Related Experiment Video

Updated: Jul 18, 2026

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils
15:04

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Published on: September 28, 2019

[Cytotoxicity of amyloid fibrils of X-protein]

L G Marsagishvili, M D Shpagina, Iu V Shatalin

    Biofizika
    |November 30, 2006
    PubMed

    Insights

    Tetracycline disassembles X-protein amyloid fibrils and protects polymorphonuclear leukocytes from cell death. This demonstrates tetracycline

    Area of Science:

    • Biochemistry
    • Cell Biology
    • Pharmacology

    Context:

    • Amyloid fibrils are known to induce cell death.
    • Tetracycline inhibits amyloid fibril formation and disassembles pre-formed fibrils.
    • Sarcomeric cytoskeletal proteins, including titin family members (X-, C-, and H-proteins), can form amyloid fibrils in vitro.

    Purpose:

    • To investigate the cytotoxic effects of X-protein amyloids on polymorphonuclear leukocytes.
    • To evaluate the efficacy of tetracycline in disaggregating X-protein amyloid fibrils and mitigating their cytotoxic effects.
    • To explore the potential of this model system for assessing anti-amyloidosis drug effectiveness.

    Summary:

    • The viability of polymorphonuclear leukocytes exposed to X-protein amyloids was found to be dependent on both amyloid concentration and incubation time.
    • Tetracycline effectively disaggregated X-protein amyloid fibrils.
    • Tetracycline treatment eliminated the cytotoxic effect of X-protein amyloids, with no observed toxicity and even an increase in cell viability.

    Impact:

    • This study highlights tetracycline's potential in combating amyloid cytotoxicity.
    • The findings suggest a novel approach for evaluating drugs aimed at preventing or treating amyloidosis.
    • Demonstrates the therapeutic potential of targeting amyloid structures with existing antibiotics.

    More Related Videos

    Rapid Generation of Amyloid from Native Proteins In vitro05:48

    Rapid Generation of Amyloid from Native Proteins In vitro

    Published on: December 5, 2013

    Amyloid and the Cross-Beta Architecture09:06

    Amyloid and the Cross-Beta Architecture

    Published on: February 13, 2026

    Related Concept Videos

    Amyloid Fibrils03:03

    Amyloid Fibrils

    Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
    Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
    Amyloid Fibrils03:03

    Amyloid Fibrils

    Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
    Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...