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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. 
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Imaging the Intracellular Trafficking of APP with Photoactivatable GFP
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FE65 proteins regulate NMDA receptor activation-induced amyloid precursor protein processing.

Jaehong Suh1, Alvin Lyckman, Lirong Wang

  • 1Genetics and Aging Research Unit, MassGeneral Institute for Neurodegenerative Disease, Massachusetts General Hospital, Harvard Medical School, Charlestown, Massachusetts, USA.

Journal of Neurochemistry
|August 10, 2011
PubMed
Summary

FE65 proteins facilitate amyloid precursor protein (APP) processing and Aβ secretion in neurons. They also promote non-amyloidogenic APP processing and the accumulation of APP metabolic products following NMDA receptor activation.

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cell Biology

Background:

  • Amyloid precursor protein (APP) processing is crucial for nervous system function and Alzheimer's disease (AD).
  • Neuronal activity, particularly NMDA receptor (NMDAR) activation, influences APP processing pathways.
  • The role of FE65 proteins in neuronal APP trafficking and processing remains largely unexplored.

Purpose of the Study:

  • To investigate the role of the FE65 protein family in APP trafficking and processing within neurons.
  • To determine FE65 protein contribution under basal conditions and following NMDAR activation.
  • To elucidate the impact of FE65 proteins on amyloid-beta (Aβ) secretion and APP processing pathways.

Main Methods:

  • Utilized wild-type (WT) and FE65/FE65L1 double knockout (KO) neuronal models.
  • Examined APP trafficking and processing under basal and NMDAR-activated conditions.
  • Analyzed Aβ secretion, APP axonal transport, and the formation of high-molecular weight (HMW) APP species.

Main Results:

  • FE65 proteins enhance neuronal Aβ secretion without altering APP fast axonal transport.
  • FE65 proteins promote an NMDAR-dependent non-amyloidogenic APP processing pathway.
  • NMDAR activation leads to the accumulation of proteasome- and calpain-dependent HMW APP species.

Conclusions:

  • FE65 proteins are key facilitators of physiological APP processing in neurons.
  • FE65 proteins contribute to the accumulation of APP metabolic products upon NMDAR activation.
  • Findings shed light on APP regulation in neuronal function and potential AD pathogenesis.