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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. 
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The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...
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Translocation of Proteins into the Mitochondria01:19

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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
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The Proteasome01:13

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Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast
11:04

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast

Published on: June 23, 2018

Protein:protein aggregation induced by protein oxidation.

Hamid Mirzaei1, Fred Regnier

  • 1Department of Chemistry, Purdue University, West Lafayette, IN 47907-2084, USA.

Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences
|September 2, 2008
PubMed
Summary

Oxidative stress damages cells, causing protein aggregation. This study identified 25 proteins forming aggresomes in yeast, offering insights into aging and disease mechanisms.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Proteomics

Background:

  • Reactive oxygen species (ROS) can overwhelm cellular defenses, leading to damage and protein aggregation.
  • Protein aggregates are implicated in various diseases and aging processes.

Purpose of the Study:

  • To investigate the dynamics of oxidative stress-induced protein aggregation.
  • To identify proteins that form aggregates in vivo under oxidative stress.

Main Methods:

  • Oxidation of model proteins and analysis via size exclusion chromatography (SEC).
  • Hydrogen peroxide stress in yeast, followed by LC/MS analysis of high molecular weight aggregates.
  • Differential labeling of aggregated proteins using isotope-coded N-acetoxysuccinamide.

Main Results:

  • Oxidation causes protein aggregation in stages, with fragments also forming aggregates.
  • Twenty-five proteins were identified as part of high molecular weight aggresomes in stressed yeast.
  • Fifteen of these aggresome proteins showed evidence of carbonylation.

Conclusions:

  • The study elucidates the multi-stage process of oxidative stress-induced protein aggregation.
  • Identification of aggresome components provides potential targets for understanding and treating age-related diseases.