Partitioning and confinement of GM1 ganglioside induced by amyloid aggregates

Anno: 2013

Autori: Calamai M., Pavone F.

Affiliazione autori: CNR Neuroscience Institute, Pisa, Italy; European Laboratory for Non-Linear Spectroscopy, Sesto Fiorentino, Italy; Department of Physics and Astronomy, University of Florence, Sesto Fiorentino, Italy; National Institute of Optics, National Research Council, Florence, Italy; International Center of Computational Neurophotonics, Sesto Fiorentino, Italy

Abstract: Growing evidence shows that GM1 ganglioside is involved in amyloid deposition and toxicity. By means of real-time single particle tracking, we show that amyloid oligomers and aggregates formed by A beta 1-42 and amylin, two peptides associated, respectively, with the development of Alzheimer\’s disease and type II diabetes, interact with GM1 and decrease dramatically its lateral diffusion on the plasma membrane of living neuroblastoma cells. The confinement of GM1, a constituent of membrane rafts involved in neuroprotection, at the level of both types of amyloid aggregates can interfere with cell signaling pathways and contribute to the loss of neuroprotection. (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

Giornale/Rivista: FEBS LETTERS

Volume: 587 (9)      Da Pagina: 1385  A: 1391

Maggiori informazioni: We thank M. Capitanio and L. Gardini for technical advice and assistance, F. Vanzi, B. Bisel, M. Bucciantini and M. Stefani for critical discussions. This work was supported by the European Union Seventh Framework Programme (FP7/2007-2013) under grant agreements No. 228334 and PIEF-GA-2009-254791, the Italian Ministry for Education, University and Research in the framework of the Flagship Project NANOMAX, the European Union Seventh Framework Programme (FP7/2007-2013) under grant agreement No. 284464 and the Ente Cassa di Risparmio di Firenze (private foundation).
Parole chiavi: amylin; amyloid beta protein[1-42]; ganglioside GM1; gephyrin; glycine receptor; oligomer, antibody labeling; article; binding affinity; cell membrane; controlled study; human; human cell; neuroblastoma cell; priority journal; protein aggregation; protein binding; protein function; protein localization; protein protein interaction, Amyloid beta-Peptides; Animals; Biological Transport; Cell Line, Tumor; Cell Survival; Diffusion; G(M1) Ganglioside; Humans; Islet Amyloid Polypeptide; Membrane Microdomains; Peptide Fragments; Protein Multimerization; Protein Structure, Secondary; Time Factors
DOI: 10.1016/j.febslet.2013.03.014

Citazioni: 32
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