scholarly journals Biology of mammalian fertilization: role of the zona pellucida.

1992 ◽  
Vol 89 (4) ◽  
pp. 1055-1059 ◽  
Author(s):  
J Dean
Keyword(s):  
Zona Pellucida ◽  
Mammalian Fertilization

scholarly journals ZP3-dependent activation of sperm cation channels regulates acrosomal secretion during mammalian fertilization.

1996 ◽  
Vol 134 (3) ◽  
pp. 637-645 ◽  
Author(s):  
C Arnoult ◽  
Y Zeng ◽  
H M Florman
Keyword(s):  
Membrane Potential ◽  
Pertussis Toxin ◽  
Zona Pellucida ◽  
Mammalian Sperm ◽  
Transient Rise ◽  
Transduction Mechanisms ◽  
Dependent Signal ◽  
Sperm Membrane ◽  
Mammalian Fertilization

The sperm acrosome reaction is a Ca(2+)-dependent secretory event required for fertilization. Adhesion to the egg's zona pellucida promotes Ca2+ influx through voltage-sensitive channels, thereby initiating secretion. We used potentiometric fluorescent probes to determine the role of sperm membrane potential in regulating Ca2+ entry. ZP3, the glycoprotein agonist of the zona pellucida, depolarizes sperm membranes by activating a pertussis toxin-insensitive mechanism with the characteristics of a poorly selective cation channel. ZP3 also activates a pertussis toxin-sensitive pathway that produces a transient rise in internal pH. The concerted effects of depolarization and alkalinization open voltage-sensitive Ca2+ channels. These observations suggest that mammalian sperm utilize membrane potential-dependent signal transduction mechanisms and that a depolarization pathway is an upstream transducing element coupling adhesion to secretion during fertilization.

Profile of a mammalian sperm receptor

Development ◽  
1990 ◽  
Vol 108 (1) ◽  
pp. 1-17 ◽  
Author(s):  
P.M. Wassarman
Keyword(s):  
Gene Expression ◽  
Zona Pellucida ◽  
Specific Gene ◽  
Mammalian Development ◽  
Unique Nature ◽  
Mammalian Fertilization ◽  
Species Specific ◽  
Available Information ◽  
Mammalian Eggs ◽  
Sperm Receptor

Complementary molecules on the surface of eggs and sperm are responsible for species-specific interactions between gametes during fertilization in both plants and animals. In this essay, several aspects of current research on the mouse egg receptor for sperm, a zona pellucida glycoprotein called ZP3, are addressed. These include the structure, synthesis, and functions of the sperm receptor during oogenesis and fertilization in mice. Several conclusions are drawn from available information. These include (I) ZP3 is a member of a unique class of glycoproteins found exclusively in the extracellular coat (zona pellucida) of mammalian eggs. (II) ZP3 gene expression is an example of oocyte-specific and, therefore, sex-specific gene expression during mammalian development. (III) ZP3 is a structural glycoprotein involved in assembly of the egg extracellular coat during mammalian oogenesis. (IV) ZP3 is a sperm receptor involved in carbohydrate-mediated gamete recognition and adhesion during mammalian fertilization. (V) ZP3 is an inducer of sperm exocytosis (acrosome reaction) during mammalian fertilization. (VI) ZP3 participates in the secondary block to polyspermy following fertilization in mammals. (VII) The extracellular coat of other mammalian eggs contains a glycoprotein that is functionally analogous to mouse ZP3. The unique nature, highly restricted expression, and multiple roles of ZP3 during mammalian development make this glycoprotein a particularly attractive subject for investigation at both the cellular and molecular levels.

scholarly journals O ρόλος των ενεργοποιών του πλασμινογόνου και της πλασμίνης στην αναπαραγωγή των θηλαστικών

2017 ◽  
Vol 63 (2) ◽  
pp. 113
Author(s):  
M. TSANTARLIOTOU (Μ. ΤΣΑΝΤΑΡΛΙΩΤΟΥ) ◽  
V. SAPANIDOU (Β.ΣΑΠΑΝΙΔΟΥ) ◽  
I. ZERVOS (Ι. ΖΕΡΒΟΣ) ◽  
S. LAVRENTIADOU (Σ. ΛΑΥΡΕΝΤΙΑΔΟΥ) ◽  
I. TAITZOGLOU (Ι. ΤΑΪΤΖΟΓΛΟΥ) ◽  
...  
Keyword(s):  
Current Knowledge ◽  
Early Stage ◽  
Ovarian Tissue ◽  
Plasminogen Activators ◽  
Tissue Type ◽  
Pharmacological Intervention ◽  
Luteal Regression ◽  
Mammalian Fertilization ◽  
Pai 1

