Role of the Cumulus Oophorus in Mammalian Fertilization

2015 ◽  
pp. 111-124 ◽  
Author(s):  
Yutaka Toyoda ◽  
Eimei Sato ◽  
Kunihiko Naito
1982 ◽  
Vol 5 (1) ◽  
pp. 37-44 ◽  
Author(s):  
Lawrence M. Lewin ◽  
Zvi Nevo ◽  
Amos Gabsu ◽  
Ruth Weissenberg
Keyword(s):  

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) ◽  
...  

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.


1996 ◽  
Vol 134 (3) ◽  
pp. 637-645 ◽  
Author(s):  
C Arnoult ◽  
Y Zeng ◽  
H M Florman

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.


2002 ◽  
Vol 37 (3) ◽  
pp. 144-151 ◽  
Author(s):  
A Van Soom ◽  
S Tanghe ◽  
I De Pauw ◽  
D Maes ◽  
A de Kruif

2015 ◽  
Vol 210 (7) ◽  
pp. 1213-1224 ◽  
Author(s):  
Juan I. Ernesto ◽  
Mariana Weigel Muñoz ◽  
María A. Battistone ◽  
Gustavo Vasen ◽  
Pablo Martínez-López ◽  
...  

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.


1997 ◽  
Vol 321 (3) ◽  
pp. 577-581 ◽  
Author(s):  
Jennifer A. JURY ◽  
Jan FRAYNE ◽  
Len HALL

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.


1994 ◽  
Vol 40 (2) ◽  
pp. 99-105 ◽  
Author(s):  
Yuji TAKAHASHI ◽  
Hiroshi IMAHIE ◽  
Kae KAMIO ◽  
Sadahiro AZUMA ◽  
Eimei SATO ◽  
...  

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