A Guide to Zona Pellucida Domain Proteins E-Book

Eveline S. Litscher

• Herausgeber: John Wiley & Sons
• Kategorie: Wissenschaft und neue Technologien
• Serie: Wiley Series in Protein and Peptide Science
• Sprache: Englisch

Seitenzahl: 317

Veröffentlichungsjahr: 2015

Beschreibung

This book provides a coherent, clear, and uniform presentation of structural, genetic, molecular, and biochemical information available for the zona pellucida domain protein family, which impact pathologies such as infertility, deafness, and cancer. Furthermore it:

• Details information about the structure and function of the ZP domain in ZPDC-proteins
• Provides illustrations of the organization of ZPDC-proteins, the genes that encode the proteins, and examples of mutations in the ZP domain that cause diseases
• Speculates as to the evolution of the ZP domain and potential therapeutics for diseases stemming from ZP domain mutations
• Addresses mammalian and non-mammalian systems

Leseprobe

CONTENTS

COVER

TITLE PAGE

LIST OF TABLES

INTRODUCTION TO THE WILEY SERIES ON PROTEIN AND PEPTIDE SCIENCE

PREFACE

ACKNOWLEDGMENTS

LIST OF ABBREVIATIONS

PART A: ZONA PELLUCIDA DOMAIN PROTEINS

A.1 NATURE OF THE ZONA PELLUCIDA DOMAIN

FURTHER READING

A.2 MOUSE ZP PROTEINS

FURTHER READING

A.3 SYNTHESIS, SECRETION, AND ASSEMBLY OF ZP PROTEINS

FURTHER READING

A.4 STRUCTURE OF THE ZPD

FURTHER READING

A.5 EVOLUTION OF ZPD PROTEINS

FURTHER READING

PART B: MAMMALIAN ZONA PELLUCIDA PROTEINS

B.1 INTRODUCTION

B.2 MONOTREMES

FURTHER READING

B.3 MARSUPIALS

FURTHER READING

B.4 PLACENTAL MAMMALS

FURTHER READING

FURTHER READING

FURTHER READING

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FURTHER READING

FURTHER READING

FURTHER READING

FURTHER READING

FURTHER READING

B.5 MAMMALIAN ZP PROTEINS AS ANTIFERTILITY VACCINES

FURTHER READING

B.6 SUMMARY TABLES

PART C: MAMMALIAN ZONA PELLUCIDA DOMAIN PROTEINS

C.1 BETAGLYCAN/TGFβ-RECEPTOR TYPE III

FURTHER READING

C.2 CUB AND ZONA PELLUCIDA-LIKE DOMAIN 1 (CUZD-1) PROTEINS

FURTHER READING

C.3 DELETED IN MALIGNANT BRAIN TUMOR 1 (DMBT1) PROTEINS

FURTHER READING

FURTHER READING

FURTHER READING

FURTHER READING

FURTHER READING

C.4 ENDOGLIN/CD-105

FURTHER READING

C.5 LIVER-SPECIFIC ZPD-CONTAINING PROTEIN (LZP)

FURTHER READING

C.6 OOCYTE-SECRETED PROTEIN 1 (Oosp1)

FURTHER READING

C.7 PANCREATIC ZYMOGEN GRANULE PROTEIN (GP-2)

FURTHER READING

C.8 PLACENTA-SPECIFIC 1 (PLAC1)

FURTHER READING

C.9 TECTORIN-α AND -β

FURTHER READING

C.10 UROMODULIN/TAMM–HORSFALL PROTEIN

FURTHER READING

C.11 UROMODULIN-LIKE PROTEINS

FURTHER READING

C.12 SUMMARY TABLES

PART D: NON-MAMMALIAN ZONA PELLUCIDA DOMAIN PROTEINS

D.1 JELLYFISH (

AURELIA AURITA

)

FURTHER READING

D.2 SEA URCHINS (

STRONGYLOCENTROTUS PURPURATUS

)

FURTHER READING

D.3 NEMATODES (

CAENORHABDITIS ELEGANS

)

