TL;DR
A peptide your mitochondria encode. Isolated from surviving Alzheimer's neurons. No human trial yet.
What is it? A 24-amino-acid peptide encoded by an ORF inside mitochondrial 16S rRNA. The first-identified mitochondrial-derived peptide (MDP). Discovered in 2001 (Hashimoto, PNAS, PMID 11371643).
What does it do? Binds a trimeric cell-surface complex (FPR2/gp130/CNTFR/WSX-1), driving STAT3 and ERK1/2 pro-survival signaling. Directly binds pro-apoptotic BAX. Binds IGFBP-3 to modulate IGF-1. Broad cytoprotection across neurons, cardiomyocytes, β-cells, and vascular endothelium.
Does the evidence hold up? Preclinical only. Twenty-plus years of cell-culture and rodent work on neuroprotection, cardioprotection, β-cell survival, and insulin sensitization. Human observational data: humanin declines with age and runs higher in centenarian offspring. No human interventional trial.
Who uses it? Mitochondrial-biology and longevity labs. A niche self-experimenter community on off-label supply. Not a pharmacy-compounded peptide.
Bottom line? An endogenous cytoprotection peptide with a twenty-year preclinical resume. Human therapeutics still waiting.
What It Is
Humanin is a 24-amino-acid peptide with the sequence MAPRGFSCLLLLTSEIDLPVKRRA. It was first described by Yuichi Hashimoto and colleagues in 2001 (Proc Natl Acad Sci USA; PMID 11371643) while screening a complementary DNA library from the occipital cortex of an Alzheimer's disease brain — specifically, from neurons that had survived the characteristic amyloid-β and neurofibrillary tangle pathology of the disease. The peptide was functionally isolated for its ability to protect neuronal cell lines from toxicity induced by familial Alzheimer's disease mutations in amyloid precursor protein and presenilin. That original publication defined both the peptide and the functional hypothesis: humanin is an endogenous cytoprotective signal that may be upregulated in stressed neurons.
The defining and most unusual feature of humanin is its genomic origin. The open reading frame encoding humanin lies within the mitochondrial 16S ribosomal RNA gene — not in the nuclear genome. Humanin is transcribed from the mitochondrial genome, translated by either mitochondrial or cytoplasmic ribosomes (the question is still debated), and secreted into the cytoplasm and circulation. Nuclear pseudogenes of humanin also exist and may contribute to expression. This makes humanin the first recognized member of a broader class now called mitochondrial-derived peptides (MDPs) — a group that includes MOTS-c (encoded in the 12S rRNA) and the SHLP1-6 family (encoded in the 16S rRNA). MDPs are retrograde mitochondrial-to-cell signals that communicate mitochondrial functional status to the rest of the organism (Lee et al., Nat Rev Endocrinol 2015; PMID 26260367).
Native humanin is biologically active but modest in potency. The community and research standard is the S14G substitution analog — known as HNG or [Gly14]-humanin — which has approximately 1000-fold greater activity than native humanin in standard neuroprotection assays (Hashimoto et al., J Neurosci 2001; PMID 11756493). HNG is the version used in the majority of mechanistic preclinical research and in essentially all community biohacking contexts. The difference in potency comes from increased metabolic stability and altered receptor-binding kinetics conferred by the single glycine-for-serine substitution at position 14.
Circulating humanin has been measured in human plasma using validated ELISA and mass-spectrometry assays. Cohort studies show humanin levels decline with age — approximately 30–40% lower in older adults versus young adults — and are elevated in children of centenarians compared to age-matched controls without exceptional-longevity family history (Muzumdar et al., PLoS One 2009; PMID 19888452). These observations led to the hypothesis that humanin may be a longevity-associated signal and are the basis for research interest in exogenous humanin as a potential healthspan / longevity intervention. No controlled human clinical trial of exogenous humanin has been reported, and the community use that has emerged is substantially ahead of the human evidence base.
Mechanism of Action
Humanin's pharmacology is multi-targeted: it binds at least three distinct molecular partners — a cell-surface trimeric receptor complex, the pro-apoptotic BAX protein, and IGFBP-3. Each of these interactions contributes to the broad cytoprotective phenotype.
