reduced fat cell accumulation after being exposed to AOD9604.

Because the beta-3-adrenergic receptor appears to influence fat loss through AOD9604, another mechanism may potentially be at work. The compound may indirectly stimulate apoptosis in white fat cells, according to this theory.

Finally, and tangentially, the peptide appears to have a potential impact in models of osteoarthritis due to alterations observed in the gross clinical exam and microscopic structure of cartilage in an arthritic joint model.

Disclaimer: The products mentioned are not intended for human or animal consumption. Research chemicals are intended solely for laboratory experimentation and/or in-vitro testing.  Bodily introduction of any sort is strictly prohibited by law.  All purchases are limited to licensed researchers and/or qualified professionals. All information shared in this article is for educational purposes only.

References

1. Ng FM, Sun J, Sharma L, Libinaka R, Jiang WJ, Gianello R. Metabolic studies of a synthetic lipolytic domain (AOD9604) of human growth hormone. Horm Res. 2000;53(6):274-8. doi: 10.1159/000053183. PMID: 11146367.
2. Stier, Heike, Evert Vos, and David Kenley. “Safety and tolerability of the hexadecapeptide AOD9604 in humans.” Journal of Endocrinology and Metabolism 3.1-2 (2013): 7-15.
3. Zieba R. Otyłość: przeglad aktualnie stosowanych leków i nowych zwiazków poddawanych ocenie klinicznej [Obesity: a review of currently used antiobesity drugs and new compounds in clinical development]. Postepy Hig Med Dosw (Online). 2007 Oct 19;61:612-26. Polish. PMID: 17971763.
4. Heffernan M, Summers RJ, Thorburn A, Ogru E, Gianello R, Jiang WJ, Ng FM. The effects of human GH and its lipolytic fragment (AOD9604) on lipid metabolism following chronic treatment in obese mice and beta(3)-AR knock-out mice. Endocrinology. 2001 Dec;142(12):5182-9. doi: 10.1210/endo.142.12.8522. PMID: 11713213.
5. Jensen MD. Potential role of new therapies in modifying cardiovascular risk in overweight patients with metabolic risk factors. Obesity (Silver Spring). 2006 Jun;14 Suppl 3:143S-149S. doi: 10.1038/oby.2006.294. PMID: 16931496.
6. Kwon DR, Park GY. Effect of Intra-articular Injection of AOD9604 with or without Hyaluronic Acid in Rabbit Osteoarthritis Model. Ann Clin Lab Sci. 2015 Summer;45(4):426-32. PMID: 26275694.

Palmitoyl Tripeptide-1, aka Pal-GHK or Palmitoyl Oligopeptide, is a hybrid peptide comprising a peptide and a fatty acid end. The peptide end is the GHK-end (Glycine, histidine, and lysine). Meanwhile, the fatty acid end is the Pal-end (Palmitoyl). Pal-GHK is a fibroblast stimulant and a small fraction of the elastin protein. It may potentially enhance the synthesis of elastin, collagen, and other extracellular matrix protein (ECM) in the connective tissues, bone, and skin.^[1]

The peptide (GHK) component of the Palmitoyl Tripeptide-1 peptide may subject fibroblasts into perceiving that elastin—one of the most abundant proteins in the ECM—is damaged. As a result, the organism may rapidly produce and multiply fibroblasts to replenish and regenerate the lost elastin. Palmitoyl Tripeptide-1 may also mitigate or prevent cell aging and re-energize fibroblasts in the ECM.

The fatty acid (Palmitoyl) end of Pal-GHK appears to serve as an intermediary, a transport complex that may perform at a higher level of impact when the GHK-end is attached to the Pal-end, resulting in potentially enhanced skin and cell penetration.

