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Related Concept Videos

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Amyloid Fibrils

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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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Cells undergoing apoptosis form apoptotic bodies that must be removed immediately to prevent inflammation, autoimmune diseases, and necrosis. Phagocytosis is carried out by professional phagocytes such as macrophages or  immature dendritic cells. Non-professional phagocytes such as  epithelial cells and fibroblasts also take part in this process; however, they are not as effective as professional phagocytes. 
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Related Experiment Video

Updated: Mar 27, 2026

Imaging the Intracellular Trafficking of APP with Photoactivatable GFP
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Perforin Promotes Amyloid Beta Internalisation in Neurons.

Erica Lana1, Mahbod Khanbolouki2, Charline Degavre2

  • 1Division of Translational Alzheimer Neurobiology, NVS Department, Center for Alzheimer Research, Karolinska Institutet, Huddinge, 141 57, Sweden.

Molecular Neurobiology
|January 19, 2016
PubMed
Summary

Alzheimer's disease research reveals amyloid-beta (Aβ) peptides enter neurons via endocytosis, with Aβ42 also using the RAGE pathway. Perforin pore formation facilitates Aβ entry in human neurons, offering new therapeutic targets.

Keywords:
Alzheimer’s diseaseAmyloid β peptidesEndocytosisHuman primary neuronsPerforinRAGESH-SY5Y

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Biochemistry

Background:

  • Neuronal amyloid-beta (Aβ) internalisation is critical for Alzheimer's disease (AD) progression.
  • Understanding Aβ uptake mechanisms is key to developing AD therapeutics.

Purpose of the Study:

  • To investigate the distinct pathways of extracellular Aβ40 and Aβ42 internalisation into neuronal cells.
  • To compare Aβ uptake in neuroblastoma cells and primary human neurons.

Main Methods:

  • Utilised retinoic acid differentiated neuroblastoma (RA-SH-SY5Y) cells and human primary cortical neurons (hPCN).
  • Employed confocal microscopy to track Aβ distribution and co-localisation with cellular organelles.
  • Investigated Aβ internalisation via endocytosis, the receptor for advanced glycation end products (RAGE), and perforin.

Main Results:

  • Both Aβ40 and Aβ42 were internalised, with different concentration requirements and distribution patterns.
  • Endocytosis was identified as the primary Aβ internalisation pathway in both cell types.
  • RAGE blockade reduced Aβ42 internalisation by 55%, while perforin-induced pore formation enabled Aβ entry into hPCN.

Conclusions:

  • Neuronal Aβ internalisation occurs through multiple pathways, including endocytosis, RAGE, and perforin.
  • Findings highlight potential therapeutic strategies targeting Aβ uptake to inhibit neurodegeneration in AD.