FURTHER READING

D.4 MOLLUSKS (

HALIOTIS RUFESCENS

)

FURTHER READING

D.5 FRUIT FLIES (

DROSOPHILA MELANOGASTER

)

FURTHER READING

D.6 TUNICATES: VITELLINE COAT PROTEINS AND OIKOSINS

FURTHER READING

D.7 FISH: VITELLINE ENVELOPE PROTEINS

FURTHER READING

D.8 AMPHIBIANS: VITELLINE ENVELOPE PROTEINS

FURTHER READING

D.9 REPTILES: PREDICTED ZPD PROTEINS

FURTHER READING

D.10 BIRDS: VITELLINE ENVELOPE PROTEINS

FURTHER READING

D.11 SUMMARY TABLES

PART E: APPENDIX

APPENDIX: TABLE E.1

APPENDIX: TABLE E.2

FURTHER READING

APPENDIX: TABLE E.3

APPENDIX: TABLE E.4

APPENDIX: TABLES E.5A AND E.5B

INDEX

END USER LICENSE AGREEMENT

List of Tables

Chapter 01

TABLE A.3.1 Conservation of the IHP and EHP of ZP3

TABLE A.4.1 Alignment of Additional Conserved Cys Residues in Trout ZP1

a

Chapter 02

TABLE B.6.1 Characteristics of ZPDs of Mammalian ZP Proteins

TABLE B.4.1 Molecular Weights and Abundance of Human ZP Proteins

TABLE B.4.2 Mutations in Human ZP1–4

TABLE B.5.1 Representative ZP-Based Antifertility Vaccines

TABLE B.6.2 CFCS Sequences of Mammalian ZP Proteins

TABLE B.6.3 Comparison of ZPDs of Mammalian ZP Proteins

TABLE B.6.4 Cys Residue Alignments for ZP–N Sub-Domains of Human ZP1-4

Chapter 03

TABLE C.12.1 Location of Mammalian ZPD Proteins

TABLE C.12.2 Additional Domains of Mammalian ZPD Proteins

TABLE C.12.3 Mammalian ZPD Proteins and Disease

Chapter 04

TABLE D.4.1 Sizes (aa) of H

. rufescens

VEZPs

TABLE D.8.1 Molecular Weights of X

. laevis

VE Proteins

TABLE D.8.2 Molecular Weights of B

. arenarum

VE Proteins

TABLE D.10.1 Molecular Weights of Chicken and Quail VE Proteins

TABLE D.11.1 Comparisons of Non-mammalian and mZP1–3 ZPDs

TABLE D.11.2 Comparisons of Non-mammalian VE/VC and mZP1–3 ZPDs

Chapter 05

TABLE E.1 Sources of Sequence Information

TABLE E.2 Site(s) of ZP Protein Synthesis

TABLE E.3 Characteristics of Mammalian and Non-mammalian ZPD Proteins

Table E.4 Comparison of Vertebrate ZP Proteins and Human ZP1–4

TABLE E.5A Positions of Cys Residues of ZPDs with 11 Cys residues. Shown are human/mouse/rat (h/m/r), zebrafish (z), and tunicate (t) ZPDs that have 11 Cys residues. The alignments of Cys residues in these ZPDs are compared to mZP2 that has 10 Cys residues.

TABLE E.5B Positions of Cys Residues of

Drosophila

ZPDs with 11 Cys Residues. These are compared with mZP2 that has 10 Cys residues.

List of Illustrations

Chapter 01

FIGURE A.1.1 Schematic representation of a ZPD. Each ZPD consists of

≃

260 aa and the ZP-N and ZP-C sub-domains are connected by a short protease-sensitive linker region.

FIGURE A.2.1 Light and electron micrographs of the mouse ZP. (a) Light micrograph of sperm bound to the mouse egg’s ZP. Bar

≃

13 µm. (b) Scanning electron micrograph of the mouse egg’s ZP. Bar

≃

200 nm. © Journal of Biological Chemistry.

