Lipids and Cellular Membranes in Amyloid Diseases E-Book

• Herausgeber: Wiley-VCH
• Kategorie: Wissenschaft und neue Technologien
• Sprache: Englisch

Seitenzahl: 601

Veröffentlichungsjahr: 2011

Beschreibung

Addressing one of the biggest riddles in current molecular cell biology, this ground-breaking monograph builds the case for the crucial involvement of lipids and membranes in the formation of amyloid deposits. Tying together recent knowledge from in vitro and in vivo studes, and built on a sound biophysical and biochemical foundation, this overview brings the reader up to date with current models of the interplay between membranes and amyloid formation.
Required reading for any researcher interested in amyloid formation and amyloid toxicity, and possible avenues for the prevention or treatment of neurodegenerative disorders.

From the contents:

* Interactions of Alpha-Synuclein with Lipids
* Interaction of hIAPP and its Precursors with Membranes
* Amyloid Polymorphisms: Structural Basis and Significance in Biology and Molecular Medicine
* The Role of Lipid Rafts in Alzheimer's Disease
* Alzheimer's Disease as a Membrane-Associated Enzymopathy of Beta-Amyloid Precursor Protein (APP) Secretases
* Impaired Regulation of Glutamate Receptor Channels and Signaling Molecules by Beta-Amyloid in Alzheimer's Disease
* Membrane Changes in BSE and Scrapie
* Experimental Approaches and Technical Challenges for Studying Amyloid-Membrane Interactions

and more

Leseprobe

Contents

Cover

Further Reading

Title Page

Copyright

Preface

List of Contributors

Chapter 1: Interactions of α-Synuclein with Lipids and Artificial Membranes Monitored by ESIPT Probes

1.1 Introduction to Parkinson's Disease and α-Synuclein

1.2 Structural Biology of α-Synuclein

1.3 Methods for Studying AS–Lipid Interactions

1.4 AS–Lipid Interactions

1.5 Interactions of Monomeric AS with Artificial Membranes Monitored with ESIPT Probes

1.6 Aggregation of AS and the Effects of Fatty Acids Monitored with ESIPT Probes

1.7 Concluding Remarks

Acknowledgments

References

Chapter 2: Structural and Functional Insights into a–Synuclein–Lipid Interactions

2.1 Introduction

2.2 Interaction of α-Synuclein with Model Membrane Systems

2.3 Biological Significance

Acknowledgments

References

Chapter 3: Surfactants and Alcohols as Inducers of Protein Amyloid: Aggregation Chaperones or Membrane Simulators?

3.1 Introduction

3.2 Aggregation in the Presence of Surfactants

3.3 Palimpsests of Future Functions: Cytotoxic Protein–Lipid Complexes

3.4 Aggregation in Fluorinated Organic Solvents

3.5 From Mimetics to the Real Thing: Aggregation on Lipids

3.6 Summary

References

Chapter 4: Interaction of hIAPP and Its Precursors with Model and Biological Membranes

4.1 Introduction

4.2 Results

4.3 Conclusions

Acknowledgments

References

Chapter 5: Amyloid Polymorphisms: Structural Basis and Significance in Biology and Molecular Medicine

5.1 Introduction

5.2 Only Generic Data Are Currently Available on the Structural Features of Amyloid Oligomers

5.3 The Plasma Membrane Can Be a Primary Site of Amyloid Oligomer Generation and Interaction

5.4 Oligomer/Fibril Polymorphism Can Underlie Amyloid Cytotoxicity

5.5 Amyloid Oligomers Grown Under Different Conditions Can Display Variable Cytotoxicity by Interacting in Different Ways with the Cell Membranes

5.6 Conclusions

Acknowledgments

References

Chapter 6: Intracellular Amyloid ß: a Modification to the Amyloid Hypothesis in Alzheimer's Disease