The current knowledge of the role of local and directed fibrinolysis controlled by plasminogen activators (PAs) and regulated by plasminogen activator inhibitors (PAls) in reproduction is summarized. The PA system has been found to play an important role in spermatogenesis in testis and modulation of sperm maturation in epididymis while a lot of studies indicate a role for sperm or seminal plasma PAs in sperm hyperactivation and/or capacitation. Hormoneinduced expression of tissue-type PA (tPA) and PAI-1 in the ovary is involved in the processes of ovulation and luteal regression; increases of urokinase-type PA (uPA) and PAI-1 in the early stage of luteinized follicles may be responsible for ovarian tissue remodeling and angiogenesis. The targeted proteolytic activity plays an essential role in the processes of the cyclic uterine angiogenesis, implantation and placentation as well as in the parturition. As the PA system is involved in multiple phases of mammalian fertilization specific regulatory molecules of this system provide opportunities for pharmacological intervention.

scholarly journals The sperm protein SPACA4 is required for efficient fertilization in mice

2021 ◽  
Author(s):  
Sarah Herberg ◽  
Yoshitaka Fujihara ◽  
Andreas Blaha ◽  
Karin Panser ◽  
Kiyonari Kobayashi ◽  
...  
Keyword(s):  
Zona Pellucida ◽  
Knockout Mice ◽  
Mammalian Species ◽  
Wild Type ◽  
Sperm Protein ◽  
Mammalian Sperm ◽  
Fundamental Process ◽  
Mammalian Fertilization

Fertilization is the fundamental process that initiates the development of a new individual in all sexually reproducing species. Despite its importance, our understanding of the molecular players that govern mammalian sperm-egg interaction is incomplete, partly because many of the essential factors found in non-mammalian species do not have obvious mammalian homologs. We have recently identified the Ly6/uPAR protein Bouncer as a new, essential fertilization factor in zebrafish (Herberg et al., 2018). Here, we show that Bouncer's homolog in mammals, SPACA4, is also required for efficient fertilization in mice. In contrast to fish, where Bouncer is expressed specifically in the egg, SPACA4 is expressed exclusively in the testis. Male knockout mice are severely sub-fertile, and sperm lacking SPACA4 fail to fertilize wild-type eggs in vitro. Interestingly, removal of the zona pellucida rescues the fertilization defect of Spaca4-deficient sperm in vitro, indicating that SPACA4 is not required for the interaction of sperm and the oolemma but rather of sperm and zona pellucida. Our work identifies SPACA4 as an important sperm protein necessary for zona pellucida penetration during mammalian fertilization.

scholarly journals Glioma Pathogenesis-Related 1-Like 1 Is Testis Enriched, Dynamically Modified, and Redistributed during Male Germ Cell Maturation and Has a Potential Role in Sperm-Oocyte Binding

Endocrinology ◽  
2010 ◽  
Vol 151 (5) ◽  
pp. 2331-2342 ◽  
Author(s):  
Gerard M. Gibbs ◽  
Jennifer Chi Yi Lo ◽  
Brett Nixon ◽  
Duangporn Jamsai ◽  
Anne E. O'Connor ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Zona Pellucida ◽  
Secretory Protein ◽  
Cellular Adhesion ◽  
Binding Assays ◽  
Distinct Subgroup ◽  
Functional Studies ◽  
Pathogenesis Related ◽  
Antigen 5

The glioma pathogenesis-related 1 (GLIPR1) family consists of three genes [GLIPR1, GLIPR1-like 1 (GLIPR1L1), and GLIPR1-like 2 (GLIPR1L2)] and forms a distinct subgroup within the cysteine-rich secretory protein (CRISP), antigen 5, and pathogenesis-related 1 (CAP) superfamily. CAP superfamily proteins are found in phyla ranging from plants to humans and, based largely on expression and limited functional studies, are hypothesized to have roles in carcinogenesis, immunity, cell adhesion, and male fertility. Specifically data from a number of systems suggests that sequences within the C-terminal CAP domain of CAP proteins have the ability to promote cell-cell adhesion. Herein we cloned mouse Glipr1l1 and have shown it has a testis-enriched expression profile. GLIPR1L1 is posttranslationally modified by N-linked glycosylation during spermatogenesis and ultimately becomes localized to the connecting piece of elongated spermatids and sperm. After sperm capacitation, however, GLIPR1L1 is also localized to the anterior regions of the sperm head. Zona pellucida binding assays indicate that GLIPR1L1 has a role in the binding of sperm to the zona pellucida surrounding the oocyte. These data suggest that, along with other members of the CAP superfamily and several other proteins, GLIPR1L1 is involved in the binding of sperm to the oocyte complex. Collectively these data further strengthen the role of CAP domain-containing proteins in cellular adhesion and propose a mechanism whereby CAP proteins show overlapping functional significance during fertilization.