Palmitoyl Tripeptide-1 may stimulate genes that might alter and reset cells. This may potentially be possible by attaching Palmitoyl to the peptide sequence, GHK, which may make it overly effective for DNA repair genes and increases expression of the 14 genes that modulate antioxidant production.^[2] The researchers also note that “The Broad Institute’s Connectivity Map indicated that GHK induces a 50% or greater change of expression in 31.2% of … genes.” After the genetic changes, reduced action of cell aging and removing radicals and toxic agents that induce the development of age-related diseases might be attained.

Palmitoyl Tripeptide-1 may potentially aid in rapid tissue repair by enhancing the production of new blood vessels (angiogenesis) at injury sites. The peptide might also repair nerves and induces the growth of new nerves. Furthermore, Pal-GHK may better the actions of genes responsible for wound healing; it may activate DNA repair genes and suppresses genes that may aid cancer growth.

Scientific research has suggested that Palmitoyl Tripeptide-1 may protect the ECM by preventing cell death in certain cases. The peptide may potentiate this action by enhancing elastin and collagen production.

Palmitoyl Tripeptide-1 may potentially replenish the skin’s extracellular matrix, inducing wrinkle reduction and alleviation. At the same time, it may prevent collagen degradation following exposure to Ultraviolet A (UVA) rays.

Disclaimer: The products mentioned are not intended for human or animal consumption. Research chemicals are intended solely for laboratory experimentation and/or in-vitro testing.  Bodily introduction of any sort is strictly prohibited by law.  All purchases are limited to licensed researchers and/or qualified professionals. All information shared in this article is for educational purposes only.

References

1. Goldsberry, S. & Garcines, L. Anti-aging cosmeceutical composition. (2013).
2. Pickart, L., Vasquez-Soltero, J. M. & Margolina, A. GHK-Cu may Prevent Oxidative Stress in Skin by Regulating Copper and Modifying Expression of Numerous Antioxidant Genes. Cosmetics 2, 236–247 (2015). doi: 10.3390/cosmetics2030236
3. Trookman, N. S., Rizer, R. L., Ford, R., Mehta, R. & Gotz, V. Clinical assessment of a combination lip treatment to restore moisturization and fullness. J. Clin. Aesthetic Dermatol. 2, 44–48 (2009).
4. Dupont, E. et al. Clinical efficacy of a serum integrating multiple cosmetic ingredients in the management of erythema of the face in aging skin. J. Cosmet. Dermatol. 11, 207–212 (2012).
5. Bradley, E. J., Griffiths, C. E. M., Sherratt, M. J., Bell, M. & Watson, R. E. B. Over-the-counter anti-ageing agents and their ability to protect and repair photoaged skin. Maturitas 80, 265–272 (2015).

DSIP may potentially lower oxidative stress and restore normal myocardial contractility. Furthermore, the peptide may potentially produce mitigatory action against depressive disorders and cancer cell proliferation. DSIP has also been researched for its potential to inhibit Somatostatin secretion, modify corticotropin levels, actions on blood pressure, stress hormone secretion and pain perception.

DSIP and Sleep Pattern Regulation

Some research suggests DSIP promotes slow-wave sleep while suppressing paradoxical sleep. It may also cause arousal in the first hour of sleep and sedation in the second. Research findings suggest that DSIP might normalize sleep and modulate sleep cycle dysfunctions. Sleep research involving DSIP was conducted in research models of chronic insomnia, and DSIP reportedly improved sleep to the same level as normal controls. This study supports previous findings that DSIP may reduce sleep latency and promotes sleep structure in chronic insomnia.^[4] The scientists note that “The [exposure] substantially improved night sleep with the first and additionally with repeated [introduction].”

According to the research, DSIP may potentially increase sleep time by 59% compared to a placebo, and delay sleep onset.^[5] These findings, however, contradict the EEG analysis of the research models under examining, which revealed no sedation. However, this may potentially be due to current testing patterns, as many EEG measures of sedation are based on pharmacologic sedation rather than natural sedation.

