Livagen is classified by scientists as a potential peptide bioregulator of the liver, GI tract, and immune system. Livagen peptide has been suggested to act on the DNA and gene expression patterns. The gene-activating potential of Livagen on the immune system and GI tract may stem from certain cell aging prevention characteristics of the peptide.

Livagen peptide has been suggested to potentially modulate Chromatin, and thereby impact immune system function. Due to DNA packing, DNA in eukaryotes may reduce to roughly 100,000. DNA is a double helix protein wrapped by histone proteins, which may combine to form chromatin structures. The chromatin structure may subsequently condense to form chromosomes.^[2] Researchers suggest that “Livagen causes de-heterochromatinization (activation) of chromatin, which is realized via modification of heterochromatin and heterochromatinized regions.”

Livagen peptide may potentially stimulate chromatin decondensation by activating multiple genes in lymphocytes, according to research. This mechanism may promote the activation of silent genes, such as ribosomal genes, which may potentially boost protein synthesis and cell activity.^[3] During the investigation, a comparison of Livagen, Epithalon, and Vilon was made. Livagen peptide was suggested to exhibit four impacts on lymphocytes, according to the results. Unpacking chromatin was one among them, as well as decondensation, reactivation of ribosomal genes to activate synthetic processes, and the changing the expression of genes may then occur.

B cells, T cells, and natural killer cells are all types of lymphocytes. T cells appear to produce antibodies specific to cells infected with viruses, bacteria, or malignant cells, whereas B cells appear to produce antiviral and antibacterial antibodies. T cells may produce cytokines that influence immune responses and inflammation.

Livagen peptide may potentially influence pain perception. Enkephalins are peptides that are suggested control nociception. They attach to mu and delta-opioid receptors and may potentially transmit pain signals. When Mu receptors, which bind to morphine, are triggered, they may lower pain, blood pressure, and awareness. Delta receptors may alleviate pain and may be involved in opiate-induced respiratory depression.^[4]According to Livagen research, the peptide may block enkephalin-degrading enzyme activity in the blood, causing a rise in natural painkiller levels.

Livagen peptide may interact with the heart muscle. According to research, chromatin dysregulation may be one of the pathogenic components of  hypertrophic cardiomyopathy (HCM) and atherosclerosis.^[5] The scientists suggest that “The peptide bioregulator Livagen could induce reactivation (deheterochromatinization) of chromatin to modify heterochromatinized chromosomal regions in cultured lymphocytes.” Scientists believe that genes produced by chromatin decondensation in lymphocytes might minimize the long-term consequences of several forms of heart disease. Livagen peptide may potentially perform this function. In research models of hypertrophic cardiomyopathy (HCM), altered lymphocyte gene expression might minimize scarring and inflammation.^[6]

Livagen may impact the gastrointestinal tract. According to the Livagen peptide study, the peptide might increase GI tract vagal nerve signaling and change levels of prostaglandins and mucosal nitric oxide. This may lead to gastroprotection, possibly managing diarrhea, symptoms, and inflammatory bowel disease.^[7]

 