FIGURE A.2.2 Schematic representation of the organization of mZP1, 2 and 3. In each case, the polypeptide contains an SS at the N-terminus, a ZPD, and a CFCS, TMD, and CT at the CTP. mZP1 also has a trefoil (P) domain adjacent to the ZPD and an extra ZP-N sub-domain close to the N-terminus of the polypeptide. mZP2 has three extra ZP-N sub-domains between the ZPD and N-terminus of the polypeptide. mZP3, the smallest of the three proteins, consists primarily of a ZPD.

FIGURE A.3.1 Transmission electron micrographs of mouse ZP fibrils. Shown are (a) adsorbed, negatively stained, (b) sprayed, unidirectionally-shadowed, and (c) freeze-dried, unidirectionally-shadowed enzyme-solubilized preparations of ZP fibrils. © Springer.

FIGURE A.3.2 Schematic representation of various features of mZP3. Shown are the positions of the SS (aa 1–22), ZPD (aa 45–302), IHP (aa 170–177), CFCS (aa 350–353), EHP (aa 357–369), TMD (aa 387–409), and CT (aa 410–424). The aa sequence of the CTP of mZP3, from aa 350–424, is shown together with the positions of the CFCS, EHP, TMD, and CT. Note that the IHP is located in the ZP-N sub-domain of the ZPD and that the EHP is located between the CFCS and TMD.

FIGURE A.3.3 Schematic representation of the effect of mutation of the EHP or IHP of mouse ZP proteins with and without a TMD. Top panel. In the absence of a TMD, mutation of either the EHP or IHP results in failure to secrete nascent ZP proteins. Bottom panel. In the presence of a TMD, mutation of either the EHP or IHP has no effect on the secretion of nascent ZP proteins but results in failure to assemble the proteins into a matrix.

FIGURE A.3.4 Schematic representation of a general mechanism for assembly of nascent ZP proteins. In all ZPD precursor proteins (precursor) the ZPD is followed by a CTP that contains a basic cleavage site, such as a CFCS, an EHP, and, in most cases, a TMD or GPI-anchor site. Precursors do not polymerize within the cell either as a result of direct interaction between the EHP and IHP or because they adopt a conformation dependent on the presence of both hydrophobic patches. C-terminal processing at the CFCS by a pro-protein convertase (cleaved at CFCS) leads to dissociation of mature proteins from the EHP and activation of the ZPD (activated ZPD) for assembly (polymerized) into fibrils and matrices.

FIGURE A.4.1 In each representation, the positions of the ZPD and TMD are indicated. For ZP1 and 4, the postion of the trefoil domain (P) is indicated and for ZPd the position of the EGF domain is indicated. Note the extra copy or copies of the ZP-N sub-domain in ZP1, 2, 4 and ax.

FIGURE A.4.2 Schematic representation of intramolecular disulfides in ZP3-like (type-I) and ZP1/2-like (type-II) ZPD proteins. Top: ZP3-like ZP-N sub-domain with four Cys residues linked 1,4 and 2,3 and ZP-C sub-domain with four Cys residues linked 5,7 and 6,8. Bottom: ZP1/2-like ZP-N sub-domain with four Cys residues linked 1,4 and 2,3 and ZP-C sub-domain with six Cys residues linked 5,6, 7,a, and b,8.

FIGURE A.4.3 Chicken ZP3 homodimer structure formed by two ZP modules each consisting of a ZP-N and ZP-C sub-domain. Dashed lines represent disordered loops. © Elsevier.

FIGURE A.4.4 Topology scheme of chicken ZP3 with secondary structure and disulfide connectivity. © Elsevier. [Note: In this figure, V54 corresponds to V63 and N316 corresponds to N325 in the chicken ZP3 sequence.]

FIGURE A.5.1 Phylogenetic relationships of ZPD proteins as depicted in the “tree of life.” A ZPD is present as early as

≃

600 million years ago in jellyfish (Part D.1). ZPD proteins that have diverse functions are found in every major animal group and in a wide variety of tissues and organs.

