NR ARDY

AU Koch,R.; Keyvani,K.; Karch,H.; Groschup,M.H.; Kuczius,T.

TI Distribution and glycoprotein patterns of cellular prion proteins in human brains

QU TSE-Forum, 4. Kongress - Nationale TSE-Forschungsplattform, Düsseldorf 28.10.-29.10.2004, Poster GL-07

PT Konferenz-Poster

AB Prion diseases are fatal neurodegenerative disorders affecting humans as Creutzfeldt-Jakob disease (CJD). They are characterized by the conversion of a host encoded cellular prion protein (PrPc) into its structurally altered and partially Proteinase K (PK) resistant pathological isoform (PrPsc). Differences of PrPsc in the molecular heterogeneity have been found by the glycoprotein typing technique in regard to the distribution of the relative staining intensities of each of the three resulting PrPsc bands of the di-, mono- and non-glycosylated isoforms. Within a species PrP are not uniform in their banding patterns thus it is conceivable that some PrPsc conformations may interact more or less efficiently with subspecies of PrPc differentially expressed in various brain regions. Using three different antibodies that detect different epitops of prion proteins we have analysed the distribution and glycoprotein patterns of seven different human brain regions in order to find out the existence of prion variations. Intensity of immunoreactive signals of the protein bands were quantified by means of a photo imager and intensities were statistically ensured. The di-glycosylated PrPc of grey and white matter of cerebrum, nucleus lentiformis, thalamus, hippocampus, cerebellum and pons was most abundant using antibody Pri 308, while the non-glycosylated PrPc immunochemically reacted very strong with 12F10. High signal intensities were detected of the non-glycosylated PrPc of white matter and pons using antibody SAF 34, while the di-glycosylated isoform was most abundant in other brain regions. Despite of individual heterogeneity decreased PrP amounts were only detected in cerebellum and pons compared with other regions. However, the regional glycoform distribution of PrPc in human brain regions is strongly dependant on the used antibody.

AD R. Koch, H. Karch, T. Kuczius, Institute for Hygiene, University Hospital Muenster, Robert Koch Strasse 41, 48149 Münster, Germany; K. Keyvani, Institute for Neuropathology, University Hospital Muenster, Domagkstrasse 19, 48149 Münster, Germany; M.H. Groschup, Institute for Novel and Emerging Infectious Diseases, Federal Research Centre for Virus Diseases of Animals, 17493 Greifswald - Insel Riems, Germany

SP englisch

PO Deutschland

OR Tagungsband

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