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

scholarly journals Hetero-oligomerization-dependent Binding of Pig Oocyte Zona Pellucida Glycoproteins ZPB and ZPC to Boar Sperm Membrane Vesicles

1998 ◽  
Vol 273 (13) ◽  
pp. 7488-7494 ◽  
Author(s):  
Edward C. Yurewicz ◽  
Anthony G. Sacco ◽  
Satish K. Gupta ◽  
Naxing Xu ◽  
Douglas A. Gage
Keyword(s):  
Zona Pellucida ◽  
Membrane Vesicles ◽  
Boar Sperm ◽  
Sperm Membrane ◽  
Pig Oocyte

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

Partial purification of a boar sperm membrane protein inducing sperm agglutinating antibody

1990 ◽  
Vol 10 (2) ◽  
pp. 131-139
Author(s):  
Oyewole Adeyemo ◽  
E. O. Okegbile ◽  
O. O. Olorunsogo
Keyword(s):  
Molecular Weight ◽  
Membrane Protein ◽  
Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Partial Purification ◽  
Boar Sperm ◽  
Sperm Membrane ◽  
Triton X

For the development of immunological contraception, attention is being concentrated on the possibility of using a sperm membrane antigen. Boar sperm membrane was extracted with triton-X 100 and fractionated by Sephadex G-150 column chromatography. The glycosylated and nonglycosylated portions of protein peaks from the gel filtration were obtained by fractionating on concanavalin A-Sepharose and eluting the bound protein with 0.3 M methyl mannoside. A glycosylated fraction was found to induce sperm agglutinating antibodies in rabbit. The partially purified protein has a molecular weight of 30 kilodaltons, as determined by sodium dodecyl polyaccyrlamide gel electrophoresis. Further work is planned on the histochemical determination of the origin of this protein and species cross-activity of the antibody.

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

scholarly journals Seminal plasma arising from the whole boar sperm-rich fraction increases the stability of sperm membrane after thawing1,2

2016 ◽  
Vol 94 (5) ◽  
pp. 1906-1912 ◽  
Author(s):  
M. A. Torres ◽  
G. M. Ravagnani ◽  
D. F. Leal ◽  
S. M. M. K. Martins ◽  
B. B. D. Muro ◽  
...  
Keyword(s):  
Seminal Plasma ◽  
Boar Sperm ◽  
Sperm Membrane ◽  
The Stability

Differential binding of gold-labeled zona pellucida glycoproteins mZP2 and mZP3 to mouse sperm membrane compartments

Development ◽  
1991 ◽  
Vol 113 (1) ◽  
pp. 141-149 ◽  
Author(s):  
S. Mortillo ◽  
P.M. Wassarman
Keyword(s):  
Plasma Membrane ◽  
Zona Pellucida ◽  
Transmission Electron ◽  
Acrosomal Membrane ◽  
Membrane Compartments ◽  
Sperm Membrane ◽  
Differential Binding ◽  
Inner Acrosomal Membrane ◽  
Low Levels ◽  
Species Specific

Egg zona pellucida glycoproteins mZP3 and mZP2 serve as primary and secondary sperm receptors, respectively, during initial stages of fertilization in mice [Wassarman (1988) A. Rev. Biochem. 57, 415–442]. These receptors interact with complementary egg-binding proteins (EBPs) located on the sperm surface to support species-specific gamete adhesion. Results of whole-mount autoradiographic experiments suggest that purified egg mZP3 and mZP2 bind preferentially to acrosome-intact (AI) and acrosome-reacted (AR) sperm heads, respectively [Bleil and Wassarman (1986) J. Cell Biol. 102, 1363–1371]. Here, we used purified egg mZP2, egg mZP3 and fetuin, which were coupled directly to colloidal gold (‘gold-probes’), to examine binding of these glycoproteins to membrane compartments of AI and AR sperm by transmission electron microscopy. mZP3 gold-probes were found associated primarily with plasma membrane overlying the acrosomal and post-acrosomal regions of AI sperm heads. They were also found associated with plasma membrane overlying the post-acrosomal region of AR sperm heads. mZP2 gold-probes were found associated primarily with inner acrosomal membrane of AR sperm heads, although some gold was associated with outer acrosomal membrane of AI sperm that had holes in plasma membrane overlying the acrosome. Fetuin gold-probes, used to assess background levels of binding, were bound at relatively low levels to plasma membrane and inner acrosomal membrane of AI and AR sperm, respectively. None of the gold-probes exhibited significant binding to sperm tails, or to red blood cells and residual bodies present in sperm preparations. These results provide further evidence that mZP2 and mZP3 bind preferentially to heads of AR and AI sperm, respectively.(ABSTRACT TRUNCATED AT 250 WORDS)

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