scholarly journals Dicalcin, a zona pellucida protein that regulates fertilization competence of the egg coat in Xenopus laevis

2015 ◽  
Vol 65 (6) ◽  
pp. 507-514 ◽  
Author(s):  
Naofumi Miwa
Keyword(s):  
Xenopus Laevis ◽  
Zona Pellucida ◽  
Egg Coat

Incorporation of mouse zona pellucida proteins into the envelope of Xenopus laevis oocytes

1999 ◽  
Vol 209 (6) ◽  
pp. 330-339 ◽  
Author(s):  
Sandra Doren ◽  
N. Landsberger ◽  
Nancy Dwyer ◽  
L. Gold ◽  
Joan Blanchette-Mackie ◽  
...  
Keyword(s):  
Xenopus Laevis ◽  
Zona Pellucida ◽  
Xenopus Laevis Oocytes

Boar Acrosin Digestion of the Porcine Egg Coat, Zona Pellucida, and Rearrangement of the Zona Proteins

1989 ◽  
Vol 105 (1) ◽  
pp. 138-142 ◽  
Author(s):  
Minoru Nakano ◽  
Yoko Tanaka ◽  
Tokutaro Kimura ◽  
Yumiko Hatanak ◽  
Tohru Tobita
Keyword(s):  
Zona Pellucida ◽  
Egg Coat

scholarly journals Identification of distinctive interdomain interactions among ZP-N, ZP-C and other domains of zona pellucida glycoproteins underlying association of chicken egg-coat matrix

FEBS Open Bio ◽  
2015 ◽  
Vol 5 (1) ◽  
pp. 454-465 ◽  
Author(s):  
Hiroki Okumura ◽  
Takahiro Sato ◽  
Rio Sakuma ◽  
Hideaki Fukushima ◽  
Tsukasa Matsuda ◽  
...  
Keyword(s):  
Zona Pellucida ◽  
Chicken Egg ◽  
Interdomain Interactions ◽  
Egg Coat

scholarly journals Proteomic characterization and evolutionary analyses of zona pellucida domain-containing proteins in the egg coat of the cephalochordate, Branchiostoma belcheri

2012 ◽  
Vol 12 (1) ◽  
pp. 239 ◽  
Author(s):  
Qianghua Xu ◽  
Guang Li ◽  
Lixue Cao ◽  
Zhongjun Wang ◽  
Hua Ye ◽  
...  
Keyword(s):  
Zona Pellucida ◽  
Branchiostoma Belcheri ◽  
Egg Coat

Spermatozoa from a marsupial, the brushtail possum, contain β1,4-galactosyltransferase

2008 ◽  
Vol 20 (3) ◽  
pp. 402 ◽  
Author(s):  
A. G. Braundmeier ◽  
William G. Breed ◽  
D. J. Miller
Keyword(s):  
Molecular Weight ◽  
Zona Pellucida ◽  
Acrosome Reaction ◽  
Brushtail Possum ◽  
Laboratory Mice ◽  
Sperm Surface ◽  
Protein Functions ◽  
Sperm Acrosome Reaction ◽  
Porcine Spermatozoa ◽  
Egg Coat

β1,4-Galactosyltransferase-I (GalTase-I) is one of the key molecules on the sperm surface of eutherian mammals that is likely to be involved in binding to the egg coat, the zona pellucida, to mediate sperm–egg interaction. In laboratory mice, the species for which most data are available, this protein functions as a receptor for the zona pellucida protein ZP3 of the oocyte and, upon binding, triggers the sperm acrosome reaction. In the present study, we investigated the presence and abundance of GalTase-I in epididymal sperm extracts of a marsupial, the brushtail possum, Trichosurus vulpecula. For this, spermatozoa were collected from cauda epididymides and the amount of β1,4-galactosyltransferase activity in washed sperm extracts was compared with that of porcine spermatozoa. Overall β1,4-galactosyltransferase enzyme activity was found to be more abundant in possum sperm extracts than those from porcine spermatozoa (P < 0.05). Immunoblots with an antibody to mouse GalTase-I revealed that the molecular weight of possum spermatozoa GalTase-I was 66 kDa, which is similar to the molecular weight of GalTase-I in spermatozoa from eutherian mammals. The molecular weight of GalTase-I was the same in sperm extracts collected from the caput and cauda epididymides. These results demonstrate that GalTase-I is indeed present in possum spermatozoa and thus it may be a gamete receptor molecule on the sperm surface of marsupials as well as those of eutherian mammals.

The egg coat zona pellucida 3 glycoprotein – evolution of its putative sperm-binding region in Old World murine rodents (Rodentia: Muridae)

2017 ◽  
Vol 29 (12) ◽  
pp. 2376 ◽  
Author(s):  
Christine A. Swann ◽  
Steven J. B. Cooper ◽  
William G. Breed
Keyword(s):  
Sexual Selection ◽  
Zona Pellucida ◽  
Laboratory Mouse ◽  
Sequence Divergence ◽  
Tail Length ◽  
Good Evidence ◽  
Sperm Binding ◽  
Molecular Divergence ◽  
Murine Rodents ◽  
Egg Coat

In eutherian mammals, before fertilisation can occur the spermatozoon has to bind to, and penetrate, the egg coat, the zona pellucida (ZP). In the laboratory mouse there is good evidence that the primary sperm-binding site is a protein region encoded by Exon 7 of the ZP3 gene and it has been proposed that binding is species specific and evolves by sexual selection. In the present study we investigate these hypotheses by comparing Exon 6 and 7 sequences of ZP3 in 28 species of murine rodents of eight different divisions from Asia, Africa and Australasia, in which a diverse array of sperm morphologies occurs. We found considerable nucleotide (and corresponding amino acid) sequence divergence in Exon 7, but not in Exon 6, across these species, with evidence for positive selection at five codon positions. This molecular divergence does not appear to be due to reinforcement to reduce hybridisation, nor does it correlate with divergence in sperm head morphology or tail length, thus it is unlikely to be driven by inter-male sperm competition. Other forms of post-copulatory sexual selection therefore appear to have resulted in the molecular divergence of this region of ZP3 in this highly speciose group of mammals.

Xenopus laevis sperm proteins, previously identified as surface proteins with egg coat binding capability, are indeed histone H4, histone H3, and sperm specific protein SP2

1992 ◽  
Vol 263 (2) ◽  
pp. 210-214 ◽  
Author(s):  
Giovanni Bernardini ◽  
Isabella Dalle Donne ◽  
Sabrina Norreri ◽  
Armando Negri ◽  
Aldo Milzani
Keyword(s):  
Xenopus Laevis ◽  
Histone H3 ◽  
Specific Protein ◽  
Surface Proteins ◽  
Histone H4 ◽  
Sperm Proteins ◽  
Binding Capability ◽  
Egg Coat
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