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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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Parkinson Disease ll: Pathophysiology01:24

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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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Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions
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Alpha-Synuclein conformation affects its tyrosine-dependent oxidative aggregation.

Rebecca A S Ruf1, Evan A Lutz, Imola G Zigoneanu

  • 1Department of Chemistry, University of North Carolina, Chapel Hill, North Carolina 27599, USA.

Biochemistry
|December 4, 2008
PubMed
Summary
This summary is machine-generated.

Oxidative stress drives alpha-synuclein aggregation in Parkinson's disease. Tyrosine 39 is crucial for this aggregation in a collapsed protein state, offering insights into Lewy body formation.

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Area of Science:

  • Biochemistry
  • Neuroscience
  • Protein Chemistry

Background:

  • Oxidative stress and alpha-synuclein aggregation are implicated in Parkinson's disease pathogenesis.
  • Cytochrome c and hydrogen peroxide induce in vitro protein aggregation via tyrosine residues.

Purpose of the Study:

  • To investigate the role of individual tyrosine residues in alpha-synuclein's oxidative aggregation.
  • To understand how protein conformation influences covalent aggregation.

Main Methods:

  • Site-directed mutagenesis of alpha-synuclein tyrosine residues.
  • In vitro peroxidative aggregation assays with cytochrome c and H(2)O(2).
  • Analysis of aggregation in different protein conformations (collapsed, denatured, fibrillar).

Main Results:

  • Tyrosine 39 is essential for wild-type-like covalent aggregation in a collapsed alpha-synuclein conformation.
  • This tyrosine is not required for aggregation in denaturants or noncovalent fibrils.
  • Preformed oxidative aggregates do not integrate into noncovalent fibrils.

Conclusions:

  • Tyrosine 39 plays a critical role in alpha-synuclein oxidative aggregation under specific conformational conditions.
  • These findings shed light on the potential formation of dityrosine cross-links in Parkinson's disease Lewy bodies.