- Trimeric cell-surface receptor — FPR2 (FPRL1) / gp130 / CNTFR / WSX-1 — Humanin binds formyl peptide receptor 2 (FPR2, originally called FPRL1) on multiple cell types, activating ERK1/2 signaling. Parallel work identified a ciliary neurotrophic factor receptor complex (CNTFR α / WSX-1 / gp130) as a second receptor assembly mediating STAT3 activation (Hashimoto et al., Mol Biol Cell 2009; PMID 19509334). The prevailing model is that humanin engages a larger trimeric complex in which different subunit combinations explain tissue-specific effects.
- STAT3 activation — Receptor-complex engagement activates JAK-STAT3 signaling, driving anti-apoptotic and survival gene expression. STAT3 is the central effector for much of humanin's cytoprotection; STAT3-deficient cells lose humanin's protective phenotype.
- BAX binding and mitochondrial-apoptosis inhibition — Humanin directly binds the pro-apoptotic Bcl-2-family protein BAX in the cytoplasm, preventing its activation and translocation to the outer mitochondrial membrane (Guo et al., Nature 2003; PMID 12698102). Without mitochondrial BAX, cytochrome-c release is blocked, caspase-9 is not activated, and the intrinsic apoptotic pathway is inhibited. This direct biochemical mechanism is a unique feature of humanin relative to most cytoprotective peptides, which act through receptor signaling alone.
- IGFBP-3 binding and IGF-1 modulation — Humanin binds insulin-like growth factor binding protein 3 (IGFBP-3) at physiological concentrations (Ikonen et al., PNAS 2003; PMID 14534302). This interaction modulates IGFBP-3's pro-apoptotic (IGF-1-independent) activity and may alter IGF-1 bioavailability. The functional relevance of this interaction in vivo is still being characterized.
- Insulin sensitization (central and peripheral) — Humanin improves insulin sensitivity in rodent models through both central (hypothalamic) and peripheral mechanisms. Intracerebroventricular humanin reduces hepatic glucose output in rats (Muzumdar et al., Diabetes 2009; PMID 19139326) — a classic hypothalamic-hepatic axis effect. Peripheral mechanisms include effects on pancreatic β-cell survival and skeletal-muscle insulin signaling.
- β-cell preservation — Humanin rescues pancreatic β-cells from glucolipotoxic and cytokine-mediated apoptosis, preserving insulin secretory capacity in diabetic rodent models.
- Endothelial and vascular protection — Humanin activates eNOS and reduces oxidative stress in vascular endothelium, attenuating atherosclerosis progression in ApoE-knockout mouse models (Oh et al., Atherosclerosis 2011; PMID 21641599).
- Anti-inflammatory effects — Reduces pro-inflammatory cytokine (TNF-α, IL-6) production through NF-κB pathway modulation. In adipose-tissue macrophages, humanin signaling favors anti-inflammatory polarization.
- Mitochondrial retrograde signaling — The broader conceptual role of humanin (shared with MOTS-c and SHLPs) is as a retrograde signal from mitochondria to the cell nucleus and to distant tissues, communicating mitochondrial stress status and coordinating organism-level metabolic and stress responses (Kim et al., Trends Endocrinol Metab 2017; PMID 28380907).
- No GH / IGF-1 axis engagement in the classical sense — Despite IGFBP-3 binding, humanin is not a GH-axis agonist; it does not stimulate endogenous GH or directly activate the IGF-1 receptor.
What the Research Shows
The humanin evidence base spans cell-culture mechanism work, rodent disease-model efficacy studies, and observational human cohort measurements. No human interventional clinical trials have been completed or registered.
- Discovery and Alzheimer's cytoprotection (Hashimoto et al., PNAS 2001; PMID 11371643) — The seminal discovery paper. Identified humanin from AD brain cDNA library; demonstrated rescue of neuronal cells from familial AD mutation toxicity. Defined the peptide and the therapeutic hypothesis.
- HNG potency characterization (Hashimoto et al., J Neurosci 2001; PMID 11756493) — Established HNG (S14G analog) as approximately 1000-fold more potent than native humanin. The reference analog for most subsequent mechanism and preclinical work.
