Humanin (10mg)

Humanin Peptide and Genetic Origin

Humanin, a concise natural peptide, is believed to trace its genetic origins to the mitochondrial genome, specifically encoded by the ’16S ribosomal RNA gene.’ Researchers suggest that the length of the Humanin peptide might vary depending on its synthesis location, with a 21-amino acid version when synthesized within mitochondria and a 24-amino acid version when synthesized outside mitochondria but within the cytosol. The exploration of these genetic origins offers insights into the peptide’s potential biological activity.

The mitochondria, renowned as the cellular powerhouse, originates from a process involving the assimilation of distinct prokaryotes. Eukaryotic cells, at a certain juncture, seem to engulf these single-celled prokaryotic organisms, establishing an endosymbiotic relationship. Over time, the prokaryotes evolve within the host cell, ultimately giving rise to the intricate structures known as mitochondria.

Mitochondria are implicated in a myriad of crucial cellular processes, spanning from energy production to the orchestration of apoptosis, hemostasis, and the synthesis of heme proteins, among various other functions. The regulation of these diverse functions is seemingly executed by mitochondria through intricate communication with the cell, facilitated by a network of retrograde signals. These signals may originate from the nuclear genome housed within mitochondria, a feature possibly inherited from its prokaryotic ancestry.

A concise peptide known as Humanin is extracted from this genomic source. Given the pivotal role played by this genome, researchers have delved into the potential of Humanin in various biological functions.

Overview

Humanin peptide exhibits potential through its interaction with intracellular molecules and cell membrane receptors, potentially triggering cytoprotective and/or neuroprotective responses. Scientific investigations propose that Humanin might form complexes with the Bcl-2 associated X protein, commonly known as Bax protein, a crucial contributor to cellular apoptosis. By binding with the inactive state of Bax protein, Humanin may impede the alterations in Bax protein, potentially thwarting cellular apoptosis.

In addition to its exploration in the context of Bax interaction, Humanin investigations indicate potential binding with other intracellular molecules like actinin-4 and phosphoprotein 8, both associated with cellular apoptosis. Engagement with these proteins may instigate cytoprotective effects. Researchers propose that Humanin could potentially bind to two G protein-coupled peptide receptors, specifically FPRL-1 and FPRL-2 receptors, implicated in neurological functions. By binding to these receptors, Humanin might have the capacity to hinder amyloid β binding with FPRL-1 and FPRL-2 receptors, potentially offering a protective influence against certain neurological deteriorations.

Scientific Investigations and Clinical Trials

Humanin Peptide and Cellular Resilience

Cellular resilience, particularly against oxidative stress, is a critical aspect of maintaining cellular functions. Investigations into Humanin peptide’s impact on cellular resilience have shown promising results. In a study focusing on human dermal fibroblasts, the cells were exposed to hydrogen peroxide to induce oxidative stress. Cells treated with Humanin peptide exhibited a notable reduction in oxidative stress markers compared to untreated cells, suggesting a potential role in enhancing cellular resilience. The findings hint at Humanin’s capacity to support cellular health under conditions of oxidative challenge, presenting intriguing possibilities for further exploration in cellular biology and potential therapeutic applications.

Humanin Peptide and Metabolic Signaling

Exploring the intricate web of metabolic signaling, research(12) delved into the potential role of Humanin peptide in influencing key metabolic pathways. In a study on adipocytes, Humanin treatment was found to modulate insulin sensitivity and glucose metabolism. The peptide appeared to enhance insulin signaling pathways, promoting better glucose uptake and utilization. Additionally, Humanin exhibited regulatory effects on lipid metabolism, suggesting a multifaceted impact on metabolic homeostasis. These findings open avenues for understanding how Humanin may contribute to metabolic signaling, offering insights into its potential applications in addressing metabolic disorders and promoting overall metabolic health.

In a distinctive approach, Ames mice with a mutated prop-1 gene exhibited negligible GH and IGF-1 levels alongside a notable 40% surge in Humanin concentrations. Surprisingly, these mice displayed an extended lifespan compared to their normal counterparts. These outcomes substantiated the researchers’ proposition that Humanin might exhibit an inverse association with GH and IGF-1 levels while showcasing a direct correlation with cellular longevity. The intricate relationship observed in Ames mice offers intriguing perspectives on the molecular interplay governing the intricate balance between Humanin, growth hormones, and cellular aging.