6.1 Introduction

6.2 Evidence for the Presence of Intracellular Amyloid

6.3 Sources of Intracellular Amyloid

6.4 Relationship Between Intracellular and Extracelluar Amyloid

6.5 Prevention of Intracellular Amyloid Toxicity

6.6 Concluding Remarks

6.7 Disclosure Statement

Acknowledgments

References

Chapter 7: Lipid Rafts Play a Crucial Role in Protein Interactions and Intracellular Signaling Involved in Neuronal Preservation Against Alzheimer's Disease

7.1 Lipid Rafts: Keys to Signaling Platforms in Neurons

7.2 Estrogen Receptors Are Part of Signaling Platforms in Neuronal Rafts

7.3 Role of Lipid Raft ERα–VDAC Interactions in Neuronal Preservation Against Aβ Toxicity

7.4 Disruption of ERα–VDAC Complex in AD Brains

7.5 Future Studies

Acknowledgments

References

Chapter 8: Alzheimer's Disease as a Membrane-Associated Enzymopathy of ß-Amyloid Precursor Protein (APP) Secretases

8.1 Introduction

8.2 Intramembrane-Cleaving Enzyme of Type I Membrane Proteins

8.3 Alcadein Processing by γ-Secretase in Alzheimer's Disease

References

Chapter 9: Impaired Regulation of Glutamate Receptor Channels and Signaling Molecules by ß-Amyloid in Alzheimer's Disease

9.1 Introduction

9.2 AMPAR-Mediated Synaptic Transmission and Ionic Current are Impaired by Aβ

9.3 CaMKII is Causally Involved in Aβ Impairment of AMPAR Trafficking and Function

9.4 PIP2 Regulation of NMDAR Currents is Lost by Aβ

9.5 The Effect of AChE Inhibitor on NMDAR Response is Impaired in APP Transgenic Mice

9.6 Aβ Impairs PKC-Dependent Signaling and Functions

9.7 Conclusion

References

Chapter 10: Membrane Changes in BSE and Scrapie

10.1 Prion Diseases

10.2 The Cellular Prion Protein (PrPc) and Conversion to Disease-Associated Prion Protein (PrPd)

10.3 PrPd Accumulation in the Central Nervous System and Lymphatic Tissues

10.4 Aberrant Endocytosis and Trafficking of PrPd in Neurons and Tingible Body Macrophages

10.5 Abnormal Maturation Cycle and Immune Complex Trapping of Follicular Dendritic Cells in Lymphoid Germinal Centers

10.6 Molecular Changes of Plasma Membranes Associated with PrPd Accumulation

10.7 Transfer of PrPd Between Cells

10.8 Extracellular Amyloid Form of PrPd

10.9 Strain-Directed Effects of Prion Infection

10.10 Conclusion and Perspectives

10.11 Summary

References

Chapter 11: Interaction of Alzheimer Amyloid Peptide with Cell Surfaces and Artificial Membranes

11.1 Introduction

11.2 Comparison of the Neurotoxicity of Oligomeric and Fibrillar Alzheimer Amyloid Peptides

11.3 Aβ Oligomerization at the Cell Surface

11.4 Catalysis of Aβ Oligomerization by the Cell Surface

11.5 Type of Aβ Complexes that Form on the Cell Surface

11.6 Association of Alzheimer Amyloid Peptides with Lipid Particles

11.7 Future Directions

Acknowledgments

References

Chapter 12: Experimental Approaches and Technical Challenges for Studying Amyloid–Membrane Interactions

12.1 Introduction

12.2 Unilamellar Vesicles and Micelles

12.3 Black Lipid Membranes

12.4 Langmuir Monolayers

12.5 Solid-Supported Bilayers

12.6 Other Techniques

12.7 Challenges and Future Work

References

Index

Further Reading

Gravanis, A. G., Mellon, S. H. (eds.)

Hormones in Neurodegeneration, Neuroprotection, and Neurogenesis

2011

ISBN: 978-3-527-32627-3

Ramirez-Alvarado, M., Kelly, J. W.,

Dobson, C. M. (eds.)

