Yu Claudins

1. Auflage 2010
ISBN: 978-0-12-381040-3
Verlag: Elsevier Science & Techn.
Format: EPUB
Kopierschutz: 6 - ePub Watermark

E-Book, Englisch, Band Volume 65, 373 Seiten

Reihe: Current Topics in Membranes

This volume of Current Topics in Membranes focuses on Membrane Protein Crystallization, beginning with a review of past successes and general trends, then further discussing challenges of mebranes protein crystallization, cell free production of membrane proteins and novel lipids for membrane protein crystallization.
This publication also includes tools to enchance membrane protein crystallization, technique advancements, and crystallization strategies used for photosystem I and its complexes, establishing Membrane Protein Crystallization as a needed, practical reference for researchers.

Autoren/Hrsg.

Yu, Alan

Inhaltsverzeichnis

1;Front Cover;1
2;Current Topics in Membranes;4
3;Copyright Page;5
4;Dedication;6
5;Contents;8
6;Contributors;14
7;Preface;18
8;Previous Volumes in Series;20
9;Chapter 1: Introduction: Claudins, Tight Junctions, and the Paracellular Barrier;24
9.1;I. Overview;24
9.2;II. Introduction;25
9.3;III. History of the Identification of Claudins;25
9.3.1;A. Identification of TJ-Associated Proteins by Immunological Approaches;25
9.3.2;B. Identification of the Claudin Family;27
9.4;IV. Structure of Claudins;28
9.5;V. TJ Formation by the Claudin Family;29
9.6;VI. Complex Structure of TJ Strands Formed by Multiple Claudin Subtypes;30
9.7;VII. Functional Diversity of the Barrier Property of Claudin-Based TJs;31
9.8;VIII. In vivo Functions of Claudins: Claudin-Deficient Mice and Hereditary Diseases with Claudin Mutations;33
9.9;IX. Dynamic Behavior of Claudin-Based TJs;35
9.10;X. Summary and Future Perspectives;36
9.11;Acknowledgments;37
9.12;References;37
10;Chapter 2: Morphological Studies of Claudins in the Tight Junction;44
10.1;I. Overview;44
10.2;II. Background;45
10.3;III. Claudins but not Occludin Form Tight Junction Strands;47
10.4;IV. Morphological Tools for the Study of Tight Junctions;48
10.4.1;A. Localization of Tight Junction Proteins by Immunofluorescence Microscopy;49
10.4.2;B. Localization of Tight Junction Proteins at the Ultrastructural Level;50
10.5;V. Claudins are Relatively Stable Components of the Tight Junction;54
10.6;VI. Claudin-Claudin Interactions;55
10.7;VII. Claudins, Regulators of Paracellular Ion Selectivity;56
10.8;VIII. Summary;57
10.9;References;57
11;Chapter 3: Biophysical Methods to Study Tight Junction Permeability;62
11.1;I. Overview;63
11.2;II. Introduction;63
11.3;III. Resistance Measurements;64
11.3.1;A. Transepithelial Resistance (TER, Rt);64
11.3.2;B. Chopstick Electrodes;65
11.3.3;C. Ussing Chamber;66
11.3.4;D. Impedance Spectroscopy;66
11.3.5;E. One-Path Impedance Spectroscopy;69
11.3.6;F. Two-Path Impedance Spectroscopy;70
11.3.7;G. Conductance Scanning;74
11.4;IV. Ion Permeability Measurements;76
11.4.1;A. Ion Flux Measurements;77
11.4.2;B. Dilution and Biionic Potentials;78
11.4.3;C. Conductance Measurements;80
11.5;V. Fluxes of Uncharged Paracellular Tracers;82
11.6;VI. Paracellular Water Transport;85
11.7;VII. Experimental Strategies for TJ Perturbation;87
11.7.1;A. Cell Culture Models: Overexpression and Knockdown;87
11.7.2;B. In Vivo Models: Knockout Mice;89
11.7.3;C. Established Mouse Models;90
11.8;VIII. Conclusion;93
11.9;References;94
12;Chapter 4: Structure-Function Studies of the Claudin Pore;102
12.1;I. Overview;102
12.2;II. Introduction;103
12.3;III. Methodological Challenges in Measuring Pore Function of Individual Claudins;103