FIGURE A.5.2 Evolutionary scheme of the organization of

ZP

genes in mammals, fish, amphibians, reptiles, and birds.

ZP1–4

are found in mammals and other vertebrates,

ZPd

in amphibians and birds, and

ZPax

in fish, amphibians, and birds.

Chapter 02

FIGURE B.4.1 Electron micrographs of the human ZP. Left panel. Transmission electron micrograph of a mature oocyte (MO) with ZP (arrowheads: irregular margin) (1,500×). Right panel. Scanning electron micrograph of the outer surface of the ZP. Fibrils are arranged in fine networks and appear as a beads-on-a-string structure (50,000×).

FIGURE B.4.2 Human oocytes with ZP anomalies. (a) A split in the ZP. (b) Oval shaped ZP. (c) Thin ZP. (d). Thick ZP. .

Chapter 03

FIGURE C.2.1 Domain organization of mouse UTCZP1/Itmap-1.

FIGURE C.3.1 Domain organization of mouse DMBT1.

FIGURE C.3.2 Domain organization of rat ebnerin.

FIGURE C.3.3 Domain organization of rabbit hensin.

FIGURE C.3.4 Domain organization of mouse vomeroglandin.

FIGURE C.5.1 Domain organization of mouse LZP.

FIGURE C.8.1 Domain organization of human Plac1.

FIGURE C.9.1 Ultrastructure of the tectorial membrane. Electron micrograph of the striated sheet matrix.

FIGURE C.9.2 Domain organization of human tectorin-α.

FIGURE C.9.3 Domain organization of human tectorin-β.

FIGURE C.10.1 Electron micrographs of negatively stained and unidirectionally shadowed samples. First panel. Fibrillar structure of native uromodulin. Second panel. Uromodulin-ZPD, encompassing aa residues 292–587. Third panel. A single uromodulin-ZPD fibril, suggesting an overall double-helical structure. Fourth panel. Unidirectionally shadowed ZP fibril samples. Panels 1–3, bars 0.1 µm. Panel 4,

≃

100,000×.

FIGURE C.10.2 Domain organization of human UMOD.

FIGURE C.10.3 Missense mutations in the ZPD of human uromodulin.

Chapter 04

FIGURE D.1.1 Light micrograph of a growing

A. aurita

oocyte. CP, contact plate; ge, germinal epithelium; N, nucleus; O, oocyte.

FIGURE D.1.2 Contact plate at higher magnification at the final stage of oocyte maturation. CP, contact plate; ge, germinal epithelium; O, oocyte. Bar, 5 µm.

FIGURE D.3.1 Outside surface of cuticle on the lateral side bearing circumferential ridges (annuli) and furrows. Alae form over the seam cells. Bar, 10 µm.

FIGURE D.3.2 DEX-1 and DYF-7 are required for dendrite extension. (a) Wild-type. (b) Mutant

dex-1

. (c) Mutant

dyf-7

. Neurons are yellow, sheat glia are red, and socket glia are blue. Ax, axon; Dn, dendrite.

FIGURE D.3.3 Morphology of a wild-type male tail.

FIGURE D.4.1 Dark-field light micrograph of isolated

H. rufescens

egg coats (

≂

290X).

FIGURE D.4.2 Electron micrograph of the fibrous matrix of the

H. rufescens

VE following dissolution by lysin (

≂

75,000X).

FIGURE D.4.3 Comparison of the organization of abalone VEZP14 and VERL

.

Note that VEZP14 has 20 serine/threonine repeats and 1 extra ZP-N sub-domain in addition to a ZPD and TMD. VERL has 22 ZP-N sub-domains in addition to a ZPD and TMD.

FIGURE D.4.4 Conservation of Cys residues in the ZPD of VERL and VEZP14. The Cys residues are highlighted, capitalized, and underlined.

FIGURE D.4.5 Comparison of ZPD sequences for several different mammalian and non-mammalian species. Vertical bars indicate 43 identical positions in 4 of the 6 taxa; asterisks indicate 15 identical positions in all 6 taxa.