Protein Misfolding Diseases

Current and Emerging Principles and Therapies

2010

ISBN: 978-0-471-79928-3

Sipe, J. D. (ed.)

Amyloid Proteins

The Beta Sheet Conformation and Disease

2005

ISBN: 978-3-527-31072-2

Fielding, C. J. (ed.)

Lipid Rafts and Caveolae

From Membrane Biophysics to Cell Biology

2006

ISBN: 978-3-527-31261-0

Miller, L. W. (ed.)

Probes and Tags to Study Biomolecular Function

for Proteins, RNA, and Membranes

2008

ISBN: 978-3-527-31566-6

Pebay-Peyroula, E. (ed.)

Biophysical Analysis of Membrane Proteins

Investigating Structure and Function

2008

ISBN: 978-3-527-31677-9

Pignataro, B. (ed.)

Ideas in Chemistry and Molecular Sciences

Where Chemistry Meets Life

2010

ISBN: 978-3-527-32541-2

The Editor

Prof. Raz Jelinek

Ben Gurion Univ. of the Negev epartment of Chemistry Staedler Minerva Center 84105 Beer Sheva Israel

All books published by Wiley-VCH are carefully produced. Nevertheless, authors, editors, and publisher do not warrant the information contained in these books, including this book, to be free of errors. Readers are advised to keep in mind that statements, data, illustrations, procedural details or other items may inadvertently be inaccurate.

Library of Congress Card No.: applied for

British Library Cataloguing-in-Publication Data

A catalogue record for this book is available from the British Library.

Bibliographic information published by the Deutsche Nationalbibliothek

The Deutsche Nationalbibliothek lists this publication in the Deutsche Nationalbibliografie; detailed bibliographic data are available on the Internet at http://dnb.d-nb.de.

© 2011 WILEY-VCH Verlag & Co. KGaA, Boschstr. 12, 69469 Weinheim, Germany

All rights reserved (including those of translation into other languages). No part of this book may be reproduced in any form – by photoprinting, microfilm, or any other means – nor transmitted or translated into a machine language without written permission from the publishers. Registered names, trademarks, etc. used in this book, even when not specifically marked as such, are not to be considered unprotected by law.

ISBN: 978-3-527-32860-4

ISBN: oBook: 978-3-527-63432-3

ISBN ePDF: 978-3-527-63434-7

ISBN ePub: 978-3-527-63433-0

ISBN Mobi: 978-3-527-63435-4

Preface

Amyloid diseases affect millions of people. However, despite the devastating health consequences and economic cost of these pathologies, we still struggle to understand their causes and develop effective therapies. While aggregation of amyloidogenic proteins is considered a hallmark of amyloid diseases, the significance and physiological impact of protein aggregation phenomena are still not clear. Cellular membranes and their lipid constituents appear to exhibit significant, perhaps even central, roles in affecting the biological properties and toxic effects of amyloid proteins. Studying the relationships between amyloid proteins and cellular membranes has been, until fairly recently, an “uncharted frontier.” However, the interplay between membranes and amyloid aggregation pathways, and deciphering the physiological implications of amyloid–peptide/membrane interactions is currently attracting considerable interest both from a basic science point of view and also towards exploring new therapeutic avenues. This book is designed to highlight important aspects of this expanding topic, emphasizing the diversity of peptide systems, membrane assemblies, and biological phenomena investigated in the past few years.

This comprehensive volume reviews research work which utilized both model membranes and living cells, aimed at characterizing and better understanding membrane interactions of amyloid proteins. Chapter 1 (Jovin) describes applications of artificial membrane surfaces and fluorescent probes for studying lipid interactions of α-synuclein, the amyloidogenic peptide primarily associated with Parkinson's disease. α-Synuclein is also the focus of Chapter 2 (Subramaniam), which depicts structural and functional analyses of the peptide in different oligomeric forms, using various model membrane systems. Applications of artificial bilayer systems for studying membrane interactions are also discussed in the context of amylin, the amyloidogenic protein identified in type II diabetes (Chapter 4, Winter), and the amyloid-β peptide associated with Alzheimer's disease (Chapter 11, Chakrabartty).

