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Study · In vitro (cell-free) · 2020

5 results

Humanin selectively prevents the activation of pro-apoptotic protein BID by sequestering it into fibers.

Morris DL, Johnson S, Bleck CKE, Lee DY, Tjandra N

The Journal of biological chemistry26 Oct 2020Cited by 26 (Europe PMC)

PMID33106313 (opens in a new tab)PMCIDPMC11843584 (opens in a new tab)DOI10.1074/jbc.ra120.013023 (opens in a new tab)PepBankPUB-33106313
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Summary

Members of the B-cell lymphoma (BCL-2) protein family regulate mitochondrial outer membrane permeabilization (MOMP), a phenomenon in which mitochondria become porous and release death-propagating complexes during the early stages of apoptosis. Pro-apoptotic BCL-2 proteins oligomerize at the mitochondrial outer membrane during MOMP, inducing pore formation. Of current interest are endogenous factors that can inhibit pro-apoptotic BCL-2 mitochondrial outer membrane translocation and oligomerization. A mitochondrial-derived peptide, Humanin (HN), was reported being expressed from an alternate ORF in the mitochondrial genome and inhibiting apoptosis through interactions with the pro-apoptotic BCL-2 proteins. Specifically, it is known to complex with BAX and BID. We recently reported the fibrillation of HN and BAX into β-sheets. Here, we detail the fibrillation between HN and BID. These fibers were characterized using several spectroscopic techniques, protease fragmentation with mass analysis, and EM. Enhanced fibrillation rates were detected with rising temperatures or pH values and the presence of a detergent. BID fibers are similar to those produced using BAX; however, the structures differ in final conformations of the BCL-2 proteins. BID fibers display both types of secondary structure in the fiber, whereas BAX was converted entirely to β-sheets. The data show that two distinct segments of BID are incorporated into the fiber structure, whereas other portions of BID remain solvent-exposed and retain helical structure. Similar analyses show that anti-apoptotic BCL-xL does not form fibers with humanin. These results support a general mechanism of sequestration of pro-apoptotic BCL-2 proteins into fibers by HN to inhibit MOMP.
CC BYText from Europe PMC. Highlighted sentences are the source of results.

Results from this study5

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

  1. 01LabIn vitro (cell-free)Mechanism

    In cell-free tests, humanin formed fibers with the pro-apoptotic protein BID.

    In plain wordsIn lab tests with purified proteins, humanin formed fibers with the cell-death protein BID.

    Peptide
    Humanin
    Outcome
    Not applicableFibrillation of humanin with BID
    Study

    n: not reported in source

    Cell-free protein assays
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Here, we detail the fibrillation between HN and BID.
    1 context sentence
    Summary · context
    These fibers were characterized using several spectroscopic techniques, protease fragmentation with mass analysis, and EM.
  2. 02LabIn vitro (cell-free)Mechanism

    In cell-free tests, fibrillation of humanin with BID was faster at rising temperatures or pH values and in the presence of a detergent.

    In plain wordsIn lab tests, humanin and the BID protein formed fibers faster at higher temperature or pH and with a detergent.

    Peptide
    Humanin
    Outcome
    IncreaseFibrillation rate with temperature, pH and detergent
    Study

    n: not reported in source

    Cell-free protein assays
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Enhanced fibrillation rates were detected with rising temperatures or pH values and the presence of a detergent.
  3. 03LabIn vitro (cell-free)Mechanism

    In cell-free tests, BID fibers with humanin were similar to BAX fibers but differed in the final conformations of the BCL-2 proteins. BID fibers held both secondary structure types, while BAX was converted entirely to beta-sheets.

    In plain wordsIn lab tests, humanin fibers with BID were similar to those with BAX, but the protein shapes in the fibers differed.

    Peptide
    Humanin
    Outcome
    Not applicableBID fibers compared with BAX fibers
    Study

    n: not reported in source

    Cell-free protein assays
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    BID fibers are similar to those produced using BAX; however, the structures differ in final conformations of the BCL-2 proteins. BID fibers display both types of secondary structure in the fiber, whereas BAX was converted entirely to β-sheets.
  4. 04LabIn vitro (cell-free)Mechanism

    In cell-free tests, two distinct segments of BID were incorporated into the fiber structure, while other portions of BID stayed solvent-exposed and helical.

    In plain wordsIn lab tests, two parts of the BID protein joined the humanin fiber, while other parts stayed outside it.

    Peptide
    Humanin
    Outcome
    Not applicableBID segments incorporated into the fiber
    Study

    n: not reported in source

    Cell-free protein assays
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    The data show that two distinct segments of BID are incorporated into the fiber structure, whereas other portions of BID remain solvent-exposed and retain helical structure.
  5. 05LabIn vitro (cell-free)Mechanism

    In cell-free tests, anti-apoptotic BCL-xL did not form fibers with humanin.

    In plain wordsIn lab tests, the protein BCL-xL did not form fibers with humanin.

    Peptide
    Humanin
    Outcome
    No significant changeFibrillation of humanin with BCL-xL
    Study

    n: not reported in source

    Cell-free protein assays
    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Similar analyses show that anti-apoptotic BCL-xL does not form fibers with humanin.

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

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