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

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1. Lezhava T. A. (2001). Funktsional’nye osobennosti khromosom cheloveka i starenie [Human chromosome functional characteristics and aging]. Advances in gerontology = Uspekhi gerontologii, 8, 34–43.
2. Khavinson, V. K.h, Lezhava, T. A., Monaselidze, J. G., Dzhokhadze, T. A., Dvalishvili, N. A., Bablishvili, N. K., & Ryadnova, I. Y. (2002). Effects of Livagen peptide on chromatin activation in lymphocytes from old people. Bulletin of experimental biology and medicine, 134(4), 389–392. doi: 10.1023/a:1021924702103.
3. Lezhava, T., Monaselidze, J., Kadotani, T., Dvalishvili, N., & Buadze, T. (2006). Anti-aging peptide bioregulators induce reactivation of chromatin. Georgian medical news, (133), 111–115.
4. Kost, N. V., Sokolov, O. I.u, Gabaeva, M. V., Zolotarev, I.uA., Malinin, V. V., & Khavinson, V. K.h (2003). Vliianie novykh peptidnykh bioreguliatorov livagena i épitalona na énkefalindegradiruiushchie fermenty syvorotki krovi cheloveka [Effect of new peptide bioregulators livagen and epitalon on enkephalin-degrading enzymes in human serum]. Izvestiia Akademii nauk. Seriia biologicheskaia, (4), 427–429.
5. Lezhava, T., Monaselidze, J., Kadotani, T., Dvalishvili, N., & Buadze, T. (2006). Anti-aging peptide bioregulators induce reactivation of chromatin. Georgian medical news, (133), 111–115.
6. Dzhokhadze, T. A., Buadze, T. Z.h, Gaĭozishvili, M. N., Rogava, M. A., & Lazhava, T. A. (2013). Georgian medical news, (225), 94–97.
7. Gyires, K., & Rónai, A. Z. (2001). Supraspinal delta- and mu-opioid receptors mediate gastric mucosal protection in the rat. The Journal of pharmacology and experimental therapeutics, 297(3), 1010–1015.

According to a preliminary rodent study, Thymalin peptide may potentially complement pulsed laser radiation for mitigating the proliferation of cancer cells in certain subtypes of cancer.^[1] Thymalin may potentially increase antibody-producing cells in the spleen. Nonathymulin peptide has been suggested in studies to have tumor mitigating characteristics, with one study reporting tumor development mitigation in almost 80% of instances and decreasing tumor size in nearly half of the animal research models examined.^[2]  Thymalin peptide combined with plasmapheresis may potentially be more effective in combating chronic lympholeukemia.^[3] Furthermore, it might develop hematological compensation than traditional chemotherapy compounds and procedures, in addition to possible improvement in lymphoid function.^[4]

 

Thymalin Peptide and Immune Function

Thymalin peptide may potentially affect cellular immunity, modifying lymphocyte subpopulation levels, influencing T-cell development, and modulating natural killer (NK) cell activity, according to research.^[5] Nonathymulin peptide exposure may possibly correct the immune system and improve T-lymphocyte proliferation in research models of diabetic retinopathy, resulting in less inflammation and slower disease progression rates.^[6] This might apply to chronic immunological deficiency/immune HIV dysregulation. Thymalin, in combination with HAART, may repair immune system damage and increase CD4 + T-cell counts. Research is ongoing to see whether Thymalin may interact with HIV vaccinations to boost immunization responses. Thymalin peptide exposure in mice without the thyroid gland appeared to have reversed or protected the animals from weight loss and cell growth.

 

Thymalin Peptide and Kidney Diseases

Nonathymulin peptide exposure has been suggested in research to potentially mitigate inflammatory kidney disease, such as chronic glomerulonephritis. Research is ongoing.

 

Thymalin and the Circadian-Rhythm

Circadian rhythm disruptions may be due to alterations in thymic components and cellular and humoral immunity, according to research. Changes in circadian rhythm, according to scientists, might affect thymic function, leading to immune system suppression. Thymalin peptide, on the other hand, may not regulate circadian rhythm. However, it might reset alterations in immunological insufficiency induced by variations in sleep-wake cycles.

