scholarly journals Activation of mouse sperm T-type Ca2+ channels by adhesion to the egg zona pellucida

1996 ◽  
Vol 93 (23) ◽  
pp. 13004-13009 ◽  
Author(s):  
C. Arnoult ◽  
R. A. Cardullo ◽  
J. R. Lemos ◽  
H. M. Florman
Keyword(s):  
Zona Pellucida ◽  
Mouse Sperm ◽  
Ca2 Channels

scholarly journals Distinct Membrane Fractions from Mouse Sperm Bind Different Zona Pellucida Glycoproteins1

2002 ◽  
Vol 66 (1) ◽  
pp. 65-69 ◽  
Author(s):  
Catherine D. Thaler ◽  
Richard A. Cardullo
Keyword(s):  
Zona Pellucida ◽  
Mouse Sperm ◽  
Distinct Membrane

Binding of Mouse Sperm to β-Galactose Residues on Egg Zona Pellucida and Asialofetuin-Coupled Beads

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

Mouse sperm-egg plasma membrane interactions: analysis of roles of egg integrins and the mouse sperm homologue of PH-30 (fertilin) beta

1995 ◽  
Vol 108 (10) ◽  
pp. 3267-3278 ◽  
Author(s):  
J.P. Evans ◽  
R.M. Schultz ◽  
G.S. Kopf
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Guinea Pig ◽  
Ligand Binding ◽  
Zona Pellucida ◽  
Plasma Membranes ◽  
Signal Sequence ◽  
Rgd Peptides ◽  
Mouse Sperm ◽  
Disintegrin Domain

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.

Acrosomal exocytosis of mouse sperm progresses in a consistent direction in response to zona pellucida

2009 ◽  
Vol 220 (3) ◽  
pp. 611-620 ◽  
Author(s):  
Mariano G. Buffone ◽  
Esmeralda Rodriguez-Miranda ◽  
Bayard T. Storey ◽  
George L. Gerton
Keyword(s):  
Zona Pellucida ◽  
Mouse Sperm ◽  
Acrosomal Exocytosis ◽  
Consistent Direction

scholarly journals CaV2.2 and CaV2.3 (N- and R-type) Ca2+Channels in Depolarization-evoked Entry of Ca2+into Mouse Sperm

2000 ◽  
Vol 275 (28) ◽  
pp. 21210-21217 ◽  
Author(s):  
Gunther Wennemuth ◽  
Ruth E. Westenbroek ◽  
Tao Xu ◽  
Bertil Hille ◽  
Donner F. Babcock
Keyword(s):  
Mouse Sperm ◽  
Ca2 Channels

scholarly journals Studies on Mouse Sperm Binding Molecule (Ligand) to Egg Zona Pellucida. II. Purification of Ligand Molecule from Cauda Epididymal Sperm.

1991 ◽  
Vol 14 (5) ◽  
pp. 237-243 ◽  
Author(s):  
Yuichi KAWAI ◽  
Kaori FUNAKOSHI ◽  
Takao HAMA ◽  
Tadanori MAYUMI
Keyword(s):  
Zona Pellucida ◽  
Ligand Molecule ◽  
Epididymal Sperm ◽  
Mouse Sperm ◽  
Sperm Binding

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
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