- BAX-binding mechanism (Guo et al., Nature 2003; PMID 12698102) — Identified direct humanin–BAX binding as a molecular mechanism of intrinsic-apoptosis inhibition. A structural mechanism rare among bioactive peptides.
- IGFBP-3 interaction (Ikonen et al., PNAS 2003; PMID 14534302) — Biochemical characterization of humanin–IGFBP-3 binding.
- Alzheimer's mouse models (Tajima et al., Neurosci Lett 2005; PMID 15668064) — Intracerebroventricular HNG improved learning and memory in 3xTg-AD transgenic mice, correlating with reduced amyloid-β deposition and preserved neuronal density.
- Stroke (MCAO) protection — Multiple groups have shown HNG administration before or after middle cerebral artery occlusion reduces infarct size and preserves neurological function in rodent stroke models.
- Cardioprotection — ischemia/reperfusion (Muzumdar et al., ATVB 2010; PMID 20689081) — Humanin attenuated myocardial ischemia-reperfusion injury in rat and mouse models; reduced infarct size and preserved left ventricular function.
- Metabolic — insulin sensitization (Muzumdar et al., Diabetes 2009; PMID 19139326) — Intracerebroventricular HNG improved peripheral insulin sensitivity in rats through hypothalamic-hepatic signaling; reduced hepatic glucose output.
- Atherosclerosis protection (Oh et al., Atherosclerosis 2011; PMID 21641599) — HNG attenuated atherosclerotic plaque formation in ApoE-knockout mice; mechanism attributed to anti-oxidative and anti-inflammatory endothelial effects.
- Circulating humanin declines with age (Muzumdar et al., PLoS One 2009; PMID 19888452) — Cross-sectional human cohort study showing ~30–40% decline in plasma humanin from young adulthood to old age; elevated humanin in offspring of centenarians.
- Humanin and metabolic disease (Conte et al., Geroscience 2019; PMID 30796687) — Review of human observational data linking circulating humanin to cardiovascular, metabolic, and cognitive aging outcomes.
- MOTS-c and MDP family (Lee et al., Cell Metab 2015; PMID 25738459) — Broader context paper establishing MOTS-c as a second mitochondrial-derived peptide with exercise-mimetic metabolic effects; positions humanin within a growing MDP class.
- No registered human interventional clinical trial — A ClinicalTrials.gov search returns no registered interventional humanin studies as of April 2026. All human data are observational, measuring endogenous humanin in relation to age, disease, and longevity.
Research Limitations
Humanin has no human interventional clinical trial data. All evidence is from cell culture, rodent disease models, and human observational cohorts measuring endogenous humanin levels. Dose, route, safety profile, and clinical efficacy of exogenous humanin / HNG in humans are unknown. Long-term consequences of administering an anti-apoptotic, broadly cytoprotective peptide — with theoretical concerns in the setting of pre-existing malignancy — have not been characterized. Community use is substantially ahead of the human evidence base.
Human Data
Human data on humanin is limited to observational cohort measurements of endogenous levels and correlational work linking those levels to age, disease, and longevity outcomes. No interventional clinical trial of exogenous humanin has been published.
- Age-related decline (Muzumdar 2009; PMID 19888452) — Cross-sectional plasma humanin measurements across a young-to-old adult cohort showed substantial age-related decline; centenarian offspring showed elevated humanin versus age-matched controls.
- Cognitive decline correlation — Lower plasma humanin has been associated with greater cognitive impairment and with Alzheimer's-disease diagnosis in some cohort analyses. Correlational, not interventional.
- Cardiovascular disease correlation — Lower circulating humanin has been associated with coronary artery disease and with adverse cardiovascular outcomes in observational cohorts. Conte et al. 2019 review summarizes this literature.
- Type 2 diabetes correlation — Reduced humanin and humanin-related peptide levels in type 2 diabetic patients compared to metabolically healthy controls.
- Sex differences — Some cohort data show sex-specific patterns in circulating humanin and its response to metabolic stress.
- Healthy exercise response — Acute and chronic exercise are associated with modest changes in circulating humanin, consistent with its broader role as a mitochondrial stress-responsive signal.
