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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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Alzheimer disease involves structural changes in the brain that begin long before symptoms appear. The most distinctive features are extracellular neuritic plaques and intracellular neurofibrillary tangles.Neuritic plaques form in the cerebral cortex and around blood vessels. These plaques contain a dense core of beta-amyloid (Aβ)—a toxic protein fragment that clumps outside neurons. The core is surrounded by damaged neuronal extensions, as well as reactive astrocytes and microglia. Abnormal...

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Imaging the Intracellular Trafficking of APP with Photoactivatable GFP
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Natural Modulators of Amyloid-Beta Precursor Protein Processing.

C Zhang1, R E Tanzi

  • 1Genetics and Aging Research Unit, MassGeneral Institute for Neurodegenerative Diseases (MIND), Department of Neurology, Massachusetts General Hospital and Harvard Medical School, 114 16th Street, Charlestown, MA, 02129-2060, USA. tanzi@helix.mgh.harvard.edu.

Current Alzheimer Research
|September 25, 2012
PubMed
Summary

Natural products, especially from traditional Chinese medicine, show promise in treating Alzheimer's disease (AD) by modulating amyloid precursor protein (APP) processing, offering new therapeutic avenues for this neurodegenerative condition.

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Area of Science:

  • Neuroscience
  • Pharmacology
  • Biochemistry

Background:

  • Alzheimer's disease (AD) is a leading cause of dementia with no cure.
  • Amyloid-beta (Aβ) peptide accumulation in plaques drives AD pathogenesis.
  • Aβ is derived from the amyloid-beta precursor protein (APP) via secretase enzymes.

Purpose of the Study:

  • To explore how natural products influence Alzheimer's disease progression.
  • To elucidate the molecular mechanisms of natural product intervention in AD.
  • To focus on the role of natural products in modulating amyloid precursor protein (APP) processing.

Main Methods:

  • Review of existing literature on natural products and AD.
  • Analysis of studies investigating the effects of traditional Chinese medicine (TCM) on APP processing.
  • Examination of molecular pathways affected by natural compounds.

Main Results:

  • Natural products can modulate the processing of APP, a key factor in AD.
  • Specific TCM-derived compounds show potential in altering APP metabolism.
  • Understanding these mechanisms opens doors for novel therapeutic strategies.

Conclusions:

  • Natural products offer a promising avenue for developing new AD treatments.
  • Targeting APP processing with natural compounds is a viable therapeutic strategy.
  • Further research into TCM for AD is warranted to uncover effective molecular mechanisms.