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Related Concept Videos

Neural Regulation01:37

Neural Regulation

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.
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...
Parkinson Disease ll: Pathophysiology01:24

Parkinson Disease ll: Pathophysiology

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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Related Experiment Video

Updated: Jul 5, 2026

Detection of Disease-associated α-synuclein by Enhanced ELISA in the Brain of Transgenic Mice Overexpressing Human A53T Mutated α-synuclein
12:01

Detection of Disease-associated α-synuclein by Enhanced ELISA in the Brain of Transgenic Mice Overexpressing Human A53T Mutated α-synuclein

Published on: May 30, 2015

Snaring the function of alpha-synuclein.

Nancy M Bonini1, Benoit I Giasson

  • 1Department of Biology and Howard Hughes Medical Institute, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.

Cell
|November 5, 2005
PubMed
Summary

Alpha-synuclein, linked to Parkinson's disease, functions as a molecular chaperone. It aids in the folding of SNARE proteins essential for neurotransmitter release and synaptic health.

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Protein Chemistry

Background:

  • Alpha-synuclein is a neuronal protein implicated in Parkinson's disease pathogenesis.
  • The physiological functions of alpha-synuclein are not fully understood.
  • Synaptic proteins, particularly SNAREs, are critical for neuronal communication.

Discussion:

  • Chandra et al. (2005) demonstrate alpha-synuclein's role as a molecular chaperone.
  • This chaperone activity involves assisting in the folding and refolding of SNARE proteins.
  • SNARE proteins mediate neurotransmitter release, vesicle recycling, and synaptic integrity.

Key Insights:

  • Alpha-synuclein actively participates in the proper functioning of synaptic machinery.
  • The protein's normal role as a chaperone may be disrupted in Parkinson's disease.

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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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Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays
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Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Published on: August 13, 2017

Related Experiment Videos

Last Updated: Jul 5, 2026

Detection of Disease-associated α-synuclein by Enhanced ELISA in the Brain of Transgenic Mice Overexpressing Human A53T Mutated α-synuclein
12:01

Detection of Disease-associated α-synuclein by Enhanced ELISA in the Brain of Transgenic Mice Overexpressing Human A53T Mutated α-synuclein

Published on: May 30, 2015

Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains
09:27

Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains

Published on: January 5, 2016

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays
09:36

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Published on: August 13, 2017

  • Understanding this function provides new avenues for Parkinson's research.

    • Outlook:

    • Further investigation into alpha-synuclein's chaperone mechanisms.
    • Exploring therapeutic strategies targeting alpha-synuclein's interaction with SNAREs.
    • Elucidating the link between chaperone dysfunction and neurodegeneration.