Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Post-translational modifications in prion proteins.

Laszlo Otvos1, Mare Cudic

  • 1The Wistar Institute, 3601 Spruce Street, Philadelphia, PA 19104, USA. otvos@wistar.upenn.edu

Current Protein & Peptide Science
|December 10, 2002
PubMed
Summary

Prion diseases involve the transformation of normal prion protein (PrP(C)) into a disease-related form (PrP(SC)). Post-translational modifications, like glycosylation, may be key to this pathogenic process and neurodegeneration.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Probing APP Cleavage and Amyloid-β Assembly via Synthetic MUC-Type <i>O</i>-Glycosylated APP Glycopeptides.

ACS chemical neuroscience·2026
Same author

Implications of Mucin-Type <i>O</i>-Glycosylation in Alzheimer's Disease.

Molecules (Basel, Switzerland)·2025
Same author

Spectroscopic and calorimetric study of the interaction between Nile blue and double-stranded RNA.

Biochemistry and biophysics reports·2025
Same author

Preventative Cancer Vaccine-Elicited Human Anti-MUC1 Antibodies Have Multiple Effector Functions.

Antibodies (Basel, Switzerland)·2024
Same author

Amadori and Heyns rearrangement products of bioactive peptides as potential new ligands of galectin-3.

Carbohydrate research·2024
Same author

Synthesis and Thermodynamic Evaluation of Sialyl-Tn MUC1 Glycopeptides Binding to Macrophage Galactose-Type Lectin.

Chembiochem : a European journal of chemical biology·2024

Area of Science:

  • Neuroscience
  • Biochemistry
  • Molecular Biology

Background:

  • Prion diseases are fatal neurodegenerative disorders caused by the misfolding of the prion protein (PrP).
  • The cellular prion protein (PrP(C)) converts to the disease-associated scrapie form (PrP(SC)), but the exact mechanism remains unclear.
  • Post-translational modifications, particularly N-linked glycosylation, are increasingly implicated in this transformation.

Purpose of the Study:

  • To explore the role of post-translational modifications in the conversion of PrP(C) to PrP(SC).
  • To investigate how glycosylation affects PrP conformation, PrP(SC) stability, and clearance rates.
  • To understand the interplay between glycosylation, mutations, and prion pathogenesis.

Main Methods:

  • Review of existing literature on prion protein structure and function.

Related Experiment Videos

  • Analysis of glycosylation sites (Asn181, Asn197) in human PrP.
  • Consideration of molecular modeling for glycosylated PrP structures.
  • Examination of the link between PrP, copper binding, and oxidative stress.

    • Main Results:

    • Glycosylation can influence PrP(C) conformation and PrP(SC) stability.
    • The structure of glycosylated PrP is not yet determined by NMR, relying on modeling.
    • Mutations near glycosylation sites may affect prion disease mechanisms.
    • Prion protein's role in copper binding and oxidative stress tolerance is noted.

    Conclusions:

    • Post-translational modifications, alone or with mutations, are hypothesized to be critical drivers of PrP(C) to PrP(SC) conversion.
    • Further research into glycosylated PrP structure and function is needed.
    • Understanding these modifications could offer insights into prion disease pathogenesis and potential therapeutic targets.