scholarly journals Zona pellucida protein binding ability of porcine sperm during epididymal maturation and the acrosome reaction

2000 ◽  
Vol 222 (1) ◽  
pp. 99-109 ◽  
Author(s):  
Heather R. Burkin ◽  
David J. Miller
Keyword(s):  
Protein Binding ◽  
Zona Pellucida ◽  
Acrosome Reaction ◽  
Binding Ability ◽  
Epididymal Maturation

scholarly journals Epididymal Maturation and the Acrosome Reaction in Mouse Sperm: Response to Zona Pellucida Develops Coincident with Modification of M42 Antigen1

1988 ◽  
Vol 38 (1) ◽  
pp. 221-233 ◽  
Author(s):  
Katherine A. Lakoski ◽  
Christopher P. Carron ◽  
Christine L. Cabot ◽  
Patricia M. Saling
Keyword(s):  
Zona Pellucida ◽  
Acrosome Reaction ◽  
Mouse Sperm ◽  
Epididymal Maturation

Native zona pellucida structure is required for completion of sperm acrosome reaction in porcine fertilization

1994 ◽  
Vol 41 (6) ◽  
pp. 1307-1313 ◽  
Author(s):  
M. Yoshizawa ◽  
T. Nagai ◽  
N. Yonezawa ◽  
M. Nakano
Keyword(s):  
Zona Pellucida ◽  
Acrosome Reaction ◽  
Sperm Acrosome Reaction ◽  
Sperm Acrosome

Evaluation for Protein Binding Affinity of Maghemite and Magnetite Nanoparticles

2007 ◽  
Vol 7 (11) ◽  
pp. 3706-3708 ◽  
Author(s):  
Se Chan Kang ◽  
Yong Jun Jo ◽  
Jong Phil Bak ◽  
Ki-Chul Kim ◽  
Young-Sung Kim
Keyword(s):  
Protein Binding ◽  
Binding Affinity ◽  
Magnetite Nanoparticles ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Human Lung Cancer ◽  
Maghemite Nanoparticles ◽  
Binding Ability ◽  
Sds Page ◽  
Lung Cancer A549 Cell

We investigated the protein binding affinity of magnetite (Fe3O4) and maghemite (γ-Fe2O3) nanoparticles with against non-characterized protein from human lung cancer A549 cell line on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The binding ability of maghemite was 400 ng/mg. According to the SDS-PAGE results, the protein binding affinity of maghemite nanoparticles is stronger than magnetite nanoparticles. These data suggest that a protein can be detected with maghemite nanoparticles.

Cell surface beta-1,4-galactosyltransferase-I activates G protein-dependent exocytotic signaling

Development ◽  
2001 ◽  
Vol 128 (5) ◽  
pp. 645-654
Author(s):  
X. Shi ◽  
S. Amindari ◽  
K. Paruchuru ◽  
D. Skalla ◽  
H. Burkin ◽  
...  
Keyword(s):  
G Protein ◽  
G Proteins ◽  
Pertussis Toxin ◽  
Zona Pellucida ◽  
Acrosome Reaction ◽  
Cytoplasmic Domain ◽  
Protein Activation ◽  
Acrosomal Exocytosis ◽  
G Protein Activation ◽  
Galactosyltransferase I

ZP3 is a protein in the mammalian egg coat (zona pellucida) that binds sperm and stimulates acrosomal exocytosis, enabling sperm to penetrate the zona pellucida. The nature of the ZP3 receptor/s on sperm is a matter of considerable debate, but most evidence suggests that ZP3 binds to beta-1,4-galactosyltransferase-I (GalTase) on the sperm surface. It has been suggested that ZP3 induces the acrosome reaction by crosslinking GalTase, activating a heterotrimeric G protein. In this regard, acrosomal exocytosis is sensitive to pertussis toxin and the GalTase cytoplasmic domain can precipitate G(i) from sperm lysates. Sperm from mice that overexpress GalTase bind more soluble ZP3 and show accelerated G protein activation, whereas sperm from mice with a targeted deletion in GalTase have markedly less ability to bind soluble ZP3, undergo the ZP3-induced acrosome reaction, and penetrate the zona pellucida. We have examined the ability of GalTase to function as a ZP3 receptor and to activate heterotrimeric G proteins using Xenopus laevis oocytes as a heterologous expression system. Oocytes that express GalTase bound ZP3 but did not bind other zona pellucida glycoproteins. After oocyte maturation, ZP3 or GalTase antibodies were able to trigger cortical granule exocytosis and activation of GalTase-expressing eggs. Pertussis toxin inhibited GalTase-induced egg activation. Consistent with G protein activation, both ZP3 and anti-GalTase antibodies increased GTP-gamma[(35)S] binding as well as GTPase activity in membranes from eggs expressing GalTase. Finally, mutagenesis of a putative G protein activation motif within the GalTase cytoplasmic domain eliminated G protein activation in response to ZP3 or anti-GalTase antibodies. These results demonstrate directly that GalTase functions as a ZP3 receptor and following aggregation, is capable of activating pertussis toxin-sensitive G proteins leading to exocytosis.

Functional interactions between sulphated polysaccharides and proacrosin: implications in sperm binding and digestion of zona pellucida

Zygote ◽  
1999 ◽  
Vol 7 (2) ◽  
pp. 105-111 ◽  
Author(s):  
R. D. Moreno ◽  
M. Hoshi ◽  
C. Barros
Keyword(s):  
Zona Pellucida ◽  
Active Site ◽  
Acrosome Reaction ◽  
Penetration Rate ◽  
Limited Proteolysis ◽  
Sulphated Polysaccharides ◽  
Functional Interactions ◽  
Sperm Binding ◽  
Sperm Penetration ◽  
Sperm Acrosome Reaction

Acrosin is a serine protease located within mammalian acrosome as inactive proacrosin. Sulphated polymers bind to proacrosin and acrosin, to a domain different from the active site. Upon binding, these polymers induce proacrosin activation and some of them, such as fucoidan, inhibit sperm binding to the zona pellucida. In this work we have studied the interaction of solubilised zona pellucida glycoproteins (ZPGs), heparin and ARIS (Acrosome Reaction Inducing Substance of Starfish) with boar and human acrosin. We have found that ARIS, solubilised ZPGs and fucoidan, but not heparin, inhibit the binding of the monoclonal antibody against human acrosin C5F10 to boar or human proacrosin. These results suggest that fucoidan, solubilised ZPGs and ARIS bind to a related domain on the proacrosin surface. Moreover, ARIS was able to induce human proacrosin activation. On the other hand, neither ARIS nor heparin from porcine intestinal mucosa or bovine lung induced hamster sperm acrosome reaction or sperm motility. Recent data showed that acrosin is involved in dispersal of the acrosomal matrix after acrosome reaction. Thus, the control of the ZPG glycan chains over proacrosin activation may regulate both sperm penetration rate and limited proteolysis of zona pellucida proteins.

Hydrogen peroxide induces premature acrosome reaction in rat sperm and reduces their penetration of the zona pellucida

Toxicology ◽  
1999 ◽  
Vol 139 (1-2) ◽  
pp. 93-101 ◽  
Author(s):  
Ping-Chi Hsu ◽  
Chao-Chin Hsu ◽  
Yueliang Leon Guo
Keyword(s):  
Hydrogen Peroxide ◽  
Zona Pellucida ◽  
Acrosome Reaction
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