FIGURE D.5.1 Transmission electron micrographs of sections of wing epidermis of wild-type (a, c) and

dy

+

m

mutants (D

f

(

1

)

MR

) (b, d). (a) At 36 h after puparium formation (APF), the small patches of cuticulin envelope (arrowheads) appear at the tip of microvilli (mv) in the wild-type. (b) In the mutant, mv are shorter, and the process of cuticle deposition is less advanced (arrowheads). (c) At 44 h APF, the cuticulin envelope forms an almost continuous layer over the epidermis in both wild-type and mutant wings. In some regions (arrowheads), the characteristic trilayer can be observed, whereas in other regions (brackets) the cuticulin layer seems less organized. (d) The structure of the apical mv is disorganized in the mutant wings (mv). The process of wing extension is prevented in the

Df

(

1

)

MR

mutant (compare insets in panels c and d).

FIGURE D.5.2 Adult phenotypes of

dp

: Upper first panel. Wild-type wing. Upper second panel. Flies carrying the mutant

dp

o

(

oblique

) alleles have shortened wings, and altered paths of the wing veins caused by abnormal contraction of the wing epithelia during metamorphosis. Bottom first panel. Wild-type notum. Bottom second panel. Flies carrying the mutant

dp

v

(

vortex

) alleles display vortex-like depressions on the notum, coinciding with the locations of certain muscle attachment sites. The orientations of the bristles surrounding the vortex are disturbed.

FIGURE D.5.3 Schematic drawing of two sensory organs of

Drosophila.

(a) Mechanosensory bristle, an external sensory organ. (b) Chordotonal organ, an internal sensory organ.

FIGURE D.5.4 The absence of pio causes cuticle detachment and tracheal defects. (a) In wild-type embryos at the end of embryogenesis, the dorsal trunk of the trachea appears smooth and rather straight. (b) Homozygous

pio

mutant embryos complete development, but the tracheae appear twisted and broken (arrows). (c) In live wild-type embryos, the epidermis (marked with tubulin-GFP) closely follows the outline of the cuticle. (d) In homozygous

pio

mutant embryos, the cuticle detaches from the GFP-marked epidermis (arrow).

FIGURE D.5.5 Electron micrographs of denticles. ZPD mutants display specific alterations in epidermal cell shape. wt, wildtype. Bar, 500 nm.

FIGURE D.7.1 Transmission electron micrographs of ZP1β and ZP3 in buffer. Left panel. ZP1β (~200,000X)—arrows indicate contiguous beads along a fibril and asterisk indicates individual beads. Right panel. ZP3 fibrils (

≃

370,000X).

FIGURE D.8.1 Electron micrograph of the VE (

X. laevis

), quick frozen without fixation. Outer layer of VE. Large fibers run for long distances and occasionally form bundles. Intermediate-size fibrils often bifurcate. Fine filaments interconnect larger fibers and fibrils. Bar, 0.1 µm.

FIGURE D.10.1 Schematic diagram of a 3-dimensional view of the chicken VE. (a) cm, continuous membrane; il, inner layer; ol, outer layer. (b) cm, continuous membrane. (c) il, inner layer or PVL, perivitelline layer.

FIGURE D.10.2 Schematic representation of the chicken ZP3 homodimer.

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WILEY SERIES IN PROTEIN AND PEPTIDE SCIENCE

VLADIMIR N. UVERSKY, Series Editor

Metalloproteomics • Eugene A. Permyakov

Instrumental Analysis of Intrinsically Disordered Proteins: Assessing Structure and Conformation  • Vladimir Uversky and Sonia Longhi

Protein Misfolding Diseases: Current and Emerging Principles and Therapies • Marina Ramirez-Alvarado, Jeffery W. Kelly, Christopher M. Dobson