DSIP and Metabolism

DSIP research in rat models suggests that the peptide may limit stress-induced metabolic disturbances that cause the mitochondria to switch from oxygen-dependent to oxygen-independent respiration. The latter may produce dangerous metabolic byproducts. DSIP may be employed in research related to conditions such as heart attack and stroke due to its potential to maintain oxidative phosphorylation even in hypoxic conditions.^[8] DSIP may mitigate metabolic damage caused by oxygen deprivation by preserving normal mitochondrial function, thereby protecting tissues until blood flow is restored. DSIP may potentially reduce free radical production by maintaining normal mitochondrial functions.

DSIP research further suggests that the peptide may inhibit somatostatin secretion, contributing to skeletal muscle hypertrophy and hyperplasia.
According to Delta Sleep Inducing Peptide research, the peptide may influence blood pressure, thermogenesis, the lymphokine system, and heart rate.

Disclaimer: The products mentioned are not intended for human or animal consumption. Research chemicals are intended solely for laboratory experimentation and/or in-vitro testing.  Bodily introduction of any sort is strictly prohibited by law.  All purchases are limited to licensed researchers and/or qualified professionals. All information shared in this article is for educational purposes only.

References

1. Popovich IG, Voitenkov BO, Anisimov VN, Ivanov VT, Mikhaleva II, Zabezhinski MA, Alimova IN, Baturin DA, Zavarzina NY, Rosenfeld SV, Semenchenko AV, Yashin AI. Effect of delta-sleep inducing peptide-containing preparation Deltaran on biomarkers of aging, life span and spontaneous tumor incidence in female SHR mice. Mech Ageing Dev. 2003 Jun;124(6):721-31. doi: 10.1016/s0047-6374(03)00082-4. PMID: 12782416.
2. A. B. Sinyukhin, G. P. Timoshinov, V. A. Kornilov, and P. D. Shabanov, “P.7.a.006 Delta sleep-inducing peptide analogue corrects the CNS functional state of children treated with antiblastomic therapy,” Eur. Neuropsychopharmacol., vol. 19, pp. S681–S682, Sep. 2009.
3. E. V. Koplik et al., “Delta sleep-inducing peptide and Deltaran: potential approaches to antistress protection,” Neurosci. Behav. Physiol., vol. 38, no. 9, pp. 953–957, Nov. 2008
4. Schneider-Helmert D. Effects of delta-sleep-inducing peptide on 24-hour sleep-wake behaviour in severe chronic insomnia. Eur Neurol. 1987;27(2):120-9. doi: 10.1159/000116143. PMID: 3622582.
5. Schneider-Helmert D, Gnirss F, Monnier M, Schenker J, Schoenenberger GA. Acute and delayed effects of DSIP (delta sleep-inducing peptide) on human sleep behavior. Int J Clin Pharmacol Ther Toxicol. 1981 Aug;19(8):341-5. PMID: 6895513.
6. Larbig W, Gerber WD, Kluck M, Schoenenberger GA. Therapeutic effects of delta-sleep-inducing peptide (DSIP) in patients with chronic, pronounced pain episodes. A clinical pilot study. Eur Neurol. 1984;23(5):372-85. doi: 10.1159/000115716. PMID: 6548970.
7. Nakamura A, Nakashima M, Sugao T, Kanemoto H, Fukumura Y, Shiomi H. Potent antinociceptive effect of centrally administered delta-sleep-inducing peptide (DSIP). Eur J Pharmacol. 1988 Oct 18;155(3):247-53. doi: 10.1016/0014-2999(88)90510-9. PMID: 2853064.
8. Khvatova EM, Samartzev VN, Zagoskin PP, Prudchenko IA, Mikhaleva II. Delta sleep inducing peptide (DSIP): effect on respiration activity in rat brain mitochondria and stress protective potency under experimental hypoxia. Peptides. 2003 Feb;24(2):307-11. doi: 10.1016/s0196-9781(03)00040-8. PMID: 12668217.

