Humanin (Bioregulator)

Research Overview

1. Structure and Molecular Characteristics

Humanin is a naturally occurring peptide encoded within the mitochondrial 16S ribosomal RNA gene [1]. Its canonical sequence is Met-Ala-Pro-Arg-Gly-Phe-Ser-Cys-Leu-Leu-Leu-Leu-Thr-Ser-Glu-Ile-Asp-Leu-Pro-Val-Lys-Arg-Arg-Ala (HNG variant contains Ser14Gly substitution) [1][2]. The peptide has a molecular weight of ~2.6 kDa and is classified as a mitochondrial-derived peptide (MDP), distinct from nuclear-encoded peptides due to its origin [2].

2. Apoptosis and Cellular Stress Research

Humanin has been extensively studied for its ability to modulate apoptosis in experimental models. It binds pro-apoptotic proteins such as Bax, tBid, and IGFBP-3, preventing mitochondrial outer membrane permeabilization and subsequent cytochrome c release [3]. These anti-apoptotic mechanisms have made Humanin a useful research tool in studies of programmed cell death and oxidative stress regulation [3].

In cell culture and animal models, Humanin has been shown to reduce oxidative damage and support mitochondrial function, highlighting its role as a stress-response peptide [4].

3. Neurobiology Research

Experimental studies demonstrate that Humanin influences neuronal survival, differentiation, and synaptic plasticity [5]. In models of neurodegeneration, Humanin reduced neuronal apoptosis by modulating JAK2/STAT3 and ERK1/2 signaling pathways [5]. Furthermore, Humanin enhanced neuronal resistance to excitotoxicity and amyloid aggregation in vitro, making it a valuable peptide for probing mechanisms of neuroprotection [5].

4. Metabolic and Endocrine Research

Humanin is expressed in multiple tissues including hypothalamus, skeletal muscle, and testis. Research indicates that it modulates insulin sensitivity and glucose metabolism in experimental systems [6]. In rodent studies, Humanin improved pancreatic β-cell survival and insulin secretion under stress conditions [6]. These findings support its role as a mitochondrial-derived regulator in metabolic signaling.

• Aging and Gerontology Research

Circulating Humanin levels decline with age in both humans and animal models [7]. This decline has made it a focal point of gerontology research, as mitochondrial peptides are increasingly recognized as contributors to aging-related cellular regulation. Humanin’s ability to regulate apoptosis and stress responses links it directly to age-associated cellular decline [7].

Referenced Citations

1. PubChem. Humanin. CID 16132373. PubChem
2. Hashimoto Y, et al. Discovery of a novel neuroprotective peptide, Humanin, encoded in the mitochondrial 16S rRNA. Proc Natl Acad Sci USA. 2001. PubMed
3. Guo B, et al. Humanin peptide inhibits Bax-induced apoptosis by binding to pro-apoptotic proteins. Nature. 2003. PubMed
4. Klein LE, et al. Humanin suppresses oxidative stress and preserves mitochondrial function. Exp Gerontol. 2013. PubMed
5. Matsuoka M, et al. Neuroprotective properties of Humanin in neuronal cell culture models. J Neurosci Res. 2002. PubMed
6. Muzumdar R, et al. Humanin regulates insulin sensitivity and β-cell survival in rodents. Diabetes. 2009. PubMed
7. Cobb LJ, et al. Plasma Humanin levels decline with age and correlate with health status. Proc Natl Acad Sci USA. 2016. PubMed

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