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Study · Animal study (in vivo) · caenorhabditis elegans · 2017

8 results

Humanin Specifically Interacts with Amyloid-β Oligomers and Counteracts Their in vivo Toxicity.

Romeo M, Stravalaci M, Beeg M, Rossi A, Fiordaliso F, Corbelli A, Salmona M, Gobbi M, Cagnotto A, Diomede L

Journal of Alzheimer's disease : JAD1 Jan 2017Cited by 26 (Europe PMC)

PMID28282805 (opens in a new tab)DOI10.3233/jad-160951 (opens in a new tab)PepBankPUB-28282805
Publisher pagePubMedAsk about this study
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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: Publisher copyright. Results still quote short attributed sentences.

Results from this study8

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

  1. 01AnimalAnimal study (in vivo)Efficacy outcome

    In transgenic C. elegans, both HN and HNG decreased the relative abundance of A11-positive prefibrillar oligomers.

    In plain wordsIn worms engineered to make Aβ, humanin and its derivative lowered the amount of A11-positive prefibrillar oligomers.

    Peptide
    Humanin
    Outcome
    DecreaseA11-positive prefibrillar oligomers
    Study

    Caenorhabditis elegansn: not reported in source

    transgenic strain with oligomer-driven Aβ toxicity
    Outcome group
    Neuroprotection · Nervous system and cognition
    Studied dose
    Dose not stated

    Source sentences

    Summary
    In vivo studies indicated that both HN and HNG decrease the relative abundance of A11-positive prefibrillar oligomers as well as OC-positive fibrillar oligomers and had similar protective effects.
    1 context sentence
    Summary · context
    Experiments were run in cell-free conditions and in vivo in a transgenic C. elegans strain in which the Aβ toxicity was specifically due to oligomeric species.
  2. 02AnimalAnimal study (in vivo)Efficacy outcome

    In transgenic C. elegans, both HN and HNG decreased the relative abundance of OC-positive fibrillar oligomers.

    In plain wordsIn worms engineered to make Aβ, humanin and its derivative lowered the amount of OC-positive fibrillar oligomers.

    Peptide
    Humanin
    Outcome
    DecreaseOC-positive fibrillar oligomers
    Study

    Caenorhabditis elegansn: not reported in source

    transgenic strain with oligomer-driven Aβ toxicity
    Outcome group
    Neuroprotection · Nervous system and cognition
    Studied dose
    Dose not stated

    Source sentences

    Summary
    In vivo studies indicated that both HN and HNG decrease the relative abundance of A11-positive prefibrillar oligomers as well as OC-positive fibrillar oligomers and had similar protective effects.
    1 context sentence
    Summary · context
    Experiments were run in cell-free conditions and in vivo in a transgenic C. elegans strain in which the Aβ toxicity was specifically due to oligomeric species.
  3. 03AnimalAnimal study (in vivo)Efficacy outcome

    In transgenic C. elegans, HN and HNG had similar protective effects.

    In plain wordsIn worms engineered to make Aβ, humanin and its derivative had similar protective effects.

    Peptide
    Humanin
    Outcome
    Not applicableProtective effects of HN versus HNG on Aβ toxicity
    Study

    Caenorhabditis elegansn: not reported in source

    transgenic strain with oligomer-driven Aβ toxicity
    Outcome group
    Neuroprotection · Nervous system and cognition
    Studied dose
    Dose not stated

    Source sentences

    Summary
    In vivo studies indicated that both HN and HNG decrease the relative abundance of A11-positive prefibrillar oligomers as well as OC-positive fibrillar oligomers and had similar protective effects.
    1 context sentence
    Summary · context
    Experiments were run in cell-free conditions and in vivo in a transgenic C. elegans strain in which the Aβ toxicity was specifically due to oligomeric species.
  4. 04AnimalAnimal study (in vivo)Efficacy outcome

    In transgenic C. elegans, HNG caused a marked decrease of total Aβ levels.

    In plain wordsIn worms engineered to make Aβ, the humanin derivative HNG markedly lowered total Aβ.