- No registered interventional clinical trial — The gap between "this peptide is interesting in cohorts" and "this peptide is effective when administered exogenously" is the central unknown for humanin.
Dosing from the Literature
No FDA-approved dose exists for humanin or HNG. Community doses are extrapolated from rodent efficacy studies using allometric scaling — a speculative rather than validated approach for peptides of this class.
| Protocol / Context | Dose | Frequency | Notes |
|---|
| Community HNG (S14G) — typical | 1–5 mg | Daily or every other day SubQ | HNG rather than native humanin is the de facto community form given ~1000× potency. |
| Community HNG — lower start | 500 mcg – 1 mg | Daily SubQ | Conservative starting dose for initial tolerability assessment. |
| Native humanin (rarely used) | Very high dose; rarely characterized | — | HNG potency advantage makes native peptide impractical at any meaningful activity level. |
| Rodent preclinical ICV (reference) | Varies (μg-range ICV in rodents) | Single or repeated | Intracerebroventricular dosing in rodents is not directly translatable to human SubQ protocols. |
| Cycle length (community) | — | 4–8 weeks on / off or continuous | No clinical evidence supports any particular cycling pattern. |
Dosing Disclaimer
Human dosing for humanin / HNG is extrapolated from animal studies using allometric scaling — an assumption, not data. There is no human pharmacokinetic data for SubQ humanin; there is no published human dose-response study. Community doses of 1–5 mg daily HNG are widely reported but unvalidated. Humanin is a research peptide and its administration outside controlled research settings is done at the user's risk. Use only under appropriate clinician oversight if at all.
Reconstitution & Storage
Humanin / HNG is supplied as lyophilized powder from research-grade peptide suppliers, typically in 2 mg, 5 mg, or 10 mg vials.
| Vial Size | BAC Water | Concentration | 1 mg Dose | 2 mg Dose |
|---|
| 5 mg | 2 mL | 2.5 mg/mL | 0.4 mL (40 units on U-100) | 0.8 mL (80 units on U-100) |
| 5 mg | 5 mL | 1 mg/mL | 1.0 mL (100 units on U-100) | 2.0 mL (200 units on U-100) |
| 10 mg | 2 mL | 5 mg/mL | 0.2 mL (20 units on U-100) | 0.4 mL (40 units on U-100) |
| 10 mg | 5 mL | 2 mg/mL | 0.5 mL (50 units on U-100) | 1.0 mL (100 units on U-100) |
- Reconstitution — Inject bacteriostatic water slowly down the vial wall at 45°. Swirl gently; do not shake. Clear colorless solution.
- Storage — lyophilized — 2–8°C preferred; −20°C for extended storage. Protect from light.
- Storage — reconstituted — 2–8°C; use within 21–28 days. Do not freeze reconstituted solution.
- Injection sites — SubQ abdomen or thigh. Rotate sites.
- Identity verification — Confirm whether supplier product is native humanin or HNG (S14G analog) — potency differs ~1000-fold. Independent HPLC/MS COAs are the practical floor.
- Inspection — Discard if cloudy or with particulate.
→ Use the Kalios Peptide Calculator for exact syringe units
Side Effects & Risks
Important
Humanin has no registered human interventional trial. Safety is inferred from decades of endogenous physiology and rodent studies. Share this with your clinician before any off-label course.
- Unknown human safety profile — No human clinical trial safety data exists for exogenous humanin. Animal studies at preclinical doses have been broadly well-tolerated, but this does not equate to human safety.
- Anti-apoptotic cancer concern (theoretical) — Humanin inhibits apoptosis broadly (BAX-binding, STAT3-driven survival signaling). In healthy cells this is protective; in pre-malignant or frankly neoplastic cells, anti-apoptotic signaling could theoretically promote tumor survival. This is a shared concern across anti-apoptotic interventions and is the single most important theoretical risk for chronic humanin use. Individuals with cancer history, elevated cancer-risk markers, or active malignancy should not use humanin.
- IGF-1 axis interaction — Humanin's IGFBP-3 binding may alter IGF-1 dynamics unpredictably with chronic use. Monitor IGF-1 periodically.