 

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

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1. Kozlov, A. P., & Moskalik, K. G. (1980). Pulsed laser radiation therapy of skin tumors. Cancer, 46(10), 2172–2178. doi:10.1002/1097-0142(19801115)46:10‹2172::aid-cncr2820461013›3.0.co;2-l.
2. Zhukova, G. V., Schikhlyarova, A. I., Barteneva, T. A., Shevchenko, A. N., & Zakharyuta, F. M. (2018). Effect of Thymalin on the Tumor and Thymus under Conditions of Activation Therapy In Vivo. Bulletin of experimental biology and medicine, 165(1), 80–83. doi:10.1007/s10517-018-4104-z.
3. Tretiak, N. N., Babenko, T. F., Gaĭdukova, S. N., Zverkova, A. S., & Beschastnaia, S. P. (1998). Effektivnost’ primeneniia timalina i plazmafereza v kompleksnom lechenii bol’nykh khronicheskim limfoleĭkozom [The efficacy of using thymalin and plasmapheresis in the combined treatment of patients with chronic lympholeukemia]. Likars’ka sprava, (2), 93–96.
4. Babenko, T. F., Antonenko, V. T., & SkuratovskiUi, M. F. (1989). Timalin v kompleksnom lechenii bol’nykh khronicheskim limfoleĭkozom [Thymalin in the combined treatment of patients with chronic lympholeukemia]. Vrachebnoe delo, (3), 47–49.
5. Bach, J., Bardenne, M., Pleau, J., & Rosa, J. (1977). Biochemical characterisation of a serum thymic factor. Nature, 266(5597), 55–57. doi:10.1038/266055a0.
6. Zhaboiedov, H. D., Bychkova, N. H., Skrypnik, R. L., & Sydorova, M. V. (2001). Doslidzhennia stanu klitynnoho i humoral’noho imunitetu ta vyznachennia indyvidual’noï chutlyvosti T-limfotsytiv do imunokorektoriv u khvorykh s diabetychnoiu retynopatiieiu [Evaluation of cellular and humoral immunity and individual sensitivity of T-lymphocytes to immunocorrectors in patients with diabetic retinopathy]. Likars’ka sprava, (1), 53–56.
7. Isaeva, M. P., Budazhabon, G. B., & Kuznik, B. I. (1989). Vliianie timalina na pokazateli immuniteta i gemostaza u bol’nykh rasprostranennymi formami psoziaza [The effect of thymalin on indices of immunity and hemostasis in patients with disseminated forms of psoriasis]. Vestnik dermatologii i venerologii, (10), 42–43.
8. Budazhabon, G. V., Kuznik, B. I., Morozov, V. G., Orlova, N. N., & Khavinson, V. K.h (1984). Sostoianie immunogeneza i gemostaza u bol’nykh s obostreniem khronicheskogo glomerulonefrita, lechennykh timalinom [Immunogenesis and hemostasis in patients with exacerbated chronic glomerulonephritis treated with thymalin]. Terapevticheskii arkhiv, 56(10), 62–66.
9. Maslennikov, A. A., Kamenev, V. F., & Kolomiets, V. M. (2007). Problemy tuberkuleza i boleznei legkikh, (9), 30–33.

GHRP-2, also known as Pralmorelin, is a synthetic peptide that researchers developed to potentially stimulate growth hormone secretion by binding to the growth/ghrelin hormone secretagogue receptor. GHRP-2 is the first growth hormone secretion promoter to be introduced. It has been lauded by scientists as a potential diagnostic peptide for growth hormone insufficiency and subsequent adrenal failure. Its effects on muscular growth, the immune system, hunger, and sleep cycles are still under study.

 

GHRP-2 (Pralmorelin) Research

Muscle Structure: According to a study in Yaks, GHRP-2 was suggested to increase muscle growth in two ways: through possible increased protein deposition and reduced protein degradation. Pralmorelin (GHRP-2) may potentially aid in the mitigation of natural growth plateaus caused by disease, poor environmental conditions, or food shortages.^[1] According to preliminary studies, Pralmorelin (GHRP-2) may potentially reduce muscle atrophy by inactivating atrogin-1 and MurRF1, two proteins involved in the muscle breakdown process.^[2] The researchers suggested that “GHRP-2 attenuated dexamethasone-induced expression of them dose-dependently and decreased the basal level of MuRF1 mRNA.”  Pralmorelin may possibly increase muscle protein deposition by activating growth hormone and insulin-like growth factor-1. Even in critical situations, the combined impact of lowering disintegration and increasing deposition may possibly allow for the formation of lean body mass.