    Peptide
    Humanin
    Outcome
    DecreaseTotal Aβ levels with HNG
    Study

    Caenorhabditis elegansn: not reported in source

    transgenic strain with oligomer-driven Aβ toxicity
    Outcome group
    Neuroprotection · Nervous system and cognition
    Studied dose
    Dose not stated

    Source sentences

    Summary
    However, while HN possibly decreased the oligomers by promoting their assembly into larger aggregates, the reduction of oligomers caused by HNG can be ascribed to a marked decrease of the total Aβ levels, likely the consequence of the HNG-induced overexpression of the Aβ-degrading enzyme neprilysin.
    1 context sentence
    Summary · context
    Experiments were run in cell-free conditions and in vivo in a transgenic C. elegans strain in which the Aβ toxicity was specifically due to oligomeric species.
  5. 05AnimalAnimal study (in vivo)Mechanism

    In transgenic C. elegans, HNG-induced overexpression of the Aβ-degrading enzyme neprilysin was proposed as the likely cause of lower total Aβ levels.

    In plain wordsIn worms engineered to make Aβ, the authors suggest HNG raised neprilysin, an enzyme that breaks down Aβ.

    Peptide
    Humanin
    Outcome
    IncreaseNeprilysin expression with HNG
    Study

    Caenorhabditis elegansn: not reported in source

    transgenic strain with oligomer-driven Aβ toxicity
    Outcome group
    Receptor activity and mechanism · Nervous system and cognition
    Studied dose
    Dose not stated

    Source sentences

    Summary
    However, while HN possibly decreased the oligomers by promoting their assembly into larger aggregates, the reduction of oligomers caused by HNG can be ascribed to a marked decrease of the total Aβ levels, likely the consequence of the HNG-induced overexpression of the Aβ-degrading enzyme neprilysin.
    1 context sentence
    Summary · context
    Experiments were run in cell-free conditions and in vivo in a transgenic C. elegans strain in which the Aβ toxicity was specifically due to oligomeric species.
  6. 06LabIn vitro (cell-free)Activity measurement

    In a cell-free thioflavin-T assay, both HN and HNG delayed the formation of Aβ42 fibrils.

    In plain wordsIn lab tests, humanin and its derivative slowed the formation of Aβ42 fibrils.

    Peptide
    Humanin
    Outcome
    DecreaseDelay of Aβ42 fibril formation
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Nervous system and cognition
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Thioflavin-T assay indicated that both HN and HNG delay the formation and reduce the final amount of Aβ42 fibrils.
    1 context sentence
    Summary · context
    Experiments were run in cell-free conditions and in vivo in a transgenic C. elegans strain in which the Aβ toxicity was specifically due to oligomeric species.
  7. 07LabIn vitro (cell-free)Activity measurement

    In a cell-free thioflavin-T assay, both HN and HNG reduced the final amount of Aβ42 fibrils.

    In plain wordsIn lab tests, humanin and its derivative lowered the final amount of Aβ42 fibrils.

    Peptide
    Humanin
    Outcome
    DecreaseFinal amount of Aβ42 fibrils
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Nervous system and cognition
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Thioflavin-T assay indicated that both HN and HNG delay the formation and reduce the final amount of Aβ42 fibrils.
    1 context sentence
    Summary · context
    Experiments were run in cell-free conditions and in vivo in a transgenic C. elegans strain in which the Aβ toxicity was specifically due to oligomeric species.
  8. 08LabIn vitro (cell-free)Mechanism

    In surface plasmon resonance studies, HN and HNG interacted with Aβ42 oligomers and favored the formation of amorphous larger assemblies.

    In plain wordsIn lab tests, humanin and its derivative bound Aβ42 oligomers and pushed them into larger, shapeless clumps.

    Peptide
    Humanin
    Outcome
    Not applicableInteraction with Aβ42 oligomers
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Nervous system and cognition
    Studied dose
    Dose not stated

    Source sentences

    Summary
    In vitro surface plasmon resonance studies indicated that they interact with Aβ42 oligomers favoring the formation of amorphous larger assemblies, observed with turbidity and electron microscopy.
    1 context sentence
    Summary · context
    Experiments were run in cell-free conditions and in vivo in a transgenic C. elegans strain in which the Aβ toxicity was specifically due to oligomeric species.

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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