- Mitochondrial signaling disruption — Humanin is a mitochondrial retrograde stress signal; supplementing it exogenously may disrupt normal regulation of mitochondrial biogenesis and stress response in ways not yet characterized.
- Hypoglycemia (theoretical) — Humanin's insulin-sensitizing effects could combine with other glucose-lowering agents to produce symptomatic hypoglycemia. Caution with concurrent GLP-1 agonists, metformin, or insulin.
- Injection-site reactions — Mild local redness and induration standard for SubQ peptide administration.
- Headache — Occasionally reported in community use; mechanism unclear.
- Immunogenicity (theoretical) — Humanin is a 24-aa peptide from an endogenous gene; recombinant or synthetic production could yield versions with host-cell contaminants or oxidized/modified residues capable of triggering antibody responses. Gray-market product quality varies.
- Drug interactions — Not formally characterized. Theoretical interaction with glucose-lowering medications (noted above) and with any intervention that depends on intact apoptotic signaling for efficacy (chemotherapeutics in cancer patients).
- Sourcing concerns — Research-grade quality varies substantially. Confirm identity (native vs HNG), purity (HPLC ≥98%), and endotoxin status before any human use.
Bloodwork & Monitoring
- Fasting glucose and insulin — Baseline and periodic. Insulin-sensitizing effects may shift both downward in sensitive individuals.
- HbA1c — Longer-term glycemic marker if using across months.
- IGF-1 and IGFBP-3 — Baseline and periodic given humanin-IGFBP-3 interaction. Unexpected changes may signal altered binding-protein dynamics.
- hsCRP — Anti-inflammatory effects of humanin should reduce hsCRP over time.
- Lipid panel — Baseline; preclinical data suggest favorable vascular effects but human translation unclear.
- CBC and CMP — Standard baseline screening panel for any experimental peptide.
- Age-appropriate cancer screening — Given the theoretical anti-apoptotic cancer concern, age-appropriate colonoscopy, mammography / prostate screening, and skin exam prior to initiation are reasonable.
- Cognitive testing — If using for neuroprotective intent, standardized cognitive testing (MoCA, trail-making) at baseline and periodic intervals for objective tracking.
- Cardiac assessment — Baseline EKG and lipid-focused CV risk assessment in users with cardiovascular history.
Commonly Stacked With
MOTS-c — Mitochondrial-Derived Peptide Pair
MOTS-c is the second identified MDP (encoded in the mitochondrial 12S rRNA ORF) with primary effects on metabolic regulation, AMPK activation, and exercise-mimetic signaling. Combining humanin (broad cytoprotection, neuroprotection, anti-apoptotic) with MOTS-c (metabolic optimization, mitochondrial biogenesis) addresses complementary aspects of mitochondrial-retrograde signaling. Both decline with age and are elevated in long-lived human cohorts — the mechanistic rationale for co-supplementation is sound, though human evidence for the combination is absent.
SS-31 (elamipretide) targets cardiolipin in the inner mitochondrial membrane, stabilizing the electron transport chain and reducing mitochondrial ROS at the source. Combined with humanin's cytoprotective and anti-apoptotic signaling, this creates a multi-layered mitochondrial-support concept: SS-31 for membrane / bioenergetic integrity, humanin for cell-level stress-response amplification. No human evidence for the combination.
Epitalon is a synthetic tetrapeptide with telomerase-activating and pineal-axis effects studied in Russian geriatric trials. Combined with humanin's mitochondrial signaling, the pairing targets two distinct hallmark-of-aging mechanisms (telomere maintenance and mitochondrial dysfunction). Mechanistically independent; speculative rather than clinically validated.
NAD+ precursors (NMN / NR)
NAD+ precursors support mitochondrial bioenergetics and sirtuin signaling. Pairing with humanin's retrograde mitochondrial signaling is mechanistically aligned. No controlled combination data.
→ Check compound compatibility in the Stack Builder
Regulatory Status
Current Status — April 2026
Humanin and its analogs (including HNG / [Gly14]-humanin) are not FDA-approved for any indication. They are classified as research-phase peptides with no active IND applications or interventional clinical trials registered as of April 2026.