Immune System: According to studies, Pralmorelin may possibly stimulate the Thymus—an organ in the immune system that is considered to defend certain cells. The thymus may aid the development of T lymphocytes. T cells are adaptive immune cells that help to fight off complex infections. Thymic function may potentially diminish over time, inducing possible dysfunctions ranging from diminished immunity to inadequate tissue repair and the inability to fight infections, protect against cancer cell growth, and normal tissue function maintenance.^[3] The peptide may potentially act to rejuvenate the thymus, improving the kind and quantity of T cells generated. This may in turn boost immunity.

Appetite: According to studies, Pralmorelin (GHRP-2) may potentially increase appetite and food consumption.^[4] The researchers report that “GHRP-2, like ghrelin, may increase food intake, suggesting that GHRP-2 might be a valuable tool for investigating ghrelin action on food intake.”

Sleep Quality: Research studies suggest that Pralmorelin might extend the duration of stages 3 and 4 of the sleep cycle by roughly 50% and 20%, respectively, while decreasing the frequency of deviation from normal sleep by around one-third.^[5]

Pain Perception: Previously, scientists supposed that Pralmorelin (GHRP-2) may potentially reduce pain in osteoarthritic animal models by increasing growth hormone levels and mending wounded tissues. Some researchers suggest that GHRP-2 has a direct effect on pain perception.^[6] Four opioid receptors are currently known. Some of these receptors may mediate pain, while others may control breathing and wakefulness . GHRP-2 is an opioid receptor agonist that specifically binds to opioid receptors implicated in sedation, pain relief, and reward seeking behavior.

The Heart: Research investigations in damaged heart cell culture lines sugged that Pralmorelin (GHRP-2) might protect heart cells by lowering heart cell apoptosis after a heart attack.^[7] GHRP-2 may potentially achieve this by decreasing blood circulation and, as a result, nutrition availability.
Studies on Hexarelin, a GHRP-2 analog, suggest that there may be specific peptides for these receptors.^[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

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1. Hu, R., Wang, Z., Peng, Q., Zou, H., Wang, H., Yu, X., Jing, X., Wang, Y., Cao, B., Bao, S., Zhang, W., Zhao, S., Ji, H., Kong, X., & Niu, Q. (2016). Effects of GHRP-2 and Cysteamine Administration on Growth Performance, Somatotropic Axis Hormone and Muscle Protein Deposition in Yaks (Bos grunniens) with Growth Retardation. PloS one, 11(2), e0149461. doi:10.1371/journal.pone.0149461.
2. Yamamoto, D., Ikeshita, N., Matsubara, T., Tasaki, H., Herningtyas, E. H., Toda, K., Iida, K., Takahashi, Y., Kaji, H., Chihara, K., & Okimura, Y. (2008). GHRP-2, a GHS-R agonist, directly acts on myocytes to attenuate the dexamethasone-induced expressions of muscle-specific ubiquitin ligases, Atrogin-1 and MuRF1. Life sciences, 82(9-10), 460–466. doi:10.1016/j.lfs.2007.11.019.
3. Taub, D. D., Murphy, W. J., & Longo, D. L. (2010). Rejuvenation of the aging thymus: growth hormone-mediated and ghrelin-mediated signaling pathways. Current opinion in pharmacology, 10(4), 408–424. doi:10.1016/j.coph.2010.04.015.
4. Laferrère, B., Abraham, C., Russell, C. D., & Bowers, C. Y. (2005). Growth hormone releasing peptide-2 (GHRP-2), like ghrelin, increases food intake in healthy men. The Journal of clinical endocrinology and metabolism, 90(2), 611–614. doi:10.1210/jc.2004-1719.
5. Copinschi, G., Leproult, R., Van Onderbergen, A., Caufriez, A., Cole, K. Y., Schilling, L. M., Mendel, C. M., De Lepeleire, I., Bolognese, J. A., & Van Cauter, E. (1997). Prolonged oral treatment with MK-677, a novel growth hormone secretagogue, improves sleep quality in man. Neuroendocrinology, 66(4), 278–286. doi:10.1159/000127249.
6. Zeng, P., Li, S., Zheng, Y. H., Liu, F. Y., Wang, J. L., Zhang, D. L., & Wei, J. (2014). Ghrelin receptor agonist, GHRP-2, produces antinociceptive effects at the supraspinal level via the opioid receptor in mice. Peptides, 55, 103–109. doi:10.1016/j.peptides.2014.02.013.
7. Muccioli, G., Broglio, F., Valetto, M. R., Ghè, C., Catapano, F., Graziani, A., Papotti, M., Bisi, G., Deghenghi, R., & Ghigo, E. (2000). Growth hormone-releasing peptides and the cardiovascular system. Annales d’endocrinologie, 61(1), 27–31.
8. Bodart, V., Bouchard, J. F., McNicoll, N., Escher, E., Carrière, P., Ghigo, E., Sejlitz, T., Sirois, M. G., Lamontagne, D., & Ong, H. (1999). Identification and characterization of a new growth hormone-releasing peptide receptor in the heart. Circulation research, 85(9), 796–802. doi:10.1161/01.res.85.9.796.

