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Humanin is a naturally occurring micro-peptide found in mitochondria. It protects cells from apoptosis and may be useful in staving off heart, eye, brain, and muscle diseases. Humanin is one of a select, small class of compounds targeting mitochondrial function and thus improving cellular energy efficiency and homeostasis.

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1. Humanin Overview


2. Molecular Structure of Humanin


3. Research on Humanin

Humanin Overview

Humanin is a small peptide derived from a protein called mitochondrial open reading frame of the 12S rRNA-c (MOTS-c). It was discovered in 2001 by Dr. Pinchas Cohen, a researcher at the University of California, Los Angeles (UCLA). Humanin is a part of a class of peptides known as mitochondria-derived peptides (MDPs) and is involved in various cellular processes and functions.  

Molecular Structure of Humanin


Molecular Formula: C152H252N44O42

Molecular Weight: 2611.41 grams per mole

Research on Humanin

What Is a Micro-peptide?
Micro-peptides are unique molecules in comparison to standard peptides and proteins. They are produced through short, open reading frames (sORFs) and remain unaltered after their formation. sORFs, typically spanning 100-150 amino acids, were initially disregarded, as it was widely believed that all peptides followed the same DNA-to-RNA-to-protein-to-modified protein process. The concept that modification could be bypassed entirely was overlooked.

In the human body, numerous sORFs have been identified, each with diverse functions ranging from facilitating mRNA processing to DNA damage repair and complex protein interaction, leading to the formation of macro-proteins. Humanin, one of the smallest micro-peptides, comprising only 24 amino acids, plays a crucial role in regulating apoptosis by interacting with the Bcl2-associated X protein (Bax), inhibiting Bax’s function when needed to safeguard vulnerable cells from destruction.

Studies in rats demonstrate that humanin offers protection against programmed cell death, particularly in scenarios like Alzheimer’s disease, where beta-amyloid plaque buildup triggers cell death. Additionally, research indicates that the peptide shields against excitotoxic neuron death in experiments involving NMDA pulses.

Similar findings have emerged in investigations of neuron death linked to prion disease. The potential of humanin to slow or halt neurodegenerative diseases, such as Alzheimer’s, by preventing apoptosis is encouraging, despite not addressing the root causes of conditions like amyloid plaque formation in Alzheimer’s disease. Humanin operates through two distinct mechanisms, both designed to prevent mitochondria from initiating the apoptosis pathway. Under normal conditions, Bcl-2 family proteins initiate the release of mitochondrial proteins, activating caspases that orchestrate orderly cell destruction and recycling. However, in certain diseases, this process goes awry, leading to uncontrolled, widespread cell death. Humanin binds to Bcl-2 stimulating proteins Bid and tBid, obstructing their function and thus halting the apoptosis pathway at its source.

Recent research from Argentina reveals that astrocytes release humanin to safeguard synapses in hippocampal neurons. As with many natural regulatory processes, it is speculated that humanin’s function may diminish with age, potentially contributing to age-related memory loss and increased neurodegenerative disease prevalence. Some researchers suggest that supplementing humanin in older adults could counteract the normal age-related decline in this critical micro-peptide’s production.

Humanin Interfaces with IGF-1:
Recent studies from the University of Southern California demonstrate that humanin interacts with insulin-like growth factor 1 (IGF-1). These two peptides mutually influence each other, with humanin reducing circulating IGF-1 levels and IGF-1 affecting humanin levels. While the precise mechanism remains unclear, evidence strongly suggests that humanin plays a significant role in IGF-1 signaling. These peptides collaborate to inhibit apoptosis, enhance insulin sensitivity, mitigate inflammation, and protect against specific heart diseases, although they may also act antagonistically in other contexts. Further research is necessary to fully understand their intricate interactions.

Heart Disease:
Research from the Mayo Clinic reveals that humanin is present in the walls of human blood vessels, where it shields these vessels from the harmful effects of oxidized LDL cholesterol. Humanin disrupts the production of reactive oxygen species (free radicals) in response to LDL oxidation, reducing both reactive oxygen species and apoptosis within the vasculature by 50%.

Additionally, research suggests that humanin levels may serve as a valuable marker in cardiovascular disease assessment, declining proportionally with disease severity. In this context, humanin could function as both a diagnostic marker and a potential treatment option for cardiovascular conditions by safeguarding stressed mitochondria.

Humanin Research and Retinal Disease:
Humanin has emerged as a vital component in the retinal pigment epithelium (RPE), a layer that nourishes and supports vision-related cells in the retina. It plays essential roles in light absorption, blood component filtration, and maintaining the immune-privileged status of the inner eye. Studies indicate that humanin reduces oxidative stress in the RPE and enhances its resistance to apoptosis. In cell cultures, supplementation with humanin has shown promise in improving RPE function, offering potential avenues for more effective treatments and prevention strategies for retinal diseases like macular degeneration.

Bone Health:
Bone loss, a significant concern, particularly in aging individuals, can result from various factors, including certain diseases and medical interventions. Notably, glucocorticoids used to combat severe inflammation can cause substantial bone loss when administered in high doses or for extended periods. Research from Sweden and Korea suggests that humanin may benefit bones in two ways: by preventing the death of chondrocytes, the cells responsible for the collagen matrix underlying bone, without interfering with the anti-inflammatory effects of glucocorticoids, and by reducing osteoclast formation, the cells responsible for bone breakdown. These effects promote bone and cartilage growth while curbing excessive bone remodeling and loss.

It is worth noting that humanin exhibits minimal side effects, offers low oral bioavailability, and excellent subcutaneous bioavailability in mice. However, dosages per kilogram in mice cannot be directly extrapolated to humans. Humanin available at Peptide Sciences is strictly for educational and scientific research purposes and is not intended for human consumption. Only licensed researchers should purchase and use humanin for their studies.

Humanin levels in relation to age. A significant decline in humanin levels is seen in older individuals.

Article Author

The above literature was researched, edited and organized by Dr. Logan, M.D. Dr. Logan holds a doctorate degree from Case Western Reserve University School of Medicine and a B.S. in molecular biology.


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