In:
Journal of Cellular Biochemistry, Wiley, Vol. 114, No. 12 ( 2013-12), p. 2690-2698
Abstract:
Prion diseases entail the conversion of a normal host‐encoded prion protein (PrP C ) into an infectious isoform (PrP Sc ). Various PrP C types differing in banding profiles and detergent solubility are present in different tissues, but only few PrP Sc types have been generated although PrP C acts as substrate. We hypothesize that distinct PrP C subtypes may be converted more efficiently to PrP Sc than others. One prerequisite for the analysis is the identification of the PrP C subtypes present in the protein complexes. Metal binding to PrP C is one of the most prominent features of the protein which induces increased proteolysis resistance and structural changes which might play an important role in the conversion process. Here we analyzed the metal‐induced structural PrP C transformation of two different Triton X‐100 soluble PrP C types derived from human platelets and brains by changes in protein solubility. We found that zinc and copper rendered approximately half of total PrP C and mainly un‐ and low‐glycosylated PrP C to the Triton insoluble fraction. Our results indicate the presence of at least two distinct PrP C subtypes by metal interactions. The differentiation of high and low soluble metal bound PrP C offers precious information about PrP C protein composition and provides approaches for analyzing the transformation efficiency to PrP Sc . J. Cell. Biochem. 114: 2690–2698, 2013. © 2013 Wiley Periodicals, Inc.
Type of Medium:
Online Resource
ISSN:
0730-2312
,
1097-4644
Language:
English
Publisher:
Wiley
Publication Date:
2013
detail.hit.zdb_id:
1479976-5
SSG:
12
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