The Difference Between CJC-1295 and CJC-1295 DAC

These two peptides seem similar but are not identical. CJC-1295 is a modified equivalent of the first 29 amino acids of GHRH, chemically identical to other growth hormone analogs like Sermorelin. Meanwhile, CJC-1295 DAC is created by adding the Drug Affinity Complex DAC, to CJC-1295.
DAC is added to CJC-1295 using the lysine linker. The DAC appears to protect CJC-1295 while it circulates in the bloodstream. DAC may ensure the increased half-life of CJC-1295 by allowing the peptide to bind to blood proteins such as Albumin.

The Functions of CJC-1295

CJC-1295 NO DAC appears to function to enhance protein synthesis. The peptide may achieve this by inhibiting the natural process of cellular degradation, thereby increasing protein synthesis. The peptide may also potentially improve lipolytic processes by increasing the rate of synthesis and disintegration. By increasing the lipolytic process, CJC-1295 NO DAC peptide may influence the increased efficiency of fat cell dissolution.

CJC-1295 and Hemorrhagic Shock and GHRH 1-29 Interaction

CJC-1295 NO DAC has been hypothesized to stimulate and improve nerve reflexes within the brain and may modulate blood flow, thereby preventing acute organ failure following hemorrhagic shock. On the other hand, hemorrhagic shock may be an acute condition followed by reduced tissue perfusion and insufficient nutrient and oxygen delivery necessary for cellular functions. Hemorrhagic shock is classified as cardiogenic, hypovolemic, septic, and neurogenic.

CJC-1295 NO DAC and Growth

The peptide is considered a potential enhancing agent for maintaining the normal rate of growth hormone release.^[1] By doing this, the peptide may exert action in cases of abnormal growth in varieties of animal species. Maintaining the normal growth hormone level may be critical to releasing downstream hormones like insulin-like growth factor-2 (IGF-1). CJC-1295 appears to significantly enhance the synthesis of IGF-1. GH, CJC-1295, and IGF-1 collectively influence the pro-inflammatory mechanisms when activated.

In mouse models of GHRH knockout, the exposure to CJC-1295 appeared to reduce growth deficits. Furthermore, CJC-1295 appeared to steadily enhance the total body weight and length.^[2] This study reports that “These findings [indicate that exposure to] CJC-1295 is able to maintain normal body composition and growth in GHRHKO mice.” The peptide also assessed the abnormal response to GRF following obesity.

CJC-1295 and Infertility

Scientists suggest GRF analogs, CJC-1295, might induce ovulation in infertile female species. Data findings imply that ovulation may be solely dependent on IGF-1 and may be regulated by the release and cycling of growth hormones. However, research in mouse models of superovulation suggest that the levels of IGF-1 and growth hormone may increase with ovulation.^[3] These results posit that the exposure to a GH secretagogue like CJC-1295 may induce ovulation. Scientific research also suggests that CJC-1295 NO DAC and other GHRH analogs may impact male infertility by inducing sperm production. However, note that this hypothesis is still undergoing testing.^[4] The researchers report that “these results led to the identification of CJC-1295 as a stable and active hGRF1-29 analogwith an extended plasma half-life.”

Disclaimer: The products mentioned are not intended for human or animal consumption. Research chemicals are intended solely for laboratory experimentation and/or in-vitro testing.  Bodily introduction of any sort is strictly prohibited by law.  All purchases are limited to licensed researchers and/or qualified professionals. All information shared in this article is for educational purposes only.

