A Guide to Zona Pellucida Domain Proteins

ISBN-13: 9780470528112 / Angielski / Twarda / 2015 / 200 str.

Paul Wassarman; Eveline Litscher; Vladimir Uversky

Opis

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

Spis treści

List of Tables xi

Introduction to the Wiley Series on Protein and Peptide Science xiii

Preface xv

Acknowledgments xvii

List of Abbreviations xix

Part A Zona Pellucida Domain Proteins 1

A.1 Nature of the Zona Pellucida Domain 1

A.2 Mouse ZP Proteins 2

A.3 Synthesis, Secretion, and Assembly of ZP Proteins 7

A.4 Structure of the ZPD 13

A.5 Evolution of ZPD Proteins 18

Part B Mammalian Zona Pellucida Proteins 21

B.1 Introduction 21

B.2 Monotremes 22

B.3 Marsupials 24

B.4 Placental Mammals 25

B.4.a Mouse 26

B.4.b Rat 26

B.4.c Hamster 28

B.4.d Rabbit 30

B.4.e Cow 32

B.4.f Pig 33

B.4.g Dog 35

B.4.h Monkey 36

B.4.i Chimpanzee 38

B.4.j Human 40

B.5 Mammalian ZP Proteins as Antifertility Vaccines 45

B.6 Summary Tables 48

Part C Mammalian Zona Pellucida Domain Proteins 53

C.1 Betaglycan/TGF ]Receptor Type III 53

C.2 CUB and Zona Pellucida ]like Domain 1 (CUZD ]1) Proteins 55

C.2.a UTCZP/Itmap–1 55

C.2.b UO–44/ERG–1 56

C.3 Deleted in Malignant Brain Tumor 1 (DMBT1) Proteins 58

C.3.a CRP–Ductin 58

C.3.b DMBT1 60

C.3.c Ebnerin 62

C.3.d Hensin 63

C.3.e Vomeroglandin 65

C.4 Endoglin/CD ]105 66

C.5 Liver ]Specific ZPD ]Containing Protein (LZP) 68

C.6 Oocyte ]Secreted Protein 1 (Oosp1) 69

C.7 Pancreatic Zymogen Granule Protein (GP ]2) 70

C.8 Placenta ]Specific 1 (Plac1) 71

C.9 Tectorin ] and ] 72

C.10 Uromodulin/Tamm Horsfall Protein 78

C.11 Uromodulin ]like Proteins 81

C.12 Summary Tables 84

Part D Non ]mammalian Zona Pellucida Domain Proteins 87

D.1 Jellyfish (Aurelia aurita) 87

D.1.a Mesoglein 87

D.2 Sea Urchins (Strongylocentrotus purpuratus) 90

D.2.a Oit–3 90

D.2.b UO–44 90

D.3 Nematodes (Caenorhabditis elegans) 91

D.3.a Cuticlins 91

D.3.b DYF–7 93

D.3.c RAM–5 94

D.4 Mollusks (Haliotis rufescens) 96

D.4.a Vitelline envelope ZPs 96

D.5 Fruit Flies (Drosophila melanogaster) 101

D.5.a Dusky (dy), dusky–like (dyl), and miniature (m) 102

D.5.b Dumpy (dp) 104

D.5.c NompA (nompA) 105

D.5.d Papillote (pot) and piopio (pio) 107

D.5.e Quasimodo (qsm) 109

D.5.f Shavenbaby target genes (cyr, dyl, m, mey, neo, nyo, tyn, and zye) 109

D.6 Tunicates: Vitelline Coat Proteins and Oikosins 113

D.6.a Ciona: CiVC–16, –20, –182–1, –569 114

D.6.b Halocynthia: HrVC–120, HaVC–130 115

D.6.c Oikopleura: oikosins 117

D.7 Fish: Vitelline Envelope Proteins 118

D.7.a Salmonidae 119

D.7.b Cyprinidae 121

D.7.c Sparidae 122

D.7.d Adrianichthyidae 124

D.7.e Cynoglossidae 125

D.8 Amphibians: Vitelline Envelope Proteins 127

D.8.a Xenopus laevis 127

D.8.b Bufo arenarum 130

D.9 Reptiles: Predicted ZPD Proteins 133

D.9.a Anolis carolinensis 133

D.9.b Chelonia mydas 135

D.9.c Ophiophagus hannah 136

D.10 Birds: Vitelline Envelope Proteins 138

D.10.a Chicken vitelline envelope proteins 140

D.10.b Quail vitelline envelope proteins 143

D.11 Summary Tables 145

Part E Appendix 149

E.1 Sources of Sequence Information 149

E.2 Site(s) of ZP Protein Synthesis 154

E.3 Characteristics of Mammalian and Non–Mammalian ZPD Proteins 155

E.4 Comparison of Vertebrate ZP Proteins and Human ZP1 4 159

E.5 Sequence Alignments of ZPDs with 11 Cys Residues 161

E.5A Positions of Cys Residues of ZPDs with 11 Cys Residues 162

E.5B Positions of Cys Residues of Drosophila ZPDs with 11 Cys Residues 165

Index 167

O autorze

Eveline S. Litscher, Ph.D., is Assistant Professor in the Department of Developmental and Regenerative Biology at the Icahn School of Medicine at Mount Sinai in New York City. Previously a Swiss National Science Foundation post–doctoral fellow in the Department of Cell and Developmental Biology at the Roche Institute of Molecular Biology, she has more than 20 years of research experience working on extracellular coat proteins of mammalian and non–mammalian eggs, and  has published more than 45 primary papers and reviews.

Paul M. Wassarman, Ph.D., is Professor in the Department of Developmental and Regenerative Biology at the Icahn School of Medicine at Mount Sinai in New York City. Previously a faculty member in the Department of Biological Chemistry at Harvard Medical School and in the Department of Cell and Developmental Biology at the Roche Institute of Molecular Biology, he has more than 35 years of research experience working on extracellular coat proteins of mammalian and non–mammalian eggs, and has published more than 220 primary papers and reviews.

Blurb

Focuses on the great diversity of zona pellucida domain (ZPD) proteins in mammalian and non–mammalian animal species and the roles of ZPD proteins in biology

A ZPD is present in proteins that constitute the extracellular coats of mammalian and non–mammalian eggs, as well as in hundreds of other extracellular proteins found in multicellular organisms. ZPD mutations can result in Crohn s disease, deafness, cancer, or infertility.

A Guide to Zona Pellucida Domain Proteins provides a clear, comprehensive presentation of key features of ZPD proteins, from their structure and function to their evolution. Features include:

• A description of the synthesis and structure of mouse ZP proteins, prototypical ZPD proteins, followed by a description of ZPD structure and function, evolution of ZPD proteins, and use of mammalian ZP proteins as anti–fertility vaccines
• A survey of ZP proteins in mammals, from monotremes to placental mammals
• A survey of ZPD proteins in mammals, from platypus to human beings
• A survey of ZPD proteins in non–mammals, from jellyfish to birds
• References and Summary Tables of comparative data on ZPD proteins
• Appendix with Tables of comparative data on mammalian and non–mammalian ZPD proteins

Written with advanced undergraduate students, graduate students, and practicing scientists in mind, the Guide should be useful to anyone interested in learning about or working on ZPD proteins.