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Humanin

HN, S14G-Humanin

Quick Stats
Studies 491
Trials 100
Score 2
2019 pubmed 7 citations

Comparative genomic analysis identifies small open reading frames (sORFs) with peptide-encoding features in avian 16S rDNA.

Mortz. Mathieu M; Dégletagne. Cyril C; Romestaing. Caroline C; Duchamp. Claude C

Key Findings

  • Four highly conserved small open reading frames (sORFs) were identified in avian mitochondrial rDNA, including a Humanin-like peptide.
  • The sORFs show very low mutation rates (<0.1%) and maintain start/stop codons in over 80% of bird species.
  • The amino‑acid sequences of these peptides are as conserved as typical mitochondrial proteins, indicating likely functional relevance.

Practical Outcomes

  • The finding reinforces that Humanin is an evolutionarily conserved mitochondrial peptide, supporting its potential role in health and longevity. While it doesn’t provide new dosing or protocols, it validates interest in Humanin supplementation for biohackers seeking mitochondrial‑based interventions.

Summary

Scientists compared bird mitochondrial DNA and found that birds have tiny genes that can make peptides similar to the human peptide Humanin. These tiny genes are almost identical across many bird species, which suggests they’re important and have been kept unchanged through evolution.

Abstract

The mitochondrial genome (mt-DNA) functional repertoire has recently been enriched in mammals by the identification of functional small open reading frames (sORFs) embedded in ribosomal DNAs. Through comparative genomic analyses the presence of putatively functional sORFs was investigated in birds. Alignment of available avian mt-DNA sequences revealed highly conserved regions containing four putative sORFs that presented low insertion/deletion polymorphism rate (&lt;0.1%) and preserved in frame start/stop codons in &gt;80% of species. Detected sORFs included avian homologs of human Humanin and Short-Humanin-Like-Peptide 6 and two new sORFs not yet described in mammals. The amino-acid sequences of the four putative encoded peptides were strongly conserved among birds, with amino-acid p-distances (5.6 to 25.4%) similar to those calculated for typical avian mt-DNA-encoded proteins (14.8%). Conservation resulted from either drastic conservation of the nucleotide sequence or negative selection pressure. These data extend to birds the possibility that mitochondrial rDNA may encode small bioactive peptides.

Study Information

Provider

pubmed

Year

2019

Date

2019-06-24T00:00:00.000Z

DOI

10.1016/j.ygeno.2019.06.026

Citations

7

References

49