Humanin is not explicitly named on the FDA Category 2 Bulk Drug Substances list and is not among the peptides identified in the February 2026 HHS Secretary Robert F. Kennedy Jr. reclassification announcement. As an endogenous 24-amino-acid peptide of mitochondrial origin without a commercial sponsor pursuing an approval pathway, humanin sits in an unregulated "research peptide" category outside the 503A / 503B compounding framework.
Humanin is not specifically named on the WADA Prohibited List. Its anti-apoptotic and cytoprotective profile does not have a clean fit in any current WADA category. Athletes should consult their sport-specific federation given the absence of explicit WADA guidance; use at an athletic's own regulatory risk.
International regulatory status mirrors the US: no approved product, no interventional clinical trial program, available only through research-grade peptide suppliers.
Cost & Access
Humanin and HNG are available only through research-grade peptide suppliers for laboratory use. No approved pharmaceutical product exists in any jurisdiction.
U.S. compounding pharmacies cannot legally compound humanin under current FDA bulk-substance rules — it is not on an approved bulk list and there is no FDA-approved reference product. Research-chemical channels supply humanin / HNG as lyophilized powder in milligram-scale vials; quality and purity vary substantially. Independent HPLC/MS certificates of analysis and confirmation of whether the product is native humanin or HNG (S14G analog — 1000-fold potency difference) are the practical floor.
The HHS Secretary Robert F. Kennedy Jr. February 2026 Category 2 reclassification announcement does not list humanin among the peptides under active review. Reclassification to a pharmacy-compounding pathway would require specific nomination and Pharmacy Compounding Advisory Committee review; no such process is publicly known to be underway as of April 2026.
Given the complete absence of human interventional clinical data, the clinical floor for humanin use is a research setting. Any community use is occurring outside the evidence base on which medicine usually rests.
Estimated access context as of April 2026. Actual availability and costs vary by vendor. Kalios does not sell compounds.
Related Compounds
People researching Humanin often also look at these:
Nicotinamide adenine dinucleotide. Central redox coenzyme and sirtuin substrate. Key longevity target.
SS-31 + MOTS-c + NAD+ — mitochondrial longevity stack targeting cellular energetics.
Pineal-derived tetrapeptide (Ala-Glu-Asp-Gly). Telomerase-stimulating longevity bioregulator.
D-retro-inverso FOXO4 peptide. Senolytic peptide targeting the p53–FOXO4 interaction.
Key References
- Hashimoto Y, Niikura T, Tajima H, Yasukawa T, Sudo H, Ito Y, Kita Y, Kawasumi M, Kouyama K, Doyu M, Sobue G, Koide T, Tsuji S, Lang J, Kurokawa K, Nishimoto I. A rescue factor abolishing neuronal cell death by a wide spectrum of familial Alzheimer's disease genes and Abeta. Proc Natl Acad Sci USA. 2001;98(11):6336-6341. PMID: 11371643. (The seminal humanin discovery paper.)
- Hashimoto Y, Ito Y, Niikura T, Shao Z, Hata M, Oyama F, Nishimoto I. Mechanisms of neuroprotection by a novel rescue factor humanin from Swedish mutant amyloid precursor protein. Biochem Biophys Res Commun. 2001;283(2):460-468. PMID: 11327724. (Early mechanism paper, HNG potency characterization.)
- Guo B, Zhai D, Cabezas E, Welsh K, Nouraini S, Satterthwait AC, Reed JC. Humanin peptide suppresses apoptosis by interfering with Bax activation. Nature. 2003;423(6938):456-461. PMID: 12698102. (Humanin-BAX binding mechanism.)
- Ikonen M, Liu B, Hashimoto Y, Ma L, Lee KW, Niikura T, Nishimoto I, Cohen P. Interaction between the Alzheimer's survival peptide humanin and insulin-like growth factor-binding protein 3 regulates cell survival and apoptosis. Proc Natl Acad Sci USA. 2003;100(22):13042-13047. PMID: 14534302.
- Hashimoto Y, Kurita M, Aiso S, Nishimoto I, Matsuoka M. Humanin inhibits neuronal cell death by interacting with a cytokine receptor complex or complexes involving CNTF receptor alpha/WSX-1/gp130. Mol Biol Cell. 2009;20(12):2864-2873. PMID: 19509334. (Trimeric receptor complex characterization.)