Frag 176-191, termed Lipolytic Fragment, is the modified version of AOD 9604. It is composed of a structural fragment of growth hormone. According to research, Frag 176-191 may potentially mimic certain characteristics of the parent protein. Fragment 176-191 may increase insulin levels without increasing insulin-like growth factor-1 (IGF-1) levels, which include mitigating carbohydrate metabolism, altering insulin sensitivity, and increasing long bone growth.  Fragment 176-191 peptide is suggested to be a concentrated and stabilized version of the growth hormone-releasing factor—GRF, which may potentially cause a more rapid increase in bodily growth hormone 12.5 times stronger. Fragment 176-191 may stimulate protein synthesis, increase vascularity via nitrogen retention, increase bone mineral density and modify cell aging cycles. It may exert influence in sleep cycles and possibly increase contractile strength via hyperplasia.

 

Research

 

1. Frag 176-191 and Blood Sugar Levels:

Research suggests that Frag 176-191 is a potentially potent synthetic equivalent of the growth hormone and may act to reduce blood sugar levels. This potential is secondary to the increase in plasma insulin levels. Research is ongoing to determine if Frag 176-191 may be employed effectively in research studies using research models of prediabetes and type II diabetes.

 

2. Fragment 176-191 and Cartilage:

Though interest in Frag 176-191 is primarily researched for its potential its lipolytic functions, research is ongoing to determine its other possible impacts. In 2015, research from Korea suggested that Frag 176-191 increases the effects of hyaluronic acid exposure that may promote cartilage regeneration. Studies in rabbits suggested that Frag 176-191 increased cartilage growth laboratory standards, and its combination with hyaluronic acid may produce a more potent effect. The overall result suggests that exposure to Frag 176-191 alone and alongside hyaluronic acid might reduce the disabilities following osteoarthritis.

 

3. Frag 176-191 and Weight:

Fragment 176-191 is commonly referred to as Lipolytic Fragment because of its potential lipolytic potential. This function may possibly be mediated by increased beta-3 adrenergic receptor production (𝛃3-AR or ADRB3). The agonist action of ADRB3 is to accelerate fat burning in fatty tissues and thermogenesis in skeletal muscles. Mouse models genetically induced to not produce ADRB3 appear not to respond to the lipolytic potential of hGH or Frag 176-191. Research suggests that Frag 176-191 action may be accompanied by energy expenditure and weight reduction, amounting to about 50% of reduced weight gain in animal models of obesity over exposure for three weeks. Notably, the weight reduction effect was reported only in obese mice. In lean mice, they appeared to maintain their standard body weight even on exposure to Fragment 176-191. These results suggest that specific lipolysis pathways may be responsible for overriding the effect of ADRB3.

