The Mouse Egg's Zona Pellucida

Wassarman, Paul M.; Litscher, Eveline S.

doi:10.1016/bs.ctdb.2018.01.003

Cited by 51 publications

(50 citation statements)

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“…Notably, the biosynthesis of egg coats also varies significantly among vertebrate species, both in terms of where subunits are synthesized and the kinetics of their incorporation. However, it was conclusively established that mouse ZP components are coordinately synthesized over the course of 2–3 weeks by the growing oocyte (Wassarman & Litscher, 2018), whereas granulosa cells may possibly also contribute to the synthesis of human ZP subunits (Gupta, 2018).…”

Section: Egg Coat Composition Structure and Functionmentioning

confidence: 99%

“…The ZP has different functions depending on the developmental status of the oocyte/embryo (Wassarman & Litscher, 2018). During oocyte maturation and growth, the ZP maintains the essential connection between the oocyte and the supportive surrounding cells, the cumulus cells (Liu et al, 1996; Rankin et al, 1996).…”

Section: Egg Coat Composition Structure and Functionmentioning

confidence: 99%

“…Together with experiments using recombinant ZP2 expressed in insect cells as well as oocytes with hybrid egg coats containing different combinations of mouse and human ZP proteins (Avella, Baibakov, & Dean, 2014; Baibakov, Boggs, Yauger, Baibakov, & Dean, 2012), this led to the suggestion that sperm of both species bind to the N‐terminus of ZP2 independent of N ‐ and O ‐glycosylation (Tokuhiro & Dean, 2018). The currently available data does, however, not exclude that O ‐glycans positioned elsewhere on ZP3 may underlie its in vitro sperm‐binding activity (Han et al, 2010), and it is possible that the ZP3‐ and ZP2‐centric models of fertilization may simply reflect two alternative pathways of egg–sperm interaction (Wassarman & Litscher, 2018). Nonetheless, all studies agree with the observation that sperm binding to the ZP is abolished upon site‐specific cleavage of ZP2 (Bleil, Beall, & Wassarman, 1981; Gahlay et al, 2010), an event that, in turn, depends on the post‐fertilization exocytosis of the egg's cortical granules (CGs).…”

Section: Egg Coat Composition Structure and Functionmentioning

confidence: 99%

“…Additional studies should thus be undertaken to provide a definitive answer to these questions, in particular with relation to a possible role of the other glycosylation sites of ZP3. At the same time, it is important to consider that glycosylation‐independent recognition of ZP2 and sugar‐mediated binding to ZP3 may not necessarily be mutually exclusive, but rather contribute to a common “hybrid” mechanism (Visconti & Florman, 2010) or constitute alternative ways in which sperm can productively interact with the ZP to accomplish fertilization (Wassarman & Litscher, 2018).…”

Section: Cg Exocytosis Modifies the Zp After Fertilizationmentioning

confidence: 99%

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Mammalian egg coat modifications and the block to polyspermy

Fahrenkamp

Algarra

Jovine

2020

Molecular Reproduction Devel

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Fertilization by more than one sperm causes polyploidy, a condition that is generally lethal to the embryo in the majority of animal species. To prevent this occurrence, eggs have developed a series of mechanisms that block polyspermy at the level of the plasma membrane or their extracellular coat. In this review, we first introduce the mammalian egg coat, the zona pellucida (ZP), and summarize what is currently known about its composition, structure, and biological functions. We then describe how this specialized extracellular matrix is modified by the contents of cortical granules (CG), secretory organelles that are exocytosed by the egg after gamete fusion. This process releases proteases, glycosidases, lectins and zinc onto the ZP, resulting in a series of changes in the properties of the egg coat that are collectively referred to as hardening. By drawing parallels with comparable modifications of the vitelline envelope of nonmammalian eggs, we discuss how CG‐dependent modifications of the ZP are thought to contribute to the block to polyspermy. Moreover, we argue for the importance of obtaining more information on the architecture of the ZP, as well as systematically investigating the many facets of ZP hardening.