References

1. Ionescu M, Frohman LA. Pulsatile secretion of growth hormone (GH) persists during continuous stimulation by CJC-1295, a long-acting GH-releasing hormone analog. J Clin Endocrinol Metab. 2006 Dec;91(12):4792-7. doi: 10.1210/jc.2006-1702. Epub 2006 Oct 3. PMID: 17018654.
2. Alba M, Fintini D, Sagazio A, Lawrence B, Castaigne JP, Frohman LA, Salvatori R. Once-daily administration of CJC-1295, a long-acting growth hormone-releasing hormone (GHRH) analog, normalizes growth in the GHRH knockout mouse. Am J Physiol Endocrinol Metab. 2006 Dec;291(6):E1290-4. doi: 10.1152/ajpendo.00201.2006. Epub 2006 Jul 5. PMID: 16822960.
3. Volpe A, Coukos G, Barreca A, Giordano G, Artini PG, Genazzani AR. Clinical use of growth hormone-releasing factor for induction of superovulation. Hum Reprod. 1991 Oct;6(9):1228-32. doi: 10.1093/oxfordjournals.humrep.a137517. PMID: 1752922.
4. Jetté, Lucie, et al. “hGRF1-29-Albumin Bioconjugates Activate the GRF Receptor on the Anterior Pituitary in Rats: Identification of CJC-1295 as a Long Lasting GRF Analog.” (2005)
5. Teichman SL, Neale A, Lawrence B, Gagnon C, Castaigne JP, Frohman LA. Prolonged stimulation of growth hormone (GH) and insulin-like growth factor I secretion by CJC-1295, a long-acting analog of GH-releasing hormone, in healthy adults. J Clin Endocrinol Metab. 2006 Mar;91(3):799-805. doi: 10.1210/jc.2005-1536. Epub 2005 Dec 13. PMID: 16352683.

SNAP-8 peptide, also known as Acetyl Glutamyl Heptapeptide-1, is a hexapeptide Argireline elongation. SNAP-8, like other hexapeptide-based peptides, may exert an anti-wrinkling action on the extracellular matrix of the skin (ECM).^[1] The peptide may potentially prevent the disruption of the lipid matrix’s packing. SNAP-8 peptide is unique, as it appears to target the wrinkling mechanism in a novel and distinct manner.^[2]

SNAP-8 Peptide Research

Muscle contraction occurs following the release of neurotransmitters from vesicles. The SNARE complex is considered to be required for muscle contraction because it appears to act as a cellular hook, capturing vesicles and fusing them with the membrane to allow neurotransmitters to be released. Wrinkling occurs when muscles contract repeatedly. SNAP-8 peptide destabilizes the SNARE complex’s functions, causing vesicles to stop producing neurotransmitters efficiently and reducing the appearance of lines and wrinkles.

SNAP-8 peptide may also inhibit catecholamine release, resulting in the reduction of existing wrinkling. Catecholamine inhibition may also affect the stabilization process in muscle contraction regulation by activating the Ca2+ ion. SNAP-8 peptide appears to induce endogenous collagen production and release which may strengthen the skin structure.^[3] SNAP-8 peptide may act as a muscle contraction inhibitor, allowing muscles to achieve high homeostasis levels.^[4] SNAP-8 peptide may potentially reduce the severity of wrinkles, in some studies citing reduction up to 63.13%. The peptide’s potency appears to be 30% higher than its parent peptide, Argireline.

Glutamate is a neurotransmitter that is considered to function to excite neurons. Study findings indicate that combining SNAP-8 with Leuphasyl may have a stronger inhibitory effect on glutamate than single peptides. Meanwhile, glutamate appears to stimulate muscle contraction, resulting in wrinkling. As a result of inhibiting glutamate release, wrinkles and fine lines may potentially be avoided.^[5] Researchers conclude that the peptide works by “preventing neuromuscular signal propagation, thereby eliminating wrinkles caused by over-stimulated neurons.” Researchers performed a skin topography analysis to determine the efficacy of a 10% concentration of SNAP-8 solution, obtaining silicon imprints from the eye region. Data concluded that wrinkle depths decreased to different degrees following the study.

