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Deep membrane insertion of prion protein upon reduction of disulfide bond
- Source :
- Biochemical and biophysical research communications. 377(3)
- Publication Year :
- 2008
-
Abstract
- The membrane may play a role in the pathogenesis of the prion protein (PrP). Cytoplasmic expression of PrP causes the conversion of PrP to a self-perpetuating PrP Sc -like conformation and the interaction of polypeptide chain with the hydrophobic core of the membrane is believed to be closely correlated with neurodegeneration. However, it is still elusive what factors govern the membrane interaction of PrP. Here, we show that PrP penetrates deeply into the membrane when the single disulfide bond is reduced, which results in membrane disruption and leakage. The proteinase K treatment and the fluorescence quenching assays showed that a predicted transmembrane domain of PrP penetrates into the membrane when the disulfide bond was reduced. Therefore, the oxidation state of PrP might be an important factor that influences its neurotoxicity or pathogenesis.
- Subjects :
- Cell Membrane Permeability
PrPSc Proteins
animal diseases
Biophysics
Biochemistry
Fluorescence
Pathogenesis
Cricetinae
medicine
Animals
Immunoprecipitation
Disulfides
Molecular Biology
Unilamellar Liposomes
biology
Chemistry
Neurodegeneration
Cell Membrane
Disulfide bond
Neurotoxicity
Cell Biology
Proteinase K
medicine.disease
nervous system diseases
Transmembrane domain
Membrane
Cytoplasm
biology.protein
Endopeptidase K
Oxidation-Reduction
Subjects
Details
- ISSN :
- 10902104
- Volume :
- 377
- Issue :
- 3
- Database :
- OpenAIRE
- Journal :
- Biochemical and biophysical research communications
- Accession number :
- edsair.doi.dedup.....8e776beb94d4d7a2c2be594c7bfb288d