Several chapters are devoted to investigations of amyloid–membrane interactions and their consequences within the complex environment of the cell, rather than model membrane systems. Intracellular interactions of amyloid-β as an underlining toxic factor are discussed in Chapter 6 (Zhang), while the contribution of lipid rafts within the cellular membrane as targets for amyloid-β and consequent toxicity through intracellular signaling is presented in Chapter 7 (Marin). The possible central roles of membrane-associated enzyme catalysis (Chapter 8, Suzuki) and membrane-embedded receptors (Chapter 9, Yan) in Alzheimer's disease are also analyzed. The neuropathology of prion diseases and putative correlations with membrane modulations are discussed in Chapter 10 (Ersdal).

Additional more general contributions complement the above chapters (which focus on specific amyloid proteins and/or cell and membrane models). A critical overview of investigations of amyloid proteins interactions with simple surfactants and alcohols perceived as membrane mimetics is provided in Chapter 3 (Otzen). The significance of amyloid polymorphism as a prominent factor affecting membranes and toxicity is highlighted in Chapter 5 (Stefani). Finally, we summarize the plethora of experimental approaches employed for investigating membrane interactions of amyloid peptides (Chapter 12, Jelinek).

Raz Jelinek

January 2011

Beersheva, Israel

List of Contributors

David A. Bateman

National Institutes of Health

National Institute of Diabetes, Digestive

and Kidney Diseases

Laboratory of Biochemistry and

Genetics

Bethesda, MD 20892

USA

Avijit Chakrabartty

University of Toronto

Department of Medical Biophysics

Toronto, ON, M5G 2M9

and

Canada

University of Toronto

Department of Biochemistry

Toronto, ON, M5S 1A8

Canada

Mireille M.A.E. Claessens

University of Twente

MESA+ Institute for Nanotechnology

Nanobiophysics

Drienerlolaan 5

7522 NB Enschede

The Netherlands

Cecilie Ersdal

Norwegian School of Veterinary Science

Department of Basic Sciences and

Aquatic Medicine

Ullevålsveien 72

0033 Oslo

Norway

Lisandro J. Falomir-Lockhart

Max Planck Institute for Biophysical

Chemistry

Laboratory of Cellular Dynamics

Am Fassberg 11

37077 Göttingen

Germany

Andrea Gohlke

Technical University of Dortmund

Faculty of Chemistry

Physical Chemistry I – Biophysical

Chemistry

Otto-Hahn-Strasse 6

44227 Dortmund

Germany

Saori Hata

Hokkaido University

Graduate School of Pharmaceutical

Sciences

Laboratory of Neuroscience

Kita 12 Nishi 6, Kita-ku

Sapporo 060-0812

Japan

Martin Jeffrey

Veterinary Laboratories

Agency – Lasswade

Pentland Science Park

Bush Loan, Penicuik

Midlothian EH26 0PZ

UK

Raz Jelinek

Ben Gurion University

Department of Chemistry

1 Ben Gurion Ave

Beer Sheva 84105

Israel

Christoph Jeworrek

Technical University of Dortmund

Faculty of Chemistry

Physical Chemistry I – Biophysical

Chemistry

Otto-Hahn-Strasse 6

44227 Dortmund

Germany

Suman Jha

Technical University of Dortmund

Faculty of Chemistry

Physical Chemistry I – Biophysical

Chemistry

Otto-Hahn-Strasse 6

44227 Dortmund

Germany

Thomas M. Jovin

Max Planck Institute for Biophysical

Chemistry

Laboratory of Cellular Dynamics

Am Fassberg 11

37077 Göttingen

Germany

Raquel Marin

Laboratory of Cellular Neurobiology

