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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...
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...
Antigen Processing Pathways01:31

Antigen Processing Pathways

MHC molecules are key players in the immune response, enabling T cells to recognize and respond to specific antigens. They are present on the surface of all nucleated cells in the body and are instrumental in presenting antigens to T cells and activating them. T cells recognize the MHC-antigen complex and initiate an immune response. MHC class I and MHC class II are two main types of MHC molecules, each associated with a distinct antigen processing pathway.
MHC Class I: Presenting Endogenous...
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial precursors...
The Proteasome01:13

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...

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Related Experiment Video

Updated: Jun 21, 2026

Imaging the Intracellular Trafficking of APP with Photoactivatable GFP
07:55

Imaging the Intracellular Trafficking of APP with Photoactivatable GFP

Published on: October 17, 2015

A novel pathway for amyloid precursor protein processing.

Erik Portelius1, Eric Price, Gunnar Brinkmalm

  • 1Institute of Neuroscience and Physiology, Department of Psychiatry and Neurochemistry, The Sahlgrenska Academy, University of Gothenburg, S-431 80 Mölndal, Sweden. erik.portelius@neuro.gu.se

Neurobiology of Aging
|July 17, 2009
PubMed
Summary

Researchers discovered a new pathway for amyloid precursor protein (APP) processing. This pathway generates shorter amyloid beta (Aβ) isoforms found in cerebrospinal fluid (CSF), distinct from known Alzheimer-associated pathways.

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Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain
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Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

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Rapid Generation of Amyloid from Native Proteins In vitro
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Rapid Generation of Amyloid from Native Proteins In vitro

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Last Updated: Jun 21, 2026

Imaging the Intracellular Trafficking of APP with Photoactivatable GFP
07:55

Imaging the Intracellular Trafficking of APP with Photoactivatable GFP

Published on: October 17, 2015

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain
10:08

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain

Published on: August 28, 2012

Rapid Generation of Amyloid from Native Proteins In vitro
05:48

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Area of Science:

  • Neuroscience
  • Biochemistry
  • Molecular Biology

Background:

  • Amyloid precursor protein (APP) is processed via amyloidogenic and non-amyloidogenic pathways.
  • The amyloidogenic pathway produces Alzheimer's-associated amyloid beta (Aβ) peptides (Aβ1-40 and Aβ1-42).
  • Cerebrospinal fluid (CSF) contains various shorter Aβ isoforms alongside Aβ1-40 and Aβ1-42.

Purpose of the Study:

  • To investigate the processing pathways responsible for generating shorter Aβ isoforms in CSF.
  • To develop and utilize a cell model that accurately mimics the Aβ isoform pattern observed in human CSF.
  • To elucidate the role of α-, β-, and γ-secretase in the generation of these Aβ isoforms.

Main Methods:

  • Immunoprecipitation and mass spectrometry were used to identify Aβ isoforms in CSF.
  • A novel cell model was established to replicate the Aβ isoform profile of CSF.
  • The cell model was treated with α-, β-, and γ-secretase inhibitors to analyze their effects on Aβ isoform generation.

Main Results:

  • All Aβ isoforms of 17 amino acids or longer (Aβ1-17 and longer) were dependent on γ-secretase activity.
  • Shorter Aβ isoforms (e.g., Aβ1-14, Aβ1-15) were independent of γ-secretase.
  • Treatment with α- and β-secretase inhibitors reduced the levels of these shorter, γ-secretase-independent Aβ isoforms.

Conclusions:

  • A novel, third APP processing pathway exists, involving sequential α- and β-secretase cleavages.
  • This pathway contributes to the generation of shorter Aβ isoforms observed in CSF.
  • Understanding this pathway may offer new insights into APP processing and potential therapeutic targets.