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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. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...

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Consensus Brain-derived Protein, Extraction Protocol for the Study of Human and Murine Brain Proteome Using Both 2D-DIGE and Mini 2DE Immunoblotting
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Apolipoprotein-E forms dimers in human frontal cortex and hippocampus.

David A Elliott1, Glenda M Halliday, Brett Garner

  • 1Prince of Wales Medical Research Institute, Randwick NSW 2031, Australia.

BMC Neuroscience
|February 23, 2010
PubMed
Summary
This summary is machine-generated.

Apolipoprotein-E (apoE) dimers, specifically apoE3, were found in human brain tissue, differing from apoE4. These dimers are not post-mortem artifacts and may impact brain function.

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Enrichment of Detergent-insoluble Protein Aggregates from Human Postmortem Brain
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Enrichment of Detergent-insoluble Protein Aggregates from Human Postmortem Brain

Published on: October 24, 2017

Area of Science:

  • Neurobiology
  • Protein biochemistry
  • Alzheimer's disease research

Background:

  • Apolipoprotein-E (apoE) is crucial in neurobiology, with the apoE4 isoform linked to increased Alzheimer's disease (AD) risk.
  • ApoE3 and apoE2 form dimers in biological fluids, unlike apoE4, impacting cholesterol and amyloid-beta.
  • The presence of apoE dimers in brain tissue remained unexamined.

Purpose of the Study:

  • To investigate the occurrence and characteristics of apolipoprotein-E (apoE) dimers in human cortical and hippocampal tissues.
  • To determine if apoE dimer formation differs between control and Alzheimer's disease (AD) samples.
  • To assess if observed apoE dimers are post-mortem artifacts.

Main Methods:

  • Human frontal cortex and hippocampus from control and AD donors were homogenized.
  • Western blotting under reducing and non-reducing conditions was used to analyze apoE.
  • Thiol trapping agents were employed to rule out artifactual dimer formation.

Main Results:

  • Disulphide-linked apoE3 homodimers (approx. 12%) and heterodimers (approx. 2%) were detected in human brain samples.
  • Dimerization levels did not significantly differ between control and AD tissues.
  • ApoE4 homozygous samples lacked dimers, while apoE3/4 heterozygotes showed reduced dimerization compared to apoE3 homozygotes.
  • Similar dimers were found in neuroblastoma cells and rabbit brain homogenates, and were resistant to thiol-blocking agents, suggesting they are not post-mortem artifacts.

Conclusions:

  • Disulphide-linked apoE dimers are present in human cortical and hippocampal tissues.
  • This represents a structural difference between apoE3 and apoE4 isoforms.
  • The presence of these dimers may have functional implications in the brain.