 

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.

B7-33 is the synthetic derivative of H2-relaxin. B7-33 has been suggested to act similarly to h2-relaxin but does not appear to increase the production of cAMP. Its research relevance is suggested in the reduced fibrosis in chronic and acute diseases, such as lung inflammation, heart failure, kidney, etc. B7-33 may also act to reduce scar formation seen in cardiac injuries.

B7-33 is a soluble produced single-chain peptide equivalent of the naturally occurring protein H2-relaxin. B7-33 has been suggested to harbor properties similar to h2-relaxin without increasing the production of cAMP. B7-33 peptide may function to activate ERK1/2 phosphorylation, improve matrix metalloproteinase 2 (MMP2) expression, and extracellular collagen degradation. Despite having a possibly strong affinity for the RXFP-1 receptor, it doesn’t appear to activate the cAMP pathway. Instead, researchers hypothesize that it may activate the pERK pathway—a pathway considered to inhibit the cell cycle in the G1 phase.

The inhibition of the cell cycle progression in RXFP-1 receptor cells by the compound may induce downstream impacts. The anti-fibrotic potential of B7-33 may enhance the pERK1/2 signaling—boosting the synthesis of the enzyme matrix metalloproteinase (MMP)-2, which breaks down collagen. It may be of great advantage that B7-33 does not appear to activate cAMP as cAMP activation may modulate some tumor-promoting action.

 

Peptide Production

B7-33 may be more advantageous in research contexts than the natural H2-relaxin protein as it does not appear to activate the cAMP pathway but may instead hold onto certain anti-fibrotic characteristics. This is one of its advantages as B7-33 production is easy as it has less intricate 2D and 3D structures.

 

B7-33 and Fibrosis

Fibrosis is scarring or the unorganized regeneration of tissues. It is the last stage of several chronic diseases ranging from cardiovascular to lung diseases to cirrhosis of the liver and aberrant wound healing. Fibrosis is considered the primary cause of organ failure. According to research studies, the exposure of H2-relaxin following fibrosis may lead to vasodilatory action and a reduction in the long-term scarring effect of heart damage. That notwithstanding, H2-relaxin may exhibit some setbacks. It may potentially increase heart rate and may increase cancer cell progression. Most of these are linked to the activation of the cAMP pathway, allowing for the research on B7-33 to be relevant and of great import.

According to research by Dr. Akhter Hossain, one of the lead developers of B7-33, it may act to increase MMP-2 production slightly better than H2-relaxin. The results suggest a decrease in cardiac fibrosis in rat models of MI-induced heart failure. Subsequently, it may have improved heart function and reduced long-term symptoms such as heart failure complications. Research suggests that B7-33 reduces scarring in the heart following injury by about 50%. Similar results are reported in mouse models of asthma and lung fibrosis. Scientists introduced B7-33 in mouse models of prostate cancer, and B7-33 did not appear to promote tumor growth.

Scientific studies suggest that coating from B7-33 reduced the thickness of fibrotic capsules by about 50% in six weeks. Further research in B7-33 may aid researchers in preventing the unintentional ancillary action of certain anti-fibrotic molecules to decrease the fibrosis of implanted devices—allowing for more successful device implant.

 

B7-33 and Blood Vessels

Animal model research in male Wistar rats suggests that the compound exhibits the vasoprotective characteristics of serelaxin by promoting bradykinin-mediated endothelium-dependent relaxation in arteries. It may potentially achieve this by increasing endothelium-derived hyperpolarization in vascular beds.

