Description
Humanin Peptide
Humanin is a naturally occurring micropeptide, considered to be unique in that it is encoded by mitochondrial DNA. It appears to act as a cytoprotective protein and may protect cells from the process of apoptosis (programmed cell death) by interfering with the normal operation of the Bcl2-related X protein (Bax).[1] Researchers report that Humanin may “prevent the translocation of Bax from cytosol to mitochondria. Conversely, reducing Humanin expression by small interfering RNAs sensitizes cells to Bax and increases Bax translocation to membranes.” Studies suggest that Humanin may be important for protecting neurons, heart tissue, muscle cells, the retina of the eye, and the lining of blood vessels.
Specifications
Other Known Titles: formyl humanin, HNGF6A protein
Sequence: Met-Ala-Pro-Arg-Gly-Phe-Ser-Cys-Leu-Leu-Leu-Leu-Thr-Ser-Glu-Ile-Asp-Leu-Pro-Val-Lys-Arg-Arg-Ala
Molecular Formula: C119H204N34O32S2
Molecular Weight: 2687.3 g/mol
Humanin Research
Micropeptides
Micropeptides, like Humanin, are produced by a short open reading frame (sORF) and are not modified after production. Many sORFs have been identified, measuring 100-150 amino acids in length.[2] Researchers speculate that their functions may range from improving mRNA processing, to assisting in repairing DNA damage, and creating complex macro-proteins. Humanin, one of the smallest micropeptides known to date, is only 24 amino acids long. It appears to interact with the Bcl2-related X protein (Bax) to regulate apoptosis and, if necessary, block Bax function and protect cells that may otherwise be destroyed.
Humanin and Neuroprotection
Studies in rats have suggested that micropeptides may protect Alzheimer’s disease neurons and prevent cell death caused by the formation of beta-amyloid plaques.[3] The scientists note that “HN exhibits multiple intracellular and extracellular anti-cell death actions and antagonizes various AD-associated pathomechanisms including amyloid plaque accumulation.” Studies further suggest that peptides may prevent the death of excitotoxic neurons in experiments with NMDA pulses. It is hoped that this potential of Humanin may delay or stop neurodegenerative diseases such as Alzheimer’s disease and other forms of dementia. Under normal circumstances, Bcl2 family proteins may signal the release of proteins from mitochondrial membranes, activating caspases and coordinating the orderly destruction and recycling of cells. This process is practically useful in many situations, such as when a virus invades, where a small number of cells can be destroyed to prevent widespread tissue damage. However, the process may become dysregulated under certain conditions, leading to widespread unsuppressed cell death. Humanin appears to bind to the Bcl2-stimulating proteins Bid and tBid and block their function. This action may potentially shut down the apoptotic pathway at its origin.
Humanin and Heart Disease
A study by the Mayo Clinic posited that Humanin may be expressed on the walls of the vascular system and may interfere with the production of reactive oxygen species (free radicals) in response to LDL oxidation.[5] It appears to hold the potential to reduce active oxygen species in the vascular system by up to 50%, and may potentially reduce apoptosis by up to 50% as well. Cardiology researchers have long sought blood markers that could be used to quantify how effectively mitochondria function in cardiovascular disease. It is an important measure in the progression of heart disease and may help to estimate tissue ischemia and determine when to intervene. According to a Russian study, the reduction is proportional to the severity of cardiovascular disease, so Humanin levels may be a potential marker for cases of this kind.
Humanin and Retinal Disease
Retinal pigment epithelium (RPE) is the layer of the retina that covers and nourishes the cells that cause vision. It appears to play a role in the absorption and scattering of light, filtering blood components that reach the inside of the retina. It also, above all, may establish the nature of immune privilege inside the eye. RPE damage has been associated with age-related macular degeneration, diabetic retinopathy, and other serious eye conditions. Current studies have suggested that Humanin may be an important component of RPE and may reduce oxidative stress in this tissue.[6] Humanin supplementation in cell culture appears to improve RPE function and increase tissue resistance to apoptosis. This may help scientists in prevention research for retinal disorders such as macular degeneration.
Humanin and Bone Health
Bone loss is a serious condition, and researchers commonly employ glucocorticoids to mitigate severe inflammation (such as autoimmune inflammation), which may induce extreme bone loss when used at high concentrations or for long periods. Researchers in Sweden and South Korea have hypothesized that Humanin may impact bones in two potential ways.[7] First, micropeptides like Humanin have been suggested to prevent chondrocytes (cells that produce the collagen matrix in which bone is built) from dying, possibly without obstructing the activity of glucocorticoids such as dexamethasone. This impact may increase bone and cartilage growth or offset some of the accelerated bone loss caused by glucocorticoids. Humanin has also been suggested to reduce osteoclast formation. Osteoclasts are the cells that cause bone loss and remodeling. Overactivation of these cells may result in severe bone loss. By preventing osteoclast formation, Humanin may potentially reduce excessive bone remodeling and loss.
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
- Guo B, Zhai D, Cabezas E, Welsh K, Nouraini S, Satterthwait AC, Reed JC. Humanin peptide suppresses apoptosis by interfering with Bax activation. Nature. 2003 May 22;423(6938):456-61. doi: 10.1038/nature01627. Epub 2003 May 4. PMID: 12732850.
- Sousa ME, Farkas MH. Micropeptide. PLoS Genet. 2018 Dec 13;14(12):e1007764. doi: 10.1371/journal.pgen.1007764. PMID: 30543625; PMCID: PMC6292567.
- Niikura T. Humanin and Alzheimer’s disease: The beginning of a new field. Biochim Biophys Acta Gen Subj. 2022 Jan;1866(1):130024. doi: 10.1016/j.bbagen.2021.130024. Epub 2021 Oct 7. PMID: 34626746.
- Xiao J, Kim SJ, Cohen P, Yen K. Humanin: Functional Interfaces with IGF-I. Growth Horm IGF Res. 2016 Aug;29:21-27. doi: 10.1016/j.ghir.2016.03.005. Epub 2016 Apr 7. PMID: 27082450; PMCID: PMC4961574.
- Qin Q, Mehta H, Yen K, Navarrete G, Brandhorst S, Wan J, Delrio S, Zhang X, Lerman LO, Cohen P, Lerman A. Chronic treatment with the mitochondrial peptide humanin prevents age-related myocardial fibrosis in mice. Am J Physiol Heart Circ Physiol. 2018 Nov 1;315(5):H1127-H1136. doi: 10.1152/ajpheart.00685.2017. Epub 2018 Jul 13. PMID: 30004252; PMCID: PMC6415743.
- Li Z, Sreekumar PG, Peddi S, Hinton DR, Kannan R, MacKay JA. The humanin peptide mediates ELP nanoassembly and protects human retinal pigment epithelial cells from oxidative stress. Nanomedicine. 2020 Feb;24:102111. doi: 10.1016/j.nano.2019.102111. Epub 2019 Oct 23. PMID: 31655204; PMCID: PMC7263384.
- Kang N, Kim KW, Shin DM. Humanin suppresses receptor activator of nuclear factor-κB ligand-induced osteoclast differentiation via AMP-activated protein kinase activation. Korean J Physiol Pharmacol. 2019 Sep;23(5):411-417. doi: 10.4196/kjpp.2019.23.5.411. Epub 2019 Aug 26. PMID: 31496878; PMCID: PMC6717796.
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