The Mouse Sperm Cell Surface Needs Ca+2 to Recognize the Zona Pellucida of the Mouse Egg

Author(s):  
Patricia M. Saling ◽  
Bayard T. Storey
2002 ◽  
Vol 66 (1) ◽  
pp. 65-69 ◽  
Author(s):  
Catherine D. Thaler ◽  
Richard A. Cardullo

1997 ◽  
Vol 238 (1) ◽  
pp. 95-99 ◽  
Author(s):  
Etsuko Mori ◽  
Tsuneatsu Mori ◽  
Seiichi Takasaki
Keyword(s):  

1995 ◽  
Vol 108 (10) ◽  
pp. 3267-3278 ◽  
Author(s):  
J.P. Evans ◽  
R.M. Schultz ◽  
G.S. Kopf

The guinea pig sperm protein, PH-30 (also known as fertilin), is postulated to participate in the interaction between the sperm and egg plasma membranes. The beta subunit of guinea pig PH-30 (gpPH-30 beta) contains a domain with homology to disintegrins, snake venom proteins that bind to integrins via an integrin-binding domain containing the tripeptide RGD. This raises the question of whether an egg integrin serves as a receptor for PH-30. Although mouse eggs express integrin subunits, their role in mouse fertilization is unresolved. Therefore, we examined fertilization for two different hallmarks of integrin function, namely, dependence of ligand binding on divalent cations and the ability to inhibit ligand binding with RGD peptides. We demonstrate that sperm binding to zona pellucida-free eggs is supported by Ca2+, Mg2+, or Mn2+. Ca2+ was necessary and sufficient for sperm-egg fusion, with 2.5 mM Ca2+ being the most effective concentration. In addition, fertilization could be partially inhibited with various RGD peptides, which caused a decrease in sperm-egg fusion by 30–58%. This partial inhibition of fusion with RGD peptides prompted the cloning of the mouse homologue of gpPH-30 beta (hereafter referred to as mPH-30 beta) to determine if it possessed the tripeptide RGD or a different amino acid sequence in its disintegrin domain. mPH-30 beta, which is expressed during meiotic and post-meiotic phases of spermatogenesis, shares significant similarities to gpPH-30 beta throughout the length of the molecule, from the signal sequence to the cytoplasmic tail. The full-length deduced amino acid sequence of mPH-30 beta. The disintegrin domain of mPH-30 beta has the tripeptide QDE (instead of RGD) in its cell recognition region. Peptides containing this QDE sequence decrease the binding and fusion of sperm with zona pellucida-free eggs by approximately 70%, suggesting that the disintegrin domain of mPH-30 beta participates in the interaction between sperm and egg membranes.


2009 ◽  
Vol 220 (3) ◽  
pp. 611-620 ◽  
Author(s):  
Mariano G. Buffone ◽  
Esmeralda Rodriguez-Miranda ◽  
Bayard T. Storey ◽  
George L. Gerton

2002 ◽  
Vol 66 (5) ◽  
pp. 1328-1335 ◽  
Author(s):  
Rosaria Meccariello ◽  
Gilda Cobellis ◽  
Giovanna Berruti ◽  
Marie-Pierre Junier ◽  
Michela Ceriani ◽  
...  

PLoS ONE ◽  
2015 ◽  
Vol 10 (6) ◽  
pp. e0129907 ◽  
Author(s):  
Nathan Egge ◽  
Archana Muthusubramanian ◽  
Gail A. Cornwall
Keyword(s):  

1996 ◽  
Vol 93 (23) ◽  
pp. 13004-13009 ◽  
Author(s):  
C. Arnoult ◽  
R. A. Cardullo ◽  
J. R. Lemos ◽  
H. M. Florman

2007 ◽  
Vol 214 (1) ◽  
pp. 153-157 ◽  
Author(s):  
Eveline S. Litscher ◽  
William G. Janssen ◽  
Costel C. Darie ◽  
Paul M. Wassarman
Keyword(s):  

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