 

B7-33 and Preeclampsia

Preeclampsia, termed Toxemia, is a critical pregnancy condition characterized by high blood pressure and decreased fetal weight. Preeclampsia is complex. In some cases, it may be life-threatening to both the fetus and the mother. Animal studies suggest that B7-33 may help control preeclampsia in severe cases. In this research, B7-33 may act like an RXFP-1 receptor to boost VEGF production in cytotrophoblasts—cells found in the developing fetus that help stimulate blood flow between mother and baby. Therefore, by stimulating VEGF production, B7-33 may potentially enhance blood vessel growth—improving the blood supply between the offspring and mother. Research has supposed that lipidated B7-33 may have a longer 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.

Pinealon is a peptide made up of three amino acid sequences. It is known as a peptide regulator because of its potential capacity to interact with DNA and change gene expression levels. Pinealon may potentially protect cells and tissues from the harmful action of hypoxia.

Compared to other peptides, Pinealon does not appear to bind to cell surfaces or cytoplasmic receptors. As a result, scientists hypothesized that Pinealon may be small enough to circumvent lipid bilayers (such as the cell membrane and nuclear membrane) and interact directly with DNA. According to scientific studies in cell cultures, the peptide may directly permeate cell membranes and nuclear membranes to interact with DNA.

 

Research

 

Pinealon and Cell Aging

Pinealon may impact cell aging cycles in the central nervous system, according to studies. Pinealon and Vesugen, according to a Russian study, may be anabolic in the brain and may reduce the cell aging process when assessed using biological age markers.

According to experts, Pinealon may be active in cells outside the central nervous system. Pinealon may influence muscle irisin synthesis, an adipocytokine produced in skeletal muscles and subcutaneous and visceral adipose areas that protect myocytes during exercise, promote fat burning, and induce telomere extension. As a result, increasing the lifespan of irisin may possibly improve telomere maintenance and assist in the fight against the harmful action of oxidative stress and cell aging.

 

Pinealon and Neuron Protection

Pinealon has been suggested following scientific studies in prenatal rats to protect neurons from oxidative damage while preventing cognitive functioning and motor coordination. The findings suggest a reduction in the accumulation of reactive oxygen species (ROS) and numerous necrotic cells in the brains of the rats studied. The compound appears to control cell cycles by activating proliferation pathways. It may mitigate some of the adverse action of ROS in oxidative stress.

Pinealon has been suggested to boost cell and neuron resilience to hypoxia in adult rats. The peptide appears to achieve this by increasing anti-oxidative enzyme systems and minimizing the excitotoxic action of N-methyl-D-aspartate (NMDA), an amino acid derivative considered to be capable of killing brain cells by over-excitation.

Irisin may promote neuronal differentiation, proliferation, and energy expenditure in the brain. Pinealon appears to raise irisin levels by modulating the gene expression that codes for the enzyme, possibly resulting in higher irisin levels due to the enzyme’s longer half-life.

 

Caspase-3 and Cell Death

Peptide research in animal models of ischemic stroke was suggested to alter cytokine signaling, which may lead to a rise in the levels of caspase-3 enzyme—an enzyme that triggers apoptosis. The peptide may inhibit at least one of the processes that induce cell death by modulating the activities of caspase-3, possibly lowering the impact of oxygen deprivation in stroke. Pinealon appears to mitigate long-term remodeling that may lead to myocardial infarction-related dysfunctions.

Pinealon’s potential in reducing caspase-3 expression are suggested further in studies in skin cells. The peptide may improve cell proliferation in older and young animals by decreasing skin apoptosis.

 

Pinealon and Sleep Regulation

Pinealon, may act to reset the pineal gland, possibly allowing for circadian rhythm disturbance, improved sleep cycle regulation. The capacity of the Pinealon to potentially adjust sleep has been associated with organism age. Irregular sleep may impact metabolic function, as well as cascade of physiological processes, in some ways not yet fully understood. Pinealon’s potential to regulate sleep may support physiological functioning on a macro level.

 

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.