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Related Concept Videos

Parkinson Disease ll: Pathophysiology01:24

Parkinson Disease ll: Pathophysiology

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Parkinson disease (PD) is a progressive neurodegenerative disorder primarily affecting movement, with additional non-motor features. Its pathophysiology involves complex interactions among genetic susceptibility, environmental exposures, and cellular dysfunction, including dopaminergic neuron loss, protein aggregation, and mitochondrial impairment.Selective NeurodegenerationA key feature is the degeneration of dopaminergic neurons in the substantia nigra pars compacta, leading to reduced...
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Amyloid Fibrils03:03

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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. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
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Lysosomal Hydrolases01:22

Lysosomal Hydrolases

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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,...
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Asymmetric Lipid Bilayer01:35

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Biological membranes show uneven distribution of different types of lipids in the inner and outer layers, resulting in transverse asymmetric membranes. The treatment of the erythrocyte membrane with the enzyme phospholipase confirmed the asymmetric nature of the lipid bilayer. The enzyme hydrolyzes lipids into fatty acids and hydrophilic groups. The phospholipase acts only on the outer layer of the membrane, while the inner layer remains intact. The phospholipase treatment resulted in 80%...
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Neural Regulation01:37

Neural Regulation

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Digestion begins with a cephalic phase that prepares the digestive system to receive food. When our brain processes visual or olfactory information about food, it triggers impulses in the cranial nerves innervating the salivary glands and stomach to prepare for food.
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Updated: Apr 19, 2026

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils
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Alpha-synuclein function and dysfunction on cellular membranes.

David Snead1, David Eliezer1

  • 1Department of Biochemistry, Weill Cornell Medical College, New York, NY 10065, USA.

Experimental Neurobiology
|December 31, 2014
PubMed
Summary
This summary is machine-generated.

Alpha-synuclein protein aggregation is central to Parkinson's disease pathogenesis. This review explores how alpha-synuclein's interactions with cellular membranes influence its normal function and disease-related toxicity.

Keywords:
Parkinsonaggregationalpha-synucleinamyloidneurotransmissionsynucleinopathy

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Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions
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Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains
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Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains
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Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Background:

  • Alpha-synuclein is implicated in Parkinson's disease (PD) etiology.
  • Mutations and altered expression levels of alpha-synuclein cause hereditary PD.
  • Lewy bodies, characteristic of sporadic PD, are primarily composed of aggregated alpha-synuclein.

Purpose of the Study:

  • To review the known features of alpha-synuclein membrane interactions.
  • To contextualize these interactions within the protein's putative functions.
  • To explore their role in alpha-synuclein aggregation and toxicity in PD.

Main Methods:

  • Literature review of studies on alpha-synuclein.
  • Analysis of alpha-synuclein's biophysical properties.
  • Examination of its interactions with various cellular membranes.

Main Results:

  • Alpha-synuclein's normal function remains poorly understood.
  • Mechanisms of alpha-synuclein-induced toxicity and cell death are unclear.
  • Despite being soluble, alpha-synuclein binds to diverse cellular membranes.

Conclusions:

  • Alpha-synuclein membrane interactions are critical for its normal functions.
  • These interactions likely play key roles in protein aggregation.
  • Membrane interactions are implicated in the pathological mechanisms of Parkinson's disease.