Department of Physiology

School of Medicine

Institute of Biomedical Technologies

La Laguna University

38320 La Laguna

Spain

Gillian McGovern

Veterinary Laboratories

Agency – Lasswade

Pentland Science Park

Bush Loan, Penicuik

Midlothian EH26 0PZ

UK

Rajesh Mishra

Technical University of Dortmund

Faculty of Chemistry

Physical Chemistry I – Biophysical

Chemistry

Otto-Hahn-Strasse 6

44227 Dortmund

Germany

Simone Möbitz

Technical University of Dortmund

Faculty of Chemistry

Physical Chemistry I – Biophysical

Chemistry

Otto-Hahn-Strasse 6

44227 Dortmund

Germany

Daniel E. Otzen

Aarhus University

Interdisciplinary Nanoscience Center

(iNANO)

Department of Molecular Biology

Gustav Wieds Vej 10C

8000 Aarhus C

Denmark

Diana Radovan

Technical University of Dortmund

Faculty of Chemistry

Physical Chemistry I – Biophysical

Chemistry

Otto-Hahn-Strasse 6

44227 Dortmund

Germany

Yuhki Saito

Hokkaido University

Graduate School of Pharmaceutical

Sciences

Laboratory of Neuroscience

Kita 12 Nishi 6, Kita-ku

Sapporo 060-0812

Japan

Janine Seeliger

Technical University of Dortmund

Faculty of Chemistry

Physical Chemistry I – Biophysical

Chemistry

Otto-Hahn-Strasse 6

44227 Dortmund

Germany

Daniel Sellin

Technical University of Dortmund

Faculty of Chemistry

Physical Chemistry I – Biophysical

Chemistry

Otto-Hahn-Strasse 6

44227 Dortmund

Germany

Tania Sheynis

Ben Gurion University

Department of Chemistry

1 Ben Gurion Ave

Beer Sheva 84105

Israel

Volodymyr V. Shvadchak

Max Planck Institute for Biophysical

Chemistry

Laboratory of Cellular Dynamics

Am Fassberg 11

37077 Göttingen

Germany

Massimo Stefani

University of Florence

Department of Biochemical Sciences

and Research Centre on the Molecular

Basis of Neurodegeneration

Viale Morgagni 50

50134 Florence

Italy

Martin Stöckl

University of Twente

MESA+ Institute for Nanotechnology

Nanobiophysics

Drienerlolaan 5

7522 NB Enschede

The Netherlands

Vinod Subramaniam

University of Twente

MESA+ Institute for Nanotechnology

and MIRA Institute for Biomedical

Technology and Technical Medicine

Nanobiophysics

Drienerlolaan 5

7522 NB Enschede

The Netherlands

Toshiharu Suzuki

Hokkaido University

Graduate School of Pharmaceutical

Sciences

Laboratory of Neuroscience

Kita 12 Nishi 6, Kita-ku

Sapporo 060-0812

Japan

Bart D. van Rooijen

University of Twente

MESA+ Institute for Nanotechnology

Nanobiophysics

Drienerlolaan 5

7522 NB Enschede

The Netherlands

Katrin Weise

Technical University of Dortmund

Faculty of Chemistry

Physical Chemistry I – Biophysical

Chemistry

Otto-Hahn-Strasse 6

44227 Dortmund

Germany

Roland Winter

Technical University of Dortmund

Faculty of Chemistry

Physical Chemistry I – Biophysical

Chemistry

Otto-Hahn-Strasse 6

44227 Dortmund

Germany

Zhen Yan

State University of New York at Buffalo

School of Medicine and Biomedical

Sciences

Department of Physiology & Biophysics

Buffalo, NY 14214

USA

Dmytro A. Yushchenko

Max Planck Institute for Biophysical

Chemistry

Laboratory of Cellular Dynamics

Am Fassberg 11

37077 Göttingen

Germany

Yan Zhang

Peking University

College of Life Sciences

State Key Laboratory of Biomembrane

and Membrane Biotechnology

Laboratory of Neurobiology

5 Yiheyuan Road, Haidian District

Beijing 100871

China