Monograph

Structural and functional aspects of membranes

The involvement of lipid rafts in Alzheimer’s disease pathogenesis. The interplay between protein oligomers and plasma membrane physicochemical features in determining cytotoxicity
  • Elisa Evangelisti,

Alzheimer’s disease (AD) is a common form of dementia characterized by the formation of extracellular senile plaques composed of aggregated amyloid peptide (Aβ). The present studies provide evidence that: cell resistance to amyloid toxicity is related to lipid raft cholesterol content. Cholesterol and GM1, affect the susceptibility of Familial Alzheimer’s Disease (FAD) broblasts to Aβ42 oligomers in opposite ways, by modulating amyloid binding to lipid rafts and its subsequent toxic effects. The degree of toxicity of the oligomeric species results from a complex interplay between the structural and physicochemical features of both the oligomers and the cellular membrane. Neuronal differentiation of human mesenchymal stromal cells increases their resistance to Aβ42 aggregate toxicity.

+ Show more
Purchase
Elisa Evangelisti nel 2008 si è laureata in Biotecnologie Mediche presso l’Università di Firenze. Nel 2012 ha conseguito il titolo di Dottore di Ricerca in Biochimica e Biologia Applicata. È coautrice di molteplici pubblicazioni su riviste internazionali con peer review.
PDF
  • Publication Year: 2013
  • Pages: 152
  • eISBN: 978-88-6655-445-5
  • Content License: CC BY-ND 3.0 IT
  • © 2013 Author(s)

XML
  • Publication Year: 2013
  • eISBN: 978-88-9273-471-5
  • Content License: CC BY-ND 3.0 IT
  • © 2013 Author(s)

PRINT
  • Publication Year: 2013
  • Pages: 152
  • ISBN: 978-88-6655-444-8
  • Content License: CC BY-ND 3.0 IT
  • © 2013 Author(s)

Bibliographic Information

Book Title

Structural and functional aspects of membranes

Book Subtitle

The involvement of lipid rafts in Alzheimer’s disease pathogenesis. The interplay between protein oligomers and plasma membrane physicochemical features in determining cytotoxicity

Authors

Elisa Evangelisti

Peer Reviewed

Number of Pages

152

Publication Year

2013

Copyright Information

© 2013 Author(s)

Content License

CC BY-ND 3.0 IT

Metadata License

CC0 1.0

Publisher Name

Firenze University Press

DOI

10.36253/978-88-6655-445-5

ISBN Print

978-88-6655-444-8

eISBN (pdf)

978-88-6655-445-5

eISBN (xml)

978-88-9273-471-5

Series Title

Premio Tesi di Dottorato

Series ISSN

2612-8039

Series E-ISSN

2612-8020

695

Fulltext
downloads

742

Views

Search in This Book
Export Citation
Suggested Books

1,346

Open Access Books

in the Catalogue

2,262

Book Chapters

3,790,127

Fulltext
downloads

4,420

Authors

from 923 Research Institutions

of 65 Nations

65

scientific boards

from 348 Research Institutions

of 43 Nations

1,248

Referees

from 381 Research Institutions

of 38 Nations