12.4;IV. The First Extracellular Domain of Claudins Lines the Paracellular Pore;105
12.5;V. Molecular Basis of Charge Selectivity;106
12.6;VI. Size of Claudin Pores;111
12.7;VII. Mapping Residues onto the Structure of the Claudin Pore by Cysteine Mutagenesis;112
12.8;VIII. Stoichiometry of Claudin Pores;113
12.9;IX. Conclusions;115
12.10;References;115
13;Chapter 5: The Investigation of cis- and trans-Interactions Between Claudins;120
13.1;I. Overview;120
13.2;II. Introduction;121
13.3;III. Estimation of Interactions, Without Differentiation Between cis- and trans-Interaction;123
13.3.1;A. Conventional Techniques;123
13.3.2;B. Proteomic Approaches for Identifying Interaction Partners of Claudins;125
13.4;IV. Analysis of cis-Interactions Along the Plasma Membrane;127
13.5;V. Determination of trans-Interactions Between Opposing Cell Membranes;130
13.6;References;131
14;Chapter 6: Regulation of Claudins by Posttranslational Modifications and Cell-Signaling Cascades;136
14.1;I. Overview;137
14.2;II. Introduction;137
14.3;III. Claudin Phosphorylation;137
14.3.1;A. Phosphorylation of Claudins that Promotes their Assembly at Tight Junctions;138
14.3.2;B. Phosphorylation of Claudins that Modulates their Function as Tight Junction Pores;152
14.3.3;C. Phosphorylation of Claudins that Inhibits their Assembly at Tight Junctions;153
14.3.4;D. Kinases that Promote other Claudin Functions;154
14.3.5;E. Phosphorylation of Claudins in Cancerous Tissues;155
14.4;IV. Inhibition of Palmitoylation Impairs the Efficient Localization of Claudin-14 at Tight Junctions;156
14.5;V. Changes in Claudin Expression Triggered by Diverse Elements and Signaling Pathways;157
14.5.1;A. MAP Kinase;157
14.5.2;B. Rho Rack and CDC42 Pathways;158
14.5.3;C. Cytokines;159
14.5.4;D. Prostaglandins;163
14.5.5;E. Growth Factors;163
14.5.6;F. Hormones;164
14.6;References;167
15;Chapter 7: Claudins and Renal Magnesium Handling;174
15.1;I. Overview;174
15.2;II. Introduction;175
15.2.1;A. Claudins form Paracellular Channels in the Kidney;175
15.2.2;B. The Paracellular Reabsorption of Magnesium in the Kidney;176
15.3;III. Claudins and Human Renal Diseases of Magnesium Wasting;178
15.3.1;A. Mutations in CLDN16 Cause FHHNC;178
15.3.2;B. Mutations in CLDN19 Cause FHHNC;180
15.4;IV. Claudin Biology and Physiology;180
15.4.1;A. Biosynthesis, Trafficking, and Interaction of CLDN16 and CLDN19 Molecules;180
15.4.2;B. Biophysical Properties of CLDN16 and CLDN19 Paracellular Channels;185
15.5;V. Perspective;192
15.5.1;A. The Biochemical Nature of CLDN16 and CLDN19 Oligomerization;192
15.5.2;B. The Molecular Basis of CLDN16–CLDN19 Channel Charge Selectivity;192
15.5.3;C. Mouse Models Deficient in Both CLDN16 and CLDN19;193
15.6;Acknowledgments;194
15.7;References;194
16;Chapter 8: Claudins and Barrier Function of the Lung;200
16.1;I.Overview;201
16.2;II. Introduction;201
16.3;III. Profile of Claudin Expression in the Lung;203
16.3.1;A. Expression of Claudins in Proximal Airways;203
16.3.2;B. Expression of Claudins in Distal Lung;204
16.4;IV. Regulation of Claudin Expression in the Lung;205
16.5;V. Claudins and Barrier Functions of the Lung;206
16.6;VI. Claudins in Lung Pathology;209
16.7;VII. Concluding Remarks;212
16.8;Acknowledgments;213
16.9;References;213
17;Chapter 9: Claudins in Intestinal Function and Disease;218
17.1;I. Overview;219
17.2;II. Claudins in Intestinal Epithelia;219
17.2.1;A. Barrier and Channel Function of Intestinal Claudins;219
17.2.2;B. Claudins Along the Gut Axis;221