A similar experiment was performed with a 10% Argireline solution. The results suggested that the control group exhibited a -2.99% wrinkle reduction, Argireline exhibited a -27.05% reduction, and SNAP-8 peptide reported a -34.98% wrinkle reduction. Following these comparisons, 10% of SNAP-8 solutions appeared to have achieved a maximum wrinkle reduction of -63.13%.^[6] Indeed, the scientists conclude that “According to the data available in the manufacturer’s website, maximum wrinkle reduction strives for−62%, with the mean value at the level of −35%.”

Disclaimer: The products mentioned are not intended for human or animal consumption. Research chemicals are intended solely for laboratory experimentation and/or in-vitro testing.  Bodily introduction of any sort is strictly prohibited by law.  All purchases are limited to licensed researchers and/or qualified professionals. All information shared in this article is for educational purposes only.

References

1. Ji, Moongi, et al. “Method development for acetyl octapeptide-3 analysis by liquid chromatography-tandem mass spectrometry.” Journal of Analytical Science and Technology 11 (2020): 1-7.
2. Backardzhiev, Ilko, and Dona Filcheva. “Peptides in dermatocosmetics.” Journal of Varna Medical College 4.1 (2022): 45-49.
3. Avcil, Muhammet, et al. “Efficacy of bioactive peptides loaded on hyaluronic acid microneedle patches: A monocentric clinical study.” Journal of Cosmetic Dermatology 19.2 (2020): 328-337.
4. Raposio, Edoardo, et al. “EVALUATION OF EFFECTIVENESS OF VIPER SERUM FOR USE AS FACIAL ANTI-AGING.” (2009).
5. Gutierrez, Luis M., et al. “A peptide that mimics the C-terminal sequence of SNAP-25 inhibits secretory vesicle docking in chromaffin cells.” Journal of Biological Chemistry 272.5 (1997): 2634-2639.
6. Errante F, Ledwoń P, Latajka R, Rovero P, Papini AM. Cosmeceutical Peptides in the Framework of Sustainable Wellness Economy. Front Chem. 2020;8:572923. Published 2020 Oct 30. doi:10.3389/fchem.2020.572923.

Research and Functions Of MOTS-c Peptide

MOTS-c peptide has been suggested by researchers to improve brown fat function and decrease fat tissue accumulation in murine models. Furthermore, MOTS-c peptide may potentially prevent adipose tissue dysfunction and inflammation after insulin resistance. MOTS-c peptide has been hypothesized to influence fat metabolism by activating the AMPK pathway.^[1] Yet, the researchers note that “MOTS-c activated AMPK pathway to improve energy dissipation and insulin sensitivity.” The AMPK pathway is a cellular pathway activated when cellular energy levels are low, inducing cells to take up glucose and fatty acids for metabolism. MOTS-c peptide has been suggested to activate the AMPK by targeting the methionine-folate cycle, potentially increasing AICAR levels.

According to research, the peptide may be able to travel from the mitochondria to the nucleus, influencing nuclear gene expression. MOTS-c may potentially modulate cellular genes involved in glucose restriction and antioxidant responses during metabolic stress.^[2] MOTS-c peptide appears to be an active modulator of monoacylglycerol, sphingolipid, and dicarboxylate metabolism in research models of obesity. MOTS-c appears to reduce fat accumulation by inhibiting these pathways and increasing beta-oxidation.^[3] MOTS-c research into fat deposition and insulin resistance is gaining traction, as scientists believe the peptide may offer a novel approach to addressing the pathophysiology of obesity and diabetes.

Fat oxidation is considered to be reduced by dysregulation of fat metabolism in the mitochondria. High levels of fat circulation may occur, increasing insulin levels to combat and clear lipids from the bloodstream. As a result of high insulin levels, there may be increased fat deposition and a homeostatic change. Through examinations on the impacts of the peptide, researchers suggest that these conditions may reverse.