scholarly journals Sperm Cohort-Specific Zinc Signature Acquisition and Capacitation-Induced Zinc Flux Regulate Sperm-Oviduct and Sperm-Zona Pellucida Interactions

2020 ◽  
Vol 21 (6) ◽  
pp. 2121 ◽  
Author(s):  
Karl Kerns ◽  
Momal Sharif ◽  
Michal Zigo ◽  
Wei Xu ◽  
Lauren E. Hamilton ◽  
...  
Keyword(s):  
Zona Pellucida ◽  
Semen Analysis ◽  
Inhibitory Effect ◽  
26S Proteasome ◽  
Matrix Metalloproteinase 2 ◽  
Zinc Ions ◽  
New Paradigm ◽  
Male Factor ◽  
Sperm Penetration

Building on our recent discovery of the zinc signature phenomenon present in boar, bull, and human spermatozoa, we have further characterized the role of zinc ions in the spermatozoa’s pathway to fertilization. In boar, the zinc signature differed between the three major boar ejaculate fractions, the initial pre-rich, the sperm-rich, and the post-sperm-rich fraction. These differences set in the sperm ejaculatory sequence establish two major sperm cohorts with marked differences in their sperm capacitation progress. On the subcellular level, we show that the capacitation-induced Zn-ion efflux allows for sperm release from oviductal glycans as analyzed with the oviductal epithelium mimicking glycan binding assay. Sperm zinc efflux also activates zinc-containing enzymes and proteases involved in sperm penetration of the zona pellucida, such as the inner acrosomal membrane matrix metalloproteinase 2 (MMP2). Both MMP2 and the 26S proteasome showed severely reduced activity in the presence of zinc ions, through studies using by gel zymography and the fluorogenic substrates, respectively. In the context of the fertilization-induced oocyte zinc spark and the ensuing oocyte-issued polyspermy-blocking zinc shield, the inhibitory effect of zinc on sperm-borne enzymes may contribute to the fast block of polyspermy. Altogether, our findings establish a new paradigm on the role of zinc ions in sperm function and pave the way for the optimization of animal semen analysis, artificial insemination (AI), and human male-factor infertility diagnostics.

The role of galectin-3 in spermatozoa-zona pellucida binding and its association with fertilization in vitro

2019 ◽  
Vol 25 (8) ◽  
pp. 458-470 ◽  
Author(s):  
Si Mei ◽  
Panyu Chen ◽  
Cheuk-Lun Lee ◽  
Weie Zhao ◽  
Ying Wang ◽  
...  
Keyword(s):  
Seminal Plasma ◽  
Zona Pellucida ◽  
Binding Capacity ◽  
Fertilization Rate ◽  
Clinical Samples ◽  
Fertilization In Vitro ◽  
Human Seminal Plasma ◽  
Sperm Surface ◽  
Galectin 3

AbstractHuman spermatozoa can fertilize an oocyte only after post-testicular maturation and capacitation. These processes involve dynamic modification and reorganization of the sperm plasma membrane, which allow them to bind to the zona pellucida (ZP) of the oocyte. Defective sperm-ZP binding is one of the major causes of male subfertility. Galectin-3 is a secretory lectin in human seminal plasma well known for its action on cell adhesion. The aim of this study was to determine the role of galectin-3 in spermatozoa-ZP interaction and its association with fertilization rate in clinical assisted reproduction. Our studies revealed that the acrosomal region of ejaculated and capacitated spermatozoa possess strong galectin-3 immunoreactivity, which is much stronger than that of epididymal spermatozoa. Expression of galectin-3 can also be detected on seminal plasma-derived extracellular vesicles (EVs) and can be transferred to the sperm surface. Blocking of sperm surface galectin-3 function by antibody or carbohydrate substrate reduced the ZP-binding capacity of spermatozoa. Purified galectin-3 is capable of binding to ZP, indicating that galectin-3 may serve as a cross-linking bridge between ZP glycans and sperm surface glycoproteins. Galectin-3 levels in seminal plasma-derived EVs were positively associated with fertilization rates. These results suggest that galectin-3 in EVs is transferred to the sperm surface during post-testicular maturation and plays a crucial role in spermatozoa-ZP binding after capacitation. Reduced galectin-3 expression in seminal plasma-derived EVs may be a cause behind a low fertilization rate. Further studies with more clinical samples are required to confirm the relationship between galectin-3 levels and IVF outcomes.