Humanin Peptide and Cardiovascular Health

Exploring the potential impact on cardiovascular health, a study (13) utilized a rodent model with induced cardiac stress. The rodents were divided into two groups, one receiving Humanin treatment and the other serving as a control. Results from this study indicated that the group treated with Humanin exhibited improved cardiac function and reduced markers of oxidative stress compared to the control group. These findings suggest a promising role for Humanin in mitigating cardiovascular damage and promoting heart health. This avenue of research opens new possibilities for interventions targeting cardiovascular diseases.

In a separate investigation, (13) rodents with artificially induced cognitive decline were administered Humanin alongside a comparably structured peptide named PAGA. The study aimed to assess the impact of both peptides on the cognitive function of the rodents. Results indicated that both peptides exhibited modest enhancements in mitigating cognitive impairment, as observed and suggested by the researchers. This study sheds light on the potential cognitive benefits associated with these peptides, paving the way for further exploration in neurological therapeutics.

Humanin Peptide and Metabolic Homeostasis

To assess the impact of Humanin on metabolic homeostasis, researchers conducted a study (14) on nonobese diabetic mice. Upon administration of Humanin to a subset of these mice, there was observed improvement in glucose tolerance levels within a span of 6 weeks. Additionally, Humanin reportedly contributed to a delay in the onset of diabetes in the treated mice over a 20-week period. These findings suggest that Humanin may play a role in maintaining metabolic equilibrium, presenting potential implications for addressing metabolic disorders.

In an alternative investigation, (15) mice at the age of 12 weeks were exposed to a diet comprising 60% high fat and simultaneously administered Humanin for a duration of 4 weeks. The study results indicated no discernible variance in food intake; nevertheless, there was an observed reduction of approximately 20% in body weight gain. Notably, the mice exhibited heightened energy expenditure, lowered fasting glucose levels, and increased insulin levels, implying potential metabolic benefits associated with Humanin administration.

Humanin Peptide and Neuroprotective Potential

In a research endeavor (16), retinal cells subjected to cobalt chloride-induced hypoxia, resulting in cellular apoptosis, were examined to gauge the potential neuroprotective effects of Humanin. Following the administration of Humanin to the hypoxia-induced cells, noteworthy observations were made. Researchers reported that the peptide exhibited a capacity to reverse the deleterious effects induced by cobalt chloride, serving as a protective agent for the cells under conditions of reduced oxygen levels.

Supplementary investigations (17) propose that Humanin could potentially enhance metabolic activity, potentially elevating cell survival rates, particularly in cases of lymphocyte demise, with potential implications in conditions such as ischemia. Researchers are exploring the peptide’s multifaceted roles in cellular responses to diverse stressors.

Humanin Peptide and Neuroprotection in Cerebral Ischemia

This investigation (18) aimed to delve into the neuroprotective capabilities of Humanin in the context of cerebral ischemia. In the experimental setup, mice underwent induced cerebral artery occlusion. The mice were exposed to low concentrations of Humanin for 30 minutes, with subsequent reintroductions at 0, 2, 4, and 6 hours post-ischemia. Another group of mice received Humanin solely one hour before the ischemic event. Continuous administration of the peptide appeared to result in a nearly 30% reduction in ischemic volume. The presence of Humanin following ischemia reportedly further mitigated the impact of the ischemic event.

Humanin Peptide and Anxiolytic Action

Research (19) has proposed that Humanin might interact with the FPR2 receptor in the brain, potentially triggering anxiolytic effects. As a result, the findings from this study suggest that Humanin could alleviate symptoms of anxiety.

In this particular investigation (20), carcinogenic mice were subjected to twice-weekly induction with Bortezomib and Humanin to assess their potential impact on carcinogenic cells. While Bortezomib appeared to induce cell apoptosis, the combination of Humanin and Bortezomib demonstrated some potential, partially reversing the apoptosis of healthy cells.

Humanin peptide is exclusively provided for scientific and laboratory research applications. Prior to placing an order, we strongly recommend a thorough review and compliance with our stipulated Terms and Conditions.