NR AOTJ
AU Gonzalez-Iglesias,R.; Elvira,G.; Zorrila,S.; Rodriguez-Navarro,J.A.; Pajares,M.A.; Velez,M.; Gasset,M.
TI N-terminal domain mediated PrP aggregation
QU International Conference - Prion diseases: from basic research to intervention concepts - TSE-Forum, 08.10.-10.10.2003, Gasteig, München - Poster session - BR-23
PT Konferenz-Poster
AB PrPc, the cellular form of the prion protein, has become a key molecule in brain for the understanding of the lethal neurodegenerative diseases known as TSE. Under disease, PrP adopts alternative conformations which are characterized by a higher content of extended structure, distorted solubility, improved aggregation tendency and impaired metabolic rate clearance. Study of oligomerization events has been focused on defining the contour conditions that converts the C-terminal domain into self-perpetuating like forms. However a large number of disease variants, represented by mutation at the N-terminal region of the protein, concur with the generation of neurotoxic PrP forms. Using specific ligands of the N-terminal domain, we have been able to induce the formation of detergent-resistant protein oligomers. These oligomers are insoluble, their formation is promoted by intermolecular crosslinks and, when imaged, they appeared as a laminar amorphous mesh. Furthermore, their stability makes then compatible with an altered cellular clearance
AD Reinerio Gonzalez-Iglesias, Gema Elvira, Maria Gasset, Jose A Rodriguez-Navarro, IQFR, CSIC, Spain; Silvia Zorrila, Maria A. Pajares, IIB, CSIC-UAM, Spain; Marisela Velez, INC, UAM, Spain
SP englisch
PO Deutschland