Studies suggest Humanin is a naturally occurring peptide that may affect cell survival, inflammatory responses, metabolic rate, and mitochondrial performance. According to research, the mitochondrial '16S ribosomal RNA gene' encodes the Humanin peptide .
The peptide's final length is considered to be determined by the environment in which it was synthesized. If the peptide is made in the mitochondria, it has 21 amino acids; if it is made outside the mitochondria, in the cytosol, it has 24 amino acids [v]. Both of these peptides have been speculated to have biological action.
In the early 2000s [vi], three separate labs, each focusing on a different topic, independently discovered Humanin. Humanin [iv] was found by the Nishimoto lab during their hunt for cytoprotective proteins.
The Pinchas Cohen lab found the peptide [vii] while searching for proteins that may interact with immunoglobulin.
Finally, the Reed laboratory discovered the peptide while searching for proteins that might interact with apoptosis-related compounds [viii].
The mitochondria, the cell's energy generator, are reported to originate from ingesting individual prokaryotes. Endosymbiotic relationships between prokaryotic (single-celled) organisms and eukaryotic hosts result in the eventual development of mitochondria [i].
Numerous essential cellular processes, such as energy production, apoptosis regulation, hemostasis, and heme protein synthesis, are dubbed as mitochondrial. Mitochondria appear to communicate with the other cells through numerous retrograde signals, allowing them to control these processes. The mitochondrial, nuclear genome, which is of bacterial origin [ii], may encode these signals.
Mitochondria are suggested by scientists to be very vulnerable to the debilitating impact of reactive oxygen species (ROS). Studies suggest Humanin may inhibit mitochondrial death by inhibiting these reactive oxygen species [ix].
This was suggested in a study [ix] where oxidative stress was induced in the retinal pigment epithelium cells by treating them with tert-butyl hydroperoxide. Humanin was added to some of these cells for 24 hours.
Cells given Humanin appeared to show suppression of tert-butyl hydroperoxide-induced ROS production. This reportedly improved mitochondrial activity and restored bioenergetics in retinal pigment epithelial cells.
Cobalt chloride, which causes hypoxia and cell death, was used in research [x] on isolated retinal cells. Humanin was suggested to protect cells from hypoxia by possibly reversing the action of cobalt chloride on hypoxia-induced cells.
Furthermore, research [xi] speculated that Humanin might improve lymphocyte survival rates by increasing metabolic activity. This provides support for the potential of Humanin in mitigating the impact of metabolic dysfunction and cerebral ischemia.
The purpose of this research [xii] was to investigate the potential neuroprotective properties of Humanin under conditions of cerebral ischemia.
Experimental blockage of a cerebral artery was produced in mice as part of this investigation. After 30 minutes, mice were given Humanin at 0, 2, 4, and 6 hours post-ischemia. Other mice were given Humanin alone an hour before they were subjected to ischemia.
The study suggests Humanin may have decreased the ischemia volume by about 30%. The peptide's use appeared to mitigate the ischemic consequences even more.
Researchers speculate Humanin's anxiolytic potential may be due, at least in part, to its binding with the FPR2 receptor in the brain, as suggested by several studies [xiii]. Thus, Humanin has been hypothesized to alleviate anxiety and protect against memory impairment and anxiety.
Humanin was used to generate cancer in carcinogenic mice in this investigation [xiv].
Humanin peptide seemed to successfully reverse the apoptosis of the healthy cells that were caused. This research suggested that Humanin may shield cells from chemotherapeutic agent-induced damage and prevent carcinogenesis.
Humanin is a one-of-a-kind peptide encoded in the mitochondrial genome and is produced naturally by the body. Humanin may have anywhere from 21 to 24 amino acids depending on its production site.
Research suggests it may exert its neuroprotective and cytoprotective actions largely by interacting with intracellular or extracellular receptors of the organism. Humanin has been suggested to have several properties, including preventing cellular death, enhancing lifespan, and decreasing insulin resistance.
Only academic and scientific institutions are allowed to purchase Humanin. If you are a licensed professional interested in purchasing Humanin peptides for salefor your clinical studies, you can visit Biotech Peptides. Please note that none of the items listed are approved for human or animal consumption. Laboratory research chemicals are only for in-vitro and in-lab use. Any kind of physical introduction is illegal. Only authorized academics and working professionals may make purchases. The content of this article is intended only for educational purposes.