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Related Concept Videos

Teratogenicity01:07

Teratogenicity

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The ability of a drug to produce structural deformations and functional abnormalities in the developing embryo or the fetus is called teratogenicity, and the drug producing this effect is known as a teratogen. Teratogenic effects include stillbirth, miscarriage, intrauterine growth restriction, and neurocognitive delay. A teratogen may affect the embryo at different stages of development, which is important in determining the type and extent of the damage. During blastocyst formation, the early...
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Related Experiment Video

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Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans
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Investigating the Spreading and Toxicity of Prion-like Proteins Using the Metazoan Model Organism C. elegans

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Prions: generation and spread versus neurotoxicity.

Mark Halliday1, Helois Radford1, Giovanna R Mallucci2

  • 1From the Medical Research Council (MRC) Toxicology Unit, Hodgkin Building, University of Leicester, Lancaster Road, Leicester LE1 9HN, United Kingdom.

The Journal of Biological Chemistry
|May 27, 2014
PubMed
Summary
This summary is machine-generated.

Neurodegenerative diseases involve misfolded proteins. Targeting the unfolded protein response protects against prion disease neurotoxicity, dissociating it from protein misfolding.

Keywords:
Alzheimer DiseaseAlzheimer'sGene TherapyNeurodegenerationNeuroprotectionPrionUnfolded Protein Response (UPR)

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Area of Science:

  • Neurobiology
  • Protein Misfolding Diseases
  • Neurodegeneration

Background:

  • Neurodegenerative diseases feature misfolded protein aggregation.
  • Prion diseases involve transmissible prions as infectious agents.
  • Alzheimer's, Parkinson's, and tauopathies exhibit prion-like propagation.

Purpose of the Study:

  • To clarify the link between prion formation, spread, and neurotoxicity.
  • To investigate the role of proteostasis and the unfolded protein response in prion disease pathogenesis.

Main Methods:

  • Studied prion disease models.
  • Utilized genetic and pharmacological manipulation of the unfolded protein response.
  • Assessed neuroprotection and prion replication.

Main Results:

  • Protein misfolding in prion disease causes neurodegeneration via unfolded protein response dysregulation.
  • Manipulating the unfolded protein response provided neuroprotection.
  • Neuroprotection occurred independently of prion replication.

Conclusions:

  • The unfolded protein response is a key mediator of neurotoxicity in prion disease.
  • Targeting proteostatic mechanisms downstream of protein misfolding offers therapeutic potential.
  • This approach may benefit various neurodegenerative disorders.