17.2.3;C. Two Effects of Claudin Dysfunction;222
17.3;III. Chronic Inflammatory Disorders of The Intestine;222
17.3.1;A. Crohn’s Disease;223
17.3.2;B. Ulcerative Colitis;224
17.3.3;C. Collagenous Colitis;226
17.3.4;D. Role of Cytokines in Altered Epithelial Barrier Function in IBD;227
17.3.5;E. Celiac Disease;228
17.4;IV. Intestinal Infections;230
17.4.1;A. Salmonella enterica;231
17.4.2;B. Clostridium perfringens, C. difficile, C. botulinum;232
17.4.3;C. Escherichia coli;232
17.4.4;D. Shigella flexneri;233
17.4.5;E. Campylobacter jejuni;234
17.4.6;F. Arcobacter butzleri;234
17.4.7;G. Helicobacter pylori;235
17.4.8;H. Human Immunodeficiency Virus (HIV);237
17.4.9;I. Norovirus;237
17.4.10;J. Rotavirus;238
17.4.11;K. Giardia lamblia (Giardiasis);238
17.4.12;L. Entamoeba histolytica (Amebiasis);239
17.4.13;M. Protection of Intestinal Barrier Function in Intestinal Diseases;239
17.5;V. Conclusion;240
17.6;References;240
18;Chapter 10: Claudin Proteins and Neuronal Function;252
18.1;I. Overview;252
18.2;II. Introduction;253
18.3;III. Function of TJs in the Invertebrate Nervous System;254
18.4;IV. Function of TJs in CNS Myelin;257
18.4.1;A. Myelin Sheath Development and Structure;257
18.4.2;B. Major Structural Proteins in CNS Myelin;257
18.4.3;C. TJs form the Radial Component in CNS Myelin;258
18.4.4;D. TJs Contribute to Myelin Membrane Resistance;258
18.4.5;E. Axoglial Junctions Contribute to Axonal Conduction Independently of TJs;260
18.4.6;F. Are TJs Immune-Protective or Adhesive Components of Myelin?;263
18.5;V. Potential Clinical Relevance of CNS Myelin TJs to Neurological Diseases;268
18.5.1;A. Schizophrenia;268
18.5.2;B. Multiple Sclerosis;269
18.6;VI. Role of Claudin 11 in CNS Development;270
18.7;VII. TJs in PNS Myelin;271
18.8;Acknowledgments;271
18.9;References;271
19;Chapter 11: Claudin is Skin Deep;278
19.1;I. Overview;278
19.2;II. Introduction;279
19.3;III. The Epidermis and Epidermal Terminal Differentiation;279
19.4;IV. Tight Junctions and the Tight Junction Permeability Barrier;281
19.4.1;A. TJs and the Discovery of Cldns;281
19.4.2;B. TJs and the Epidermis;283
19.4.3;C. Cldns and Epidermal Development and Function in Health and Disease;285
19.5;V. Conclusions-Challenges for the Future;290
19.6;Acknowledgments;291
19.7;References;291
20;Chapter 12: The Involvement of Tight Junction Protein Claudin-1 in Hepatitis C Virus Entry;296
20.1;I. Overview;296
20.2;II. Introduction;297
20.3;III. Soluble HCV Glycoprotein E2;298
20.4;IV. HCV Pseudoparticles;298
20.5;V. The JFH-1 Strain of HCV;299
20.6;VI. Discovery of Receptors;299
20.7;VII. CD81;300
20.8;VIII. Scavenger Receptor Class B Type I;301
20.9;IX. Claudins;302
20.10;X. Occludin;304
20.11;XI. Tight Junction Proteins and Virus Entry;305
20.12;XII. Effects of Cell Polarization on HCV Entry;307
20.13;Acknowledgments;309
20.14;References;309
21;Chapter 13: Claudins in Cancer Biology;316
21.1;I. Overview;316
21.2;II. Introduction;317
21.3;III. Aberrant Expression of Claudins in Cancer;318
21.4;IV. Regulation of Claudin Expression;323
21.4.1;A. Pathways Implicated in Claudin Regulation;323
21.4.2;B. Epigenetic Regulation;325
21.4.3;C. Transcriptional Regulation;326
21.4.4;D. Posttranslational Regulation;327
21.4.5;E. Localization of Claudins;328
21.5;V. Roles of Claudins in Tumorigenesis;329
21.6;VI. Clinical Implications of Claudin Overexpression in Cancer;334
21.6.1;A. Detection and Diagnosis;334
21.6.2;B. Prognosis;339
21.6.3;C. Therapy;340
21.7;VII. Concluding Remarks;341
21.8;References;342
22;Index;358
23;Color Plate;366