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Study · In vitro (cells) · 2018

6 results

Humanin is an endogenous activator of chaperone-mediated autophagy.

Gong Z, Tasset I, Diaz A, Anguiano J, Tas E, Cui L, Kuliawat R, Liu H, Kühn B, Cuervo AM, Muzumdar R

The Journal of cell biology29 Nov 2017Cited by 85 (Europe PMC)

PMID29187525 (opens in a new tab)PMCIDPMC5800795 (opens in a new tab)DOI10.1083/jcb.201606095 (opens in a new tab)PepBankPUB-29187525
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Summary

The text of this summary is not shown here, because the article license does not allow reuse. Read it at the source (opens in a new tab)

Text rights: CC BY-NC. Results still quote short attributed sentences.

Results from this study6

5 results from studies that gave the peptide. No result from this study comes from people.

  1. 01LabIn vitro (cells)Mechanism

    In cells, Humanin directly activated chaperone-mediated autophagy by increasing substrate binding and translocation into lysosomes.

    In plain wordsIn cells, humanin switched on a cell cleanup process by increasing substrate binding and movement into lysosomes.

    Peptide
    Humanin
    Outcome
    IncreaseCMA substrate binding and translocation into lysosomes
    Study

    n: not reported in source

    Fibroblasts, cardiomyoblasts, neuronal cells, primary cardiomyocytes
    Outcome group
    Receptor activity and mechanism · Aging and longevity
    Studied dose
    Dose not stated

    Source sentences

    Summary
    In this study, we demonstrate that HN directly activates CMA by increasing substrate binding and translocation into lysosomes.
  2. 02LabIn vitro (cells)Efficacy outcome

    The humanin analogue HNG protected fibroblasts, cardiomyoblasts, neuronal cells and primary cardiomyocytes from stressor-induced cell death.

    In plain wordsIn cells, a humanin analogue protected several cell types from stress-induced death.

    Peptide
    Humanin
    Outcome
    IncreaseProtection from stressor-induced cell death
    Study

    n: not reported in source

    Fibroblasts, cardiomyoblasts, neuronal cells, primary cardiomyocytes
    Outcome group
    Neuroprotection · Whole body
    Studied dose
    Dose not stated

    Source sentences

    Summary
    The potent HN analogue HNG protects from stressor-induced cell death in fibroblasts, cardiomyoblasts, neuronal cells, and primary cardiomyocytes.
  3. 03LabIn vitro (cells)Mechanism

    The protective effects of HNG were lost in CMA-deficient cells.

    In plain wordsIn cells lacking the cleanup process CMA, the humanin analogue no longer protected the cells.

    Peptide
    Humanin
    Outcome
    No significant changeHNG protection in CMA-deficient cells
    Study

    n: not reported in source

    Fibroblasts, cardiomyoblasts, neuronal cells, primary cardiomyocytes
    Outcome group
    Receptor activity and mechanism · Whole body
    Studied dose
    Dose not stated

    Source sentences

    Summary
    The protective effects are lost in CMA-deficient cells, suggesting that they are mediated through the activation of CMA.
  4. 04LabIn vitro (cells)Mechanism

    Inhibition of HSP90 blocked the effect of HNG on substrate translocation.

    In plain wordsWhen HSP90 was blocked, the humanin analogue no longer increased substrate movement into lysosomes.

    Peptide
    Humanin
    Outcome
    No significant changeHNG effect on substrate translocation under HSP90 inhibition
    Study

    n: not reported in source

    Fibroblasts, cardiomyoblasts, neuronal cells, primary cardiomyocytes
    Outcome group
    Receptor activity and mechanism · Aging and longevity
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Inhibition of HSP90 blocks the effect of HNG on substrate translocation and abolishes the cytoprotective effects.
  5. 05LabIn vitro (cells)Mechanism

    Inhibition of HSP90 abolished the cytoprotective effects of HNG.

    In plain wordsWhen HSP90 was blocked, the humanin analogue no longer protected cells.

    Peptide
    Humanin
    Outcome
    No significant changeHNG cytoprotection under HSP90 inhibition
    Study

    n: not reported in source

    Fibroblasts, cardiomyoblasts, neuronal cells, primary cardiomyocytes
    Outcome group
    Neuroprotection · Whole body
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Inhibition of HSP90 blocks the effect of HNG on substrate translocation and abolishes the cytoprotective effects.

Natural levels measured1

These results measure the body's own peptide. Nobody was given the peptide. They are not evidence about taking it. They are left out of key results, evidence counts and charts.

  1. 06LabEndogenous levelIn vitro (cells)Mechanism

    A fraction of endogenous HN was present at the cytosolic side of the lysosomal membrane, where it interacted with HSP90 and stabilised chaperone binding to CMA substrates.

    In plain wordsThe body's own humanin sits at the lysosome surface, where it works with the chaperone HSP90.

    Peptide
    Humanin
    Outcome
    Not applicableEndogenous HN at the lysosomal membrane and HSP90 interaction
    Study

    n: not reported in source

    Fibroblasts, cardiomyoblasts, neuronal cells, primary cardiomyocytes
    Outcome group
    Receptor activity and mechanism · Aging and longevity

    Source sentences

    Summary
    We identified that a fraction of endogenous HN is present at the cytosolic side of the lysosomal membrane, where it interacts with heat shock protein 90 (HSP90) and stabilizes binding of this chaperone to CMA substrates as they bind to the membrane.

    This result measures the body's own Humanin. Nobody was given the peptide. It is not evidence about taking it.

AI wrote and checked these results. AI can make mistakes, so check important results against the source.

Version history

PepBank keeps every version of the data on this study. Status changes from Retraction Watch, Europe PMC and Crossref are listed with their source.

  1. Version 2Current

    13 Oct 2026, 21:44 UTC

    Study results updated

  2. Version 1

    13 Oct 2026, 16:31 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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