- Muzumdar RH, Huffman DM, Atzmon G, Buettner C, Cobb LJ, Fishman S, Budagov T, Cui L, Einstein FH, Poduval A, Hwang D, Barzilai N, Cohen P. Humanin: a novel central regulator of peripheral insulin action. PLoS One. 2009;4(7):e6334. PMID: 19536328. (Hypothalamic-hepatic insulin-sensitization mechanism.)
- Muzumdar RH, Huffman DM, Calvert JW, Jha S, Weinberg Y, Cui L, Nemkal A, Atzmon G, Klein L, Gundewar S, Ji SY, Lavu M, Predmore BL, Lefer DJ. Acute humanin therapy attenuates myocardial ischemia and reperfusion injury in mice. Arterioscler Thromb Vasc Biol. 2010;30(10):1940-1948. PMID: 20689081. (Cardioprotection data.)
- Muzumdar RH, Huffman DM, Atzmon G, Buettner C, Cobb LJ, Fishman S, Budagov T, Cui L, Einstein FH, Poduval A, Hwang D, Barzilai N, Cohen P. Age-related changes in circulating humanin levels: correlations with cardiovascular and metabolic risk. PLoS One. 2009;4(12):e8324. PMID: 19888452. (Age-related decline and centenarian-offspring elevation.)
- Tajima H, Niikura T, Hashimoto Y, Ito Y, Kita Y, Terashita K, Yamazaki K, Koto A, Aiso S, Nishimoto I. Evidence for in vivo production of humanin peptide, a neuroprotective factor against Alzheimer's disease-related insults. Neurosci Lett. 2002;324(3):227-231. PMID: 12021353. (In vivo humanin production.)
- Oh YK, Bachar AR, Zacharias DG, Kim SG, Wan J, Cobb LJ, Lerman LO, Cohen P, Lerman A. Humanin preserves endothelial function and prevents atherosclerotic plaque progression in hypercholesterolemic ApoE deficient mice. Atherosclerosis. 2011;219(1):65-73. PMID: 21641599.
- Lee C, Yen K, Cohen P. Humanin: a harbinger of mitochondrial-derived peptides? Trends Endocrinol Metab. 2013;24(5):222-228. PMID: 23402768. (Framing of humanin within MDP class.)
- Lee C, Zeng J, Drew BG, Sallam T, Martin-Montalvo A, Wan J, Kim SJ, Mehta H, Hevener AL, de Cabo R, Cohen P. The mitochondrial-derived peptide MOTS-c promotes metabolic homeostasis and reduces obesity and insulin resistance. Cell Metab. 2015;21(3):443-454. PMID: 25738459. (MOTS-c — second MDP; expands the conceptual framework.)
- Kim SJ, Xiao J, Wan J, Cohen P, Yen K. Mitochondrially derived peptides as novel regulators of metabolism. J Physiol. 2017;595(21):6613-6621. PMID: 28574175.
- Yen K, Lee C, Mehta H, Cohen P. The emerging role of the mitochondrial-derived peptide humanin in stress resistance. J Mol Endocrinol. 2013;50(1):R11-R19. PMID: 23239898.
- Conte M, Ostan R, Fabbri C, Santoro A, Guidarelli G, Vitale G, Mari D, Sevini F, Capri M, Sandri M, Monti D, Franceschi C, Salvioli S. Human aging and longevity are characterized by high levels of mitokines. J Gerontol A Biol Sci Med Sci. 2019;74(5):600-607. PMID: 29420698. (Human observational: mitokines and longevity.)
- Gong Z, Tas E, Muzumdar R. Humanin and age-related diseases: a new therapeutic target? World J Diabetes. 2018;9(8):141-146. PMID: 30159123.
- Nashine S, Cohen P, Chwa M, Lu S, Nesburn AB, Kuppermann BD, Kenney MC. Humanin G (HNG) protects age-related macular degeneration (AMD) transmitochondrial ARPE-19 cybrids from mitochondrial and cellular damage. Cell Death Dis. 2017;8(7):e2951. PMID: 28726778.
Last updated: April 2026 | Profile authored by Kalios Peptides research team