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Humanin

HN, S14G-Humanin

Quick Stats
Studies 491
Trials 100
Score 3
2009 pubmed 52 citations

Humanin and the receptors for humanin.

Matsuoka. Masaaki M; Hashimoto. Yuichi Y

Key Findings

  • Humanin protects neurons from Alzheimer’s‑related death in mouse models
  • The peptide works in living animals, not just cells in a dish
  • It signals through a receptor complex that includes CNTFRα, WSX‑1, and gp130

Practical Outcomes

  • The main takeaway is that Humanin shows potential as a neuroprotective agent against Alzheimer’s, but it’s not ready for self‑experimentation. Biohackers should wait for human safety and dosage data before trying supplements or analogs, and keep an eye on emerging clinical research.

Summary

Humanin is a tiny protein that has been shown in mouse studies to protect brain cells from the damage that leads to Alzheimer’s disease. It works by attaching to a specific set of receptors on the cell surface, which helps stop cell death and keep neurons functioning. While the results are promising, they’re still in animal models, so we don’t yet know the right dose or safety for people.

Abstract

Alzheimer's disease (AD) is a prevalent dementia-causing neurodegenerative disease. Neuronal death is closely linked to the progression of AD-associated dementia. Accumulating evidence has established that a 24-amino-acid bioactive peptide, Humanin, protects neurons from AD-related neuronal death. A series of studies using various murine AD models including familial AD gene-expressing transgenic mice have shown that Humanin is effective against AD-related neuronal dysfunction in vivo. Most recently, it has been shown that Humanin inhibits neuronal cell death and dysfunction by binding to a novel IL-6-receptor-related receptor(s) on the cell surface involving CNTFRalpha, WSX-1, and gp130. These findings suggest that endogenous Humanin [or a Humanin-like substance(s)] may suppress the onset of AD-related dementia by inhibiting both AD-related neuronal cell death and dysfunction.

Study Information

Provider

pubmed

Year

2009

Date

2009-12-09T00:00:00.000Z

DOI

10.1007/s12035-009-8090-z

Citations

52

References

78