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Related Concept Videos

Autophagy01:27

Autophagy

Autophagy is a self-digesting process by which a cell protects itself from threats both within and outside the cell, ranging from abnormal proteins to invading bacteria. In this process, obsolete components of the cell and invading microbes are degraded by hydrolytic enzymes active in an acidic environment of the lysosomal lumen.
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Lysosomes are the site for the degradation of macromolecules and biological polymers released during membrane trafficking events such as secretory, endocytic, autophagic, and phagocytic pathways. The membrane-enclosed area of the lysosome, called the lumen, contains hydrolytic enzymes active in an acidic environment. These acid hydrolases are functional at a pH between 4.5 and 5 and are involved in cellular processes such as cell signaling, energy metabolism, restoration of the plasma membrane,...
Autophagic Cell Death01:18

Autophagic Cell Death

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A Method to Study &#945;-Synuclein Toxicity and Aggregation Using a Humanized Yeast Model
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A Method to Study α-Synuclein Toxicity and Aggregation Using a Humanized Yeast Model

Published on: November 25, 2022

Alpha-synuclein aggregation involves a bafilomycin A 1-sensitive autophagy pathway.

Jochen Klucken1, Anne-Maria Poehler, Darius Ebrahimi-Fakhari

  • 1Department of Molecular Neurology, University Hospital, Erlangen, Germany. jochen.klucken@uk-erlangen.de

Autophagy
|June 1, 2012
PubMed
Summary
This summary is machine-generated.

In synucleinopathies like dementia with Lewy bodies, inhibiting the autophagy-lysosomal pathway (ALP) paradoxically reduces alpha-synuclein aggregation while increasing toxicity, suggesting aggregation may be a protective mechanism.

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Studying Pre-formed Fibril Induced α-Synuclein Accumulation in Primary Embryonic Mouse Midbrain Dopamine Neurons

Published on: August 16, 2020

Area of Science:

  • Neuroscience
  • Cell Biology
  • Biochemistry

Background:

  • Synucleinopathies, including Parkinson disease and dementia with Lewy bodies (DLB), involve alpha-synuclein aggregation in neurons.
  • The role of alpha-synuclein aggregates in disease pathology is debated, with impaired degradation implicated in their formation.
  • The autophagy-lysosomal pathway (ALP) is a key cellular mechanism for degrading alpha-synuclein.

Purpose of the Study:

  • To investigate the impact of modulating the autophagy-lysosomal pathway (ALP) on alpha-synuclein aggregation and toxicity.
  • To identify specific pathways within ALP that influence alpha-synuclein pathology.

Main Methods:

  • Analysis of ALP markers (LAMP-2A, LC3-II) in human DLB brain tissue, a transgenic mouse model, and cell culture models.
  • Inhibition of ALP using bafilomycin A1 (BafA1) in vivo and in vitro.
  • Assessment of alpha-synuclein aggregation and cellular toxicity.

Main Results:

  • ALP markers were induced in DLB patient brains, mouse models, and cell cultures.
  • Bafilomycin A1 (BafA1) treatment potentiated alpha-synuclein toxicity but reduced aggregation in both mouse and cell models.
  • This aggregation-reducing effect was specific to BafA1 and not observed with other ALP inhibitors.

Conclusions:

  • The autophagy-lysosomal pathway plays a role in degrading alpha-synuclein, with a specific BafA1-sensitive pathway influencing aggregation.
  • Alpha-synuclein aggregation may function as a cellular detoxification mechanism rather than being directly causative of toxicity.
  • Targeting specific ALP components could offer novel therapeutic strategies for synucleinopathies.