NR AOTB
AU Giese,A.; Bader,B.; Bieschke,J.G.; Schaffar,G.; Odoy,S.; Kahle,P.J.; Haass,C.; Kretzschmar,H.A.
TI Dual-colour Scanning For Intensely Fluorescent Targets (SIFT) Allows Differential Monitoring of Co-aggregating Amyloidogenic Proteins
QU International Conference - Prion diseases: from basic research to intervention concepts - TSE-Forum, 08.10.-10.10.2003, Gasteig, München - Poster session - BR-49
PT Konferenz-Poster
AB Protein aggregation is the key event in a number of human diseases such as Alzheimer's and Parkinson's disease. We present a general method to quantify and characterize protein aggregates by dual-colour scanning for intensely fluorescent targets (SIFT). In addition to high sensitivity, this approach offers a unique opportunity to study co-aggregation processes. As the ratio of two fluorescently labelled components can be analysed for each aggregate separately in a homogeneous assay, the molecular composition of aggregates can be studied even in samples containing a mixture of different types of aggregates. Using this method, we could show that wild-type ?-synuclein forms co-aggregates with a mutant variant found in familial Parkinson's disease. Moreover, we found a striking increase in aggregate formation at non-equimolar mixing ratios, which may have important therapeutic implications, as lowering the relative amount of aberrant protein may cause an increase of protein aggregation leading to adverse effects.
AD Armin Giese, Benedikt Bader, Jan G. Bieschke, Hans A. Kretzschmar, Institute of Neuropathology, LMU, Munich, Germany; Gregor Schaffar, Max-Planck-Institute for Biochemistry, Martinried, Germany; Sabine Odoy, Philipp J. Kahle, Christian Haass, Laboratory of Alzheimer's and Parkinson's Disease Research, Department of Biochemistry, LMU, Munich, Germany
SP englisch
PO Deutschland