scholarly journals The role of centrosomes in mammalian fertilization and its significance for ICSI

2009 ◽  
Vol 15 (9) ◽  
pp. 531-538 ◽  
Author(s):  
H. Schatten ◽  
Q.-Y. Sun
Keyword(s):  
Mammalian Fertilization

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 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.

scholarly journals CRISP1 as a novel CatSper regulator that modulates sperm motility and orientation during fertilization

2015 ◽  
Vol 210 (7) ◽  
pp. 1213-1224 ◽  
Author(s):  
Juan I. Ernesto ◽  
Mariana Weigel Muñoz ◽  
María A. Battistone ◽  
Gustavo Vasen ◽  
Pablo Martínez-López ◽  
...  
Keyword(s):  
Sperm Motility ◽  
Critical Role ◽  
Cumulus Cells ◽  
Fine Tuning ◽  
Patch Clamping ◽  
Successful Completion ◽  
Tuning Mechanism ◽  
Mammalian Fertilization ◽  
Ca2 Channels

Ca2+-dependent mechanisms are critical for successful completion of fertilization. Here, we demonstrate that CRISP1, a sperm protein involved in mammalian fertilization, is also present in the female gamete and capable of modulating key sperm Ca2+ channels. Specifically, we show that CRISP1 is expressed by the cumulus cells that surround the egg and that fertilization of cumulus–oocyte complexes from CRISP1 knockout females is impaired because of a failure of sperm to penetrate the cumulus. We provide evidence that CRISP1 stimulates sperm orientation by modulating sperm hyperactivation, a vigorous motility required for penetration of the egg vestments. Moreover, patch clamping of sperm revealed that CRISP1 has the ability to regulate CatSper, the principal sperm Ca2+ channel involved in hyperactivation and essential for fertility. Given the critical role of Ca2+ for sperm motility, we propose a novel CRISP1-mediated fine-tuning mechanism to regulate sperm hyperactivation and orientation for successful penetration of the cumulus during fertilization.

scholarly journals The human fertilin α gene is non-functional: implications for its proposed role in fertilization

1997 ◽  
Vol 321 (3) ◽  
pp. 577-581 ◽  
Author(s):  
Jennifer A. JURY ◽  
Jan FRAYNE ◽  
Len HALL
Keyword(s):  
Plasma Membrane ◽  
Guinea Pig ◽  
Genetic Recombination ◽  
Surface Membrane ◽  
Membrane Glycoprotein ◽  
Head Region ◽  
Α Subunit ◽  
Functional Implications ◽  
Mammalian Fertilization

In the guinea-pig, the α subunit of the fertilin complex, a heterodimeric surface membrane glycoprotein found on the head region of spermatozoa, has previously been proposed to mediate membrane fusion with the oolemma plasma membrane during fertilization. Here we describe experiments which indicate that the only fertilin α-like gene in humans is an expressed, but non-functional, pseudogene, possibly derived by genetic recombination between the two fertilin α genes found in some primates. This finding clearly raises questions about the importance and/or role of fertilin α in mammalian fertilization.

Role of the Cumulus Oophorus in Mammalian Fertilization

2015 ◽  
pp. 111-124 ◽  
Author(s):  
Yutaka Toyoda ◽  
Eimei Sato ◽  
Kunihiko Naito
Keyword(s):  
Cumulus Oophorus ◽  
Mammalian Fertilization

scholarly journals New insights into the role of centrosomes in mammalian fertilization and implications for ART

Reproduction ◽  
2011 ◽  
Vol 142 (6) ◽  
pp. 793-801 ◽  
Author(s):  
Heide Schatten ◽  
Qing-Yuan Sun
Keyword(s):  
Molecular Mechanisms ◽  
Assisted Reproductive Technologies ◽  
Mammalian Species ◽  
Reproductive Technologies ◽  
Therapeutic Approaches ◽  
Mitotic Apparatus ◽  
Proper Diagnosis ◽  
Mammalian Fertilization ◽  
Molecular Aspects

In non-rodent mammalian species, including humans, the oocyte and sperm both contribute centrosomal components that are most important for successful fertilization. Centrosome pathologies in sperm and the oocyte can be causes for infertility which may be overcome by assisted reproductive technologies based on proper diagnosis of specific centrosomal pathologies. However, we do not yet fully understand the cell and molecular mechanisms underlying centrosome functions in germ cells and in the developing embryo, which calls for directed specific investigations to identify centrosome-related pathologies that include components in sperm, egg, or centrosome regulation within the fertilized oocyte. The present review highlights cellular and molecular aspects of centrosomes and centrosome–nuclear interactions focused on nuclear mitotic apparatus protein during fertilization and proposes future directions in expanding therapeutic approaches related to centrosome pathologies that may play a role in still unexplained causes of infertility.

scholarly journals The Role of Centrioles in Mammalian Fertilization and Development

2011 ◽  
Vol 17 (S2) ◽  
pp. 218-219
Author(s):  
H Schatten
Keyword(s):  
Mammalian Fertilization

Extended abstract of a paper presented at Microscopy and Microanalysis 2011 in Nashville, Tennessee, USA, August 7–August 11, 2011.

scholarly journals The less conserved metal-binding site in human CRISP1 remains sensitive to zinc ions to permit protein oligomerization

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Jie Sheng ◽  
Bart M. Gadella ◽  
Nick K. Olrichs ◽  
Dora V. Kaloyanova ◽  
J. Bernd Helms
Keyword(s):  
Binding Site ◽  
Metal Binding ◽  
Protein Complexes ◽  
Secretory Proteins ◽  
Protein Oligomerization ◽  
Functional Protein ◽  
Metal Binding Site ◽  
Mammalian Fertilization

AbstractCysteine-rich secretory proteins (CRISPs) are a subgroup of the CRISP, antigen 5 and PR-1 (CAP) superfamily that is characterized by the presence of a conserved CAP domain. Two conserved histidines in the CAP domain are proposed to function as a Zn2+-binding site with unknown function. Human CRISP1 is, however, one of the few family members that lack one of these characteristic histidine residues. The Zn2+-dependent oligomerization properties of human CRISP1 were investigated using a maltose-binding protein (MBP)-tagging approach in combination with low expression levels in XL-1 Blue bacteria. Moderate yields of soluble recombinant MBP-tagged human CRISP1 (MBP-CRISP1) and the MBP-tagged CAP domain of CRISP1 (MBP-CRISP1ΔC) were obtained. Zn2+ specifically induced oligomerization of both MBP-CRISP1 and MBP-CRISP1ΔC in vitro. The conserved His142 in the CAP domain was essential for this Zn2+ dependent oligomerization process, confirming a role of the CAP metal-binding site in the interaction with Zn2+. Furthermore, MBP-CRISP1 and MBP-CRISP1ΔC oligomers dissociated into monomers upon Zn2+ removal by EDTA. Condensation of proteins is characteristic for maturing sperm in the epididymis and this process was previously found to be Zn2+-dependent. The Zn2+-induced oligomerization of human recombinant CRISP1 may shed novel insights into the formation of functional protein complexes involved in mammalian fertilization.

Role of dactinomycin in the improved survival of children with Wilms' tumor

JAMA ◽  
1966 ◽  
Vol 195 (12) ◽  
pp. 1005-1009 ◽  
Author(s):  
D. J. Fernbach
Keyword(s):  
Wilms Tumor
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