Isolation, characterization, and localization of the zona pellucida binding proteins of boar sperm

1991 ◽  
Vol 28 (2) ◽  
pp. 124-130 ◽  
Author(s):  
Mo Hanqing ◽  
Yan Tai-Ying ◽  
Shen Zhao-Wen
Keyword(s):  
Zona Pellucida ◽  
Binding Proteins ◽  
Boar Sperm

scholarly journals Zona pellucida-binding of boar sperm acrosin is associated with the N-terminal peptide of the acrosin B-chain (heavy chain)

FEBS Letters ◽  
1990 ◽  
Vol 265 (1-2) ◽  
pp. 51-54 ◽  
Author(s):  
E. Töpfer-Petersen ◽  
M. Steinberger ◽  
C. Ebner von Eschenbach ◽  
A. Zucker
Keyword(s):  
Heavy Chain ◽  
Zona Pellucida ◽  
Boar Sperm

Porcine zona pellucida ZP3? glycoprotein mediates binding of the biotin-labeled Mr 55,000 family (ZP3) to boar sperm membrane vesicles

1993 ◽  
Vol 36 (3) ◽  
pp. 382-389 ◽  
Author(s):  
Edward C. Yurewicz ◽  
Beverley A. Pack ◽  
D. Randall Armant ◽  
Anthony G. Sacco
Keyword(s):  
Zona Pellucida ◽  
Membrane Vesicles ◽  
Boar Sperm ◽  
Sperm Membrane

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.

Dynamics of heparin-binding proteins on boar sperm

2009 ◽  
Vol 116 (3-4) ◽  
pp. 308-317 ◽  
Author(s):  
Dora G. Dapino ◽  
Juan M. Teijeiro ◽  
Marcelo O. Cabada ◽  
Patricia E. Marini
Keyword(s):  
Binding Proteins ◽  
Heparin Binding ◽  
Boar Sperm

scholarly journals Identification of 17-18 kDa zona pellucida binding proteins from boar spermatozoa

FEBS Letters ◽  
1990 ◽  
Vol 264 (2) ◽  
pp. 243-245 ◽  
Author(s):  
J. Moos ◽  
J. Pěknicová ◽  
Ts.N. Sumeva-Nakova ◽  
M. Pavlík
Keyword(s):  
Zona Pellucida ◽  
Binding Proteins ◽  
Boar Spermatozoa

Isolation of antiSLIP1-reactive boar sperm P68/62 and its binding to mammalian zona pellucida

1998 ◽  
Vol 49 (2) ◽  
pp. 203-216 ◽  
Author(s):  
Nongnuj Tanphaichitr ◽  
Connie Moase ◽  
Tanya Taylor ◽  
Krystyna Surewicz ◽  
Christiane Hansen ◽  
...  
Keyword(s):  
Zona Pellucida ◽  
Boar Sperm

scholarly journals The interaction of boar sperm proacrosin with its natural substrate, the zona pellucida, and with polysulfated polysaccharides

Development ◽  
1991 ◽  
Vol 111 (4) ◽  
pp. 1165-1172 ◽  
Author(s):  
U.A. Urch ◽  
H. Patel
Keyword(s):  
Sea Urchin ◽  
Zona Pellucida ◽  
Consensus Sequence ◽  
Amino Acid Sequences ◽  
Relative Molecular Mass ◽  
Binding Affinities ◽  
Boar Sperm ◽  
Vitelline Envelope ◽  
Egg Jelly ◽  
Hydrolysis Of

Boar sperm acrosin is an acrosomal protease with trypsin-like specificity, and it functions in fertilization by assisting sperm passage through the zona pellucida by limited hydrolysis of this extracellular matrix. In addition to a proteolytic active site domain, acrosin binds the zona pellucida at a separate binding domain that is lost during proacrosin autolysis. In this study, we quantitate the binding of proacrosin to the physiological substrate for acrosin, the zona pellucida, and to a non-substrate, the polysulfated polysaccharide fucoidan. Binding was analogous to sea urchin sperm bindin that binds egg jelly fucan and the vitelline envelope of sea urchin eggs. Proacrosin was found to bind to fucoidan and to the zona pellucida with binding affinities similar to bindin interaction with egg jelly fucan. These interactions were competitively inhibited by similar relative molecular mass polysulfated polymers. Since bindin and proacrosin have distinctly different amino acid sequences, their interaction with acidic sulfate esters demonstrates an example of convergent evolution wherein different macromolecules localized in analogous sperm compartments have the same biological function. From cDNA sequence analysis of proacrosin, this binding may be mediated through a consensus sequence for binding sulfated glycoconjugates. Proacrosin binding to the zona pellucida may serve as both a recognition or primary sperm receptor, as well as maintaining the sperm on the zona pellucida once the acrosome reaction has occurred.

scholarly journals Molecular Cloning and Characterization of P47, a Novel Boar Sperm-Associated Zona Pellucida-Binding Protein Homologous to a Family of Mammalian Secretory Proteins1

1998 ◽  
Vol 58 (4) ◽  
pp. 1057-1064 ◽  
Author(s):  
Michael Ensslin ◽  
Tanja Vogel ◽  
Juan J. Calvete ◽  
Hubert H. Thole ◽  
Jörg Schmidtke ◽  
...  
Keyword(s):  
Molecular Cloning ◽  
Zona Pellucida ◽  
Binding Protein ◽  
Boar Sperm

The interaction of living boar sperm and sperm plasma membrane vesicles with the porcine zona pellucida

1981 ◽  
Vol 84 (1) ◽  
pp. 144-156 ◽  
Author(s):  
R.N. Peterson ◽  
L.D. Russell ◽  
D. Bundman ◽  
M. Conway ◽  
M. Freund
Keyword(s):  
Plasma Membrane ◽  
Zona Pellucida ◽  
Membrane Vesicles ◽  
Plasma Membrane Vesicles ◽  
Boar Sperm ◽  
Sperm Plasma Membrane
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