Acidic pH and Detergents Enhance in Vitro Conversion of Human Brain PrP C to a PrP Sc -like Form *
Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 277, Issue: 46, Page: 43942-43947
2002
- 83Citations
- 46Captures
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Metrics Details
- Citations83
- Citation Indexes81
- 81
- CrossRef62
- Patent Family Citations2
- Patent Families2
- Captures46
- Readers46
- 46
Article Description
In the presence of a low concentration of denaturants or detergents, acidic pH triggers a conformational transition of α-helices into β-sheets in recombinant prion protein (PrP), likely mimicking some aspects of the transformation of host-encoded normal cellular PrP (PrP C ) into its pathogenic isoform (PrP Sc ). Here we observed the effects of acidic pH and guanidine hydrochloride (GdnHCl) on the physicochemical and structural properties of PrP C derived from normal human brain and determined the ability of the acid/GdnHCl-treated PrP to form a proteinase K (PK)-resistant species in the absence and presence of PrP Sc template. After treatment with 1.5 m GdnHCl at pH 3.5, PrP C from normal brain homogenates was converted into a detergent-insoluble form similar to PrP Sc. Unlike PrP Sc, however, the treated brain PrP C was protease-sensitive and retained epitope accessibility to monoclonal antibodies 3F4 and 6H4. Brain PrP C treated with acidic pH/GdnHCl acquired partial PK resistance upon further treatment with low concentrations of sodium dodecyl sulfate (SDS). Formation of this PrP Sc -like isoform was greatly enhanced by incubation with trace quantities of PrP Sc from Creutzfeldt-Jakob disease brain. Acid/GdnHCl-treated brain PrP may constitute a “recruitable intermediate” in PrP Sc formation. Further structural rearrangement seems essential for this species to acquire PK resistance, which can be promoted by the presence of a PrP Sc template.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0021925819717384; http://dx.doi.org/10.1074/jbc.m203611200; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0037113898&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/12161431; http://www.jbc.org/lookup/doi/10.1074/jbc.M203611200; https://syndication.highwire.org/content/doi/10.1074/jbc.M203611200; https://linkinghub.elsevier.com/retrieve/pii/S0021925819717384; https://dx.doi.org/10.1074/jbc.m203611200
American Society for Biochemistry & Molecular Biology (ASBMB)
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