scholarly journals A single domain of the ZP2 zona pellucida protein mediates gamete recognition in mice and humans

2014 ◽  
Vol 205 (6) ◽  
pp. 801-809 ◽  
Author(s):  
Matteo A. Avella ◽  
Boris Baibakov ◽  
Jurrien Dean
Keyword(s):  
Transgenic Mice ◽  
Zona Pellucida ◽  
Human Sperm ◽  
Recombinant Peptide ◽  
Genetic Ablation ◽  
Sperm Binding ◽  
Gamete Recognition ◽  
Mammalian Fertilization ◽  
Human And Mouse

The extracellular zona pellucida surrounds ovulated eggs and mediates gamete recognition that is essential for mammalian fertilization. Zonae matrices contain three (mouse) or four (human) glycoproteins (ZP1–4), but which protein binds sperm remains controversial. A defining characteristic of an essential zona ligand is sterility after genetic ablation. We have established transgenic mice expressing human ZP4 that form zonae pellucidae in the absence of mouse or human ZP2. Neither mouse nor human sperm bound to these ovulated eggs, and these female mice were sterile after in vivo insemination or natural mating. The same phenotype was observed with truncated ZP2 that lacks a restricted domain within ZP251–149. Chimeric human/mouse ZP2 isoforms expressed in transgenic mice and recombinant peptide bead assays confirmed that this region accounts for the taxon specificity observed in human–mouse gamete recognition. These observations in transgenic mice document that the ZP251–149 sperm-binding domain is necessary for human and mouse gamete recognition and penetration through the zona pellucida.

Inhibition of sperm-egg fusion in the hamster and mouse by carbohydrates

Zygote ◽  
1994 ◽  
Vol 2 (3) ◽  
pp. 253-262 ◽  
Author(s):  
Ruben H. Ponce ◽  
Umbert A. Urch ◽  
Ryuzo Yanagimachi
Keyword(s):  
Extracellular Matrix ◽  
Plasma Membrane ◽  
Zona Pellucida ◽  
Binding Proteins ◽  
Toxic Effects ◽  
Carbohydrate Binding ◽  
Dextran Sulphate ◽  
Membrane Glycoproteins ◽  
Carbohydrate Binding Proteins

SummaryAfter spermatozoa bind to and penetrate the extracellular matrix of the egg, the zona pellucida, they adhere to and fuse with the plasma membrane of the egg. Since sperm–egg fusion may involve membrane glycoproteins and/or carbohydrate binding proteins, we sought to test this hypothesis by challenging sperm–egg fusion in hamster and in mouse with added carbohydrates. In this study, a number of carbohydrate and glycoconjugates were examined for their ability to inhibit sperm–eggfusion. In the hamster, D(+)-glucosamine, D(+)-galactosamine, albumin-bovine-glucosamide and-galactosamide, fucoidan and dextran sulphate inhibited the fusion of spermatozoa with zona-free eggs. The same effects were seen in the mouse, except for the toxic effects of D(+)-galactosamine. These facts suggest a role of carbohydrate binding proteins or glycoproteins in the fertilisation process at the level of binding to and fusing with the oolemma.

scholarly journals TMEM95 is a sperm membrane protein essential for mammalian fertilization

eLife ◽  
2020 ◽  
Vol 9 ◽  
Author(s):  
Ismael Lamas-Toranzo ◽  
Julieta G Hamze ◽  
Enrica Bianchi ◽  
Beatriz Fernández-Fuertes ◽  
Serafín Pérez-Cerezales ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Membrane Fusion ◽  
Zona Pellucida ◽  
Sperm Protein ◽  
Egg Protein ◽  
Egg Membrane ◽  
Sperm Membrane ◽  
Mammalian Fertilization ◽  
Male Specific ◽  
Mechanical Injection

The fusion of gamete membranes during fertilization is an essential process for sexual reproduction. Despite its importance, only three proteins are known to be indispensable for sperm-egg membrane fusion: the sperm proteins IZUMO1 and SPACA6, and the egg protein JUNO. Here we demonstrate that another sperm protein, TMEM95, is necessary for sperm-egg interaction. TMEM95 ablation in mice caused complete male-specific infertility. Sperm lacking this protein were morphologically normal exhibited normal motility, and could penetrate the zona pellucida and bind to the oolemma. However, once bound to the oolemma, TMEM95-deficient sperm were unable to fuse with the egg membrane or penetrate into the ooplasm, and fertilization could only be achieved by mechanical injection of one sperm into the ooplasm, thereby bypassing membrane fusion. These data demonstrate that TMEM95 is essential for mammalian fertilization.

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