NR ATRN
AU Kuczius,T.; Koch,R.; Keyvani,K.; Grassi,J.; Karch,H.; Groschup,M.H.
TI Heterogeneity of cellular prion proteins in different species
QU International Conference - Prion 2005: Between fundamentals and society's needs - 19.10.-21.10.2005, Congress Center Düsseldorf - Poster Session: Structure of PrP and molecular determinants of infectivity STRCT-29
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 it's partially Proteinase K (PK) resistant pathological isoform (PrPsc). Many PrPsc proteins have been characterized using 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, PrPs are also 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 different antibodies detecting the PrP the octarepeat region (A), the region between amino acids (aa) 97 to 118 (B) and the central region between the aa 140 to 160 (C) we have analysed the glycoform patterns of four different species and the distribution of seven different human brain regions in order to find out the existence of prion variations. The immunoreactive signals were quantified by means of a photo imager, and intensities were statistically ensured. The di-glycosylated PrPc was most abundant of all species using antibodies detecting regions A and B as SAF34, Pri308 or p4, while the non-glycosylated form reacted strong with antibodies detecting region C as SAF60, SAF70 or 12F10. High signal intensities were detected of the non-glycosylated PrPc of white matter and pons using antibody SAF34, while the di-glycosylated isoform was most abundant of grey matter of cerebrum, nucleus lentiformis, thalamus, hippocampus and cerebellum derived from human brains. The regional glycoform distribution of PrPc in human brain regions is strongly dependant on the used antibody.
IN In verschiedenen menschlichen Hirnregionen fanden die Autoren unterschiedliche Mengenverteilungen der un- mono- und diglykosilierten Formen des normalen zellulären Prionproteins PrPc.
AD T.Kuczius, R.Koch, H.Karch, Institute for Hygiene, University Hospital Münster, Germany; K.Keyvani, Institute for Neuropathology, University Hospital Münster, Germany; J.Grassi, Commissariat á l'Energie Atomique (CEA), Service de Pharmacologie et d'Immunologie, CEA/Saclay, France; M.H.Groschup, Friedrich-Loeffler-Institute, Institute for Novel and Emerging Infectious Diseases, Germany
SP englisch
PO Deutschland