Calcium Binding Proteins • Eugene A. Permyakov and Robert H. Kretsinger

Protein Chaperones and Protection from Neurodegenerative Diseases • Stephan Witt

Transmembrane Dynamics of Lipids • Philippe Devaux and Andreas Herrmann

Flexible Viruses: Structural Disorder in Viral Proteins • Vladimir Uversky and Sonia Longhi

Protein Families: Relating Protein Sequence, Structure, and Function • Christine A. Orengo and Alex Bateman

Protein Aggregation in Bacteria: Functional and Structural Properties of Inclusion Bodies in Bacterial Cells • Silvia Maria Doglia and Marina Lotti

Chemistry of Metalloproteins: Problems and Solutions in Bioinorganic Chemistry • Joseph J. Stephanos and Anthony W. Addison

A Guide to Zona Pellucida Domain Proteins • Eveline S. Litscher and Paul M. Wassarman

A GUIDE TO ZONA PELLUCIDA DOMAIN PROTEINS

EVELINE S. LITSCHER

PAUL M. WASSARMAN

Wiley Series in Protein and Peptide Science

Copyright © 2015 by John Wiley & Sons, Inc. All rights reserved

Published by John Wiley & Sons, Inc., Hoboken, New JerseyPublished simultaneously in Canada

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Library of Congress Cataloging-in-Publication Data:

Wassarman, Paul M., author.     A Guide to Zona pellucida domain proteins / Eveline Litscher, Paul Wassarman.          p. ; cm. – (Wiley series in protein and peptide science)     Includes bibliographical references and index.

     ISBN 978-0-470-52811-2 (cloth)I.  Litscher, Eveline, author.     II.  Title.     III.  Series: Wiley series in protein and peptide science.  [DNLM:     1.  Zona Pellucida–physiology.     2.  Egg Proteins–physiology.     3.  Membrane Glycoproteins–physiology.     4.  Receptors, Cell Surface–physiology.     WQ 205]     QP552.P73     572′.68–dc23

          2014043043

The authors dedicate this guide to the memory of Jeffrey David Bleil (1952–2014), a most valued colleague and friend whose pioneering research on the mouse egg’s zona pellucida led to the discovery of the ubiquitous zona pellucida domain.

LIST OF TABLES

Table A.3.1

Conservation of the IHP and EHP of ZP3

Table A.4.1

Alignment of Additional Conserved Cys Residues in Trout ZP1

Table B.4.1

Molecular Weights and Abundance of Human ZP Proteins

Table B.4.2

Mutations in Human ZP1–4

Table B.5.1

Representative ZP-Based Antifertility Vaccines

Table B.6.1

Characteristics of ZPDs of Mammalian ZP Proteins

Table B.6.2

CFCS Sequences of Mammalian ZP Proteins

Table B.6.3

Comparison of ZPDs of Mammalian ZP Proteins

Table B.6.4

Cys Residue Alignments for ZP–N Sub-Domains of Human ZP1-4

Table C.12.1

Location of Mammalian ZPD Proteins

Table C.12.2

Additional Domains of Mammalian ZPD Proteins

Table C.12.3

Mammalian ZPD Proteins and Disease

Table D.4.1

Sizes (aa) of

H. rufescens

VEZPs

Table D.8.1

Molecular Weights of

X. laevis

VE Proteins

Table D.8.2

Molecular Weights of

B. arenarum

VE Proteins

Table D.10.1

Molecular Weights of Chicken and Quail VE Proteins

Table D.11.1

Comparisons of Non-mammalian and mZP1–3 ZPDs

Table D.11.2

Comparisons of Non-mammalian VE/VC and mZP1–3 ZPDs

Table E.1

Sources of Sequence Information

Table E.2

Site(s) of ZP Protein Synthesis

Table E.3

Characteristics of Mammalian and Non-mammalian ZPD Proteins

Table E.4

Comparison of Vertebrate ZP Proteins and Human ZP1–4

Table E.5A

Positions of Cys Residues of ZPDs with 11 Cys Residues

Table E.5B

Positions of Cys Residues of

Drosophila

ZPDs with 11 Cys Residues