MOTS-c peptide has also been hypothesized to function to reverse age-dependent insulin resistance in muscles, potentially improving glucose uptake. MOTS-c peptide may accomplish this by increasing glucose transporter expression and promoting the response of skeletal muscles to AMPK activation.^[4] It is important to note that activating the AMPK pathway in this context may be independent of the insulin pathway, providing another method of increasing glucose uptake of muscles in the event of insulin inactivity or insufficiency.

MOTS-c may also influence Type 1 collagen synthesis, controlled by osteoblasts in the bone. MOTS-c has been suggested to act in this manner by modulating the TGF-beta/SMAD pathway, which regulates osteoblast health and survival. The potential of the peptide to modulate these pathways may promote osteoblast survival, improving type 1 collagen synthesis and bone strengthening and integrity.^[6]

The peptide appears to regulate stem cell differentiation of the bone marrow and osteogenesis (new bone formation) by modulating the TGF-beta/SMAD pathway. In addition to protecting and ensuring the survival of osteoblasts, the peptide may potentially promote their development from stem cells.

Research suggests that low MOTS-c levels may be a precursor to endothelial cell dysfunction.^[7] Endothelial cells line the inner walls of blood vessels, regulating blood pressure, forming plaques, and promoting blood clotting. MOTS-c does not appear to directly increase blood vessel responsiveness but may potentially indirectly impact endothelial cells, activating other responsive molecules such as acetylcholine. MOTS-c peptide has been suggested to improve blood vessel function at the microvascular, endothelial, and epicardial levels. Research further suggests that MOTS-c may play an active role in protecting heart cells against inflammation, stress, and reperfusion injury.^[8]

Disclaimer: The products mentioned are not intended for human or animal consumption. Research chemicals are intended solely for laboratory experimentation and/or in-vitro testing.  Bodily introduction of any sort is strictly prohibited by law.  All purchases are limited to licensed researchers and/or qualified professionals. All information shared in this article is for educational purposes only.

References

1. Lu H, Wei M, Zhai Y, et al. MOTS-c peptide regulates adipose homeostasis to prevent ovariectomy-induced metabolic dysfunction. J Mol Med (Berl). 2019;97(4):473-485. doi:10.1007/s00109-018-01738-w.
2. Kim KH, Son JM, Benayoun BA, Lee C. The Mitochondrial-Encoded Peptide MOTS-c Translocates to the Nucleus to Regulate Nuclear Gene Expression in Response to Metabolic Stress. Cell Metab. 2018;28(3):516-524.e7. doi:10.1016/j.cmet.2018.06.008.
3. Kim SJ, Miller B, Mehta HH, et al. The mitochondrial-derived peptide MOTS-c is a regulator of plasma metabolites and enhances insulin sensitivity. Physiol Rep. 2019;7(13):e14171. doi:10.14814/phy2.14171.
4. Lee C, Kim KH, Cohen P. MOTS-c: A novel mitochondrial-derived peptide regulating muscle and fat metabolism. Free Radic Biol Med. 2016;100:182-187. doi:10.1016/j.freeradbiomed.2016.05.015.
5. Fuku N, Pareja-Galeano H, Zempo H, et al. The mitochondrial-derived peptide MOTS-c: a player in exceptional longevity?. Aging Cell. 2015;14(6):921-923. doi:10.1111/acel.12389.
6. Crescenzo R, Bianco F, Mazzoli A, Giacco A, Liverini G, Iossa S. A possible link between hepatic mitochondrial dysfunction and diet-induced insulin resistance. Eur J Nutr. 2016;55(1):1-6. doi:10.1007/s00394-015-1073-0.
7. Qin Q, Delrio S, Wan J, et al. Downregulation of circulating MOTS-c levels in patients with coronary endothelial dysfunction. Int J Cardiol. 2018;254:23-27. doi:10.1016/j.ijcard.2017.12.001.
8. Yang Y, Gao H, Zhou H, et al. The role of mitochondria-derived peptides in cardiovascular disease: Recent updates. Biomed Pharmacother. 2019;117:109075. doi:10.1016/j.biopha.2019.109075.