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Section: Egg Coat Composition Structure and Functionmentioning

confidence: 99%

Section: Egg Coat Composition Structure and Functionmentioning

confidence: 99%

Section: Egg Coat Composition Structure and Functionmentioning

confidence: 99%

Section: Cg Exocytosis Modifies the Zp After Fertilizationmentioning

confidence: 99%

See 2 more Smart Citations

Mammalian egg coat modifications and the block to polyspermy

Fahrenkamp

Algarra

Jovine

2020

Molecular Reproduction Devel

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“…The polymerization of ZP proteins into the higher order structure of the egg coat is best characterized in the mouse, where the egg coat matrix consists of heterodimers of ZP2 and ZP3 that polymerize non-covalently into long fibrils interconnected by cross-links of ZP1 (25,100,111). While intramolecular disulfide bonds stabilize the native conformation of secreted ZP proteins, the mouse egg coat matrix also contains intermolecular disulfide bonds in the form of cross-linking ZP1 homodimers (20,34,(112)(113)(114).…”

Section: Discussionmentioning

confidence: 99%

Proteomics support the threespine stickleback egg coat as a protective oocyte envelope

Killingbeck

Wilburn

Merrihew

et al. 2020

Preprint

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Proteomic characterization of stickleback egg coats 2 Abbreviations BEB: Bayes empirical Bayes C/Cys: cysteine C-terminal: carboxy-terminal CAM: carbamidomethyl modification CFCS: consensus furin cleavage site d N : number of nonsynonymous substitutions per nonsynonymous codon site d S : number of synonymous substitutions per synonymous codon site IAA: iodoacetamide N-terminal: amino-terminal NSAF: normalized spectral abundance factor ꞷ: d N /d S P/Q: proline/glutamine S/Ser: serine SS: signal sequence TMD: transmembrane domain ZP: zona pellucida ZP-C: C-terminal domain of ZP module ZP-N: N-terminal domain of ZP module AbstractAfter the end of the last ice age, ancestrally marine threespine stickleback fish (Gasterosteus aculeatus) have undergone an adaptive radiation into freshwater environments throughout the Northern Hemisphere, creating an excellent model system for studying molecular adaptation and speciation. Stickleback populations are reproductively isolated to varying degrees, despite the fact that they can be crossed in the lab to produce viable offspring.Ecological and behavioral factors have been suggested to underlie incipient stickleback Proteomic characterization of stickleback egg coats 3 speciation. However, reproductive proteins represent a previously unexplored driver of speciation. As mediators of gamete recognition during fertilization, reproductive proteins both create and maintain species boundaries. Gamete recognition proteins are also frequently found to be rapidly evolving, and their divergence may culminate in reproductive isolation and ultimately speciation. As an initial investigation into the contribution of reproductive proteins to stickleback reproductive isolation, we characterized the egg coat proteome of threespine stickleback eggs. In agreement with other teleosts, we find that stickleback egg coats are comprised of homologs to the zona pellucida (ZP) proteins ZP1 and ZP3. We explore aspects of stickleback ZP protein biology, including glycosylation, disulfide bonding, and sites of synthesis, and find many substantial differences compared to their mammalian homologs. Furthermore, molecular evolutionary analyses indicate that ZP3, but not ZP1, has experienced positive Darwinian selection across teleost fish. Taken together, these changes to stickleback ZP protein architecture suggest that the egg coats of stickleback fish, and perhaps fish more generally, have evolved to fulfill a more protective functional role than their mammalian counterparts. Data are available via ProteomeXchange with identifiers PXD017488 and PXD017489.

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Gene mutations impede oocyte maturation, fertilization, and early embryonic development

Fei

Zhou

2022

BioEssays

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Reproductive diseases are a long-standing problem and have become more common in the world. Currently, 15% of the world's population suffers from infertility, and half of them are women. Maturation of oocytes, successful fertilization, and high-quality embryos are prerequisites for pregnancy. With the development of assisted reproductive technology and advanced genetic assays, we have found that infertility in many young female patients is caused by mutations in various developmental regulators.These pathogenic factors may result in impediment of oocyte maturation, failure of fertilization or early embryonic development arrest. In this review, we categorize these clinically-identified, mutated genetic factors by their molecular characteristics: nuclear factors (PALT2, TRIP13, WEE2, TBPL2, REC114, MEI1 and CDC20), cytoplasmic factors (TLE6, PADI6, NLRP2/5, FBXO43, MOS and BTG4), a factor unique to primates (TUBB8), cell membrane factor (PANX1), and zona pellucida factors (ZP1-3). We compared discrepancies observed in phenotypes between human and mouse models to provide clues for clinical diagnosis and treatment of related reproductive diseases.

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The Mouse Egg's Zona Pellucida

Cited by 51 publications

References 100 publications

Mammalian egg coat modifications and the block to polyspermy

Mammalian egg coat modifications and the block to polyspermy

Proteomics support the threespine stickleback egg coat as a protective oocyte envelope

Gene mutations impede oocyte maturation, fertilization, and early embryonic development

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