Premium
Cellular prion proteins in human platelets show a phenotype different to those in brain tissues
Author(s) -
Kuczius Thorsten,
Kleinert Julia,
Karch Helge,
Sibrowski Walter,
Kelsch Reinhard
Publication year - 2011
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.23012
Subject(s) - glycosylation , platelet , monoclonal antibody , phenotype , human brain , solubility , biology , antibody , prion protein , microbiology and biotechnology , biochemistry , chemistry , immunology , disease , gene , medicine , pathology , organic chemistry , neuroscience
Prion diseases are characterized by high accumulation of infectious prion proteins (PrP Sc ) in brains. PrP Sc are propagated by the conversion of host‐encoded cellular prion proteins (PrP C ) which are essential for developing the disease but are heterogeneously expressed in brains. The disease can be transmitted to humans and animals through blood and blood products, however, little attention has been given to molecular characterization of PrP C in blood cells. In this presented study, we characterized phenotypically PrP C of platelets (plt) and characterized the proteins regarding their glycobanding profiles by quantitative immunoblotting using a panel of monoclonal antibodies. The glycosylation patterns of plt and brain PrP C were compared using the ratios of di‐, mono‐, and non‐glycosylated prions. The detergent solubility of plt and brain PrP C was also analyzed. The distinct banding patterns and detergent solubility of plt PrP C differed clearly from the glycosylation profiles and solubility characteristics of brain PrP C . Plt PrP C exhibited single or only few prion protein types, whereas brain PrP C showed more extensive banding patterns and lower detergent solubility. Plt PrP C are post‐translational modified differently from PrP C in brain. These findings suggest other or less physiological functions of plt PrP C than in brain. J. Cell. Biochem. 112: 954–962, 2011. © 2010 Wiley‐Liss, Inc.