Surfing the wave, cycle, life history, and genes/proteins expressed by testicular germ cells. Part 3: Developmental changes in spermatid flagellum and cytoplasmic droplet and interaction of sperm with the zona pellucida and egg plasma membrane

2009 ◽  
pp. NA-NA ◽  
Author(s):  
Louis Hermo ◽  
R.-Marc Pelletier ◽  
Daniel G. Cyr ◽  
Charles E. Smith
Keyword(s):  
Life History ◽  
Plasma Membrane ◽  
Germ Cells ◽  
Zona Pellucida ◽  
Cycle Life ◽  
Developmental Changes ◽  
Cytoplasmic Droplet ◽  
Wave Cycle

Surfing the wave, cycle, life history, and genes/proteins expressed by testicular germ cells. Part 1: Background to spermatogenesis, spermatogonia, and spermatocytes

2009 ◽  
Vol 73 (4) ◽  
pp. 241-278 ◽  
Author(s):  
Louis Hermo ◽  
R.-Marc Pelletier ◽  
Daniel G. Cyr ◽  
Charles E. Smith
Keyword(s):  
Life History ◽  
Germ Cells ◽  
Cycle Life ◽  
Wave Cycle

Developmental changes in DNA methylation of the male germ cells in foetal and prepuberal mice

1998 ◽  
Vol 90 (1) ◽  
pp. 110-110
Author(s):  
Claire A. Bourgeois ◽  
Herve Coffigny ◽  
Michèle Ricoul ◽  
Bernard Malfoy ◽  
Bernard Dutrillaux
Keyword(s):  
Dna Methylation ◽  
Germ Cells ◽  
Developmental Changes ◽  
Male Germ Cells

Oocyte proteomics: localisation of mouse zona pellucida protein 3 to the plasma membrane of ovulated mouse eggs

2004 ◽  
Vol 16 (2) ◽  
pp. 69 ◽  
Author(s):  
S. A. Coonrod ◽  
M. E. Calvert ◽  
P. P. Reddi ◽  
E. N. Kasper ◽  
L. C. Digilio ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Indirect Immunofluorescence ◽  
Zona Pellucida ◽  
Surface Expression ◽  
Surface Proteins ◽  
2D Electrophoresis ◽  
Dependent Manner ◽  
Two Dimensional ◽  
Phase Partitioning ◽  
Proteomic Approach

In order to gain a deeper understanding of the molecular underpinnings of sperm–egg interaction and early development, we have used two-dimensional (2D) electrophoresis, avidin blotting and tandem mass spectrometry to identify, clone and characterise abundant molecules from the mouse egg proteome. Two-dimensional avidin blots of biotinylated zona-free eggs revealed an abundant approximately 75-kDa surface-labelled heterogeneous protein possessing a staining pattern similar to that of the zona pellucida glycoprotein, mouse ZP3 (mZP3). In light of this observation, we investigated whether mZP3 specifically localises to the plasma membrane of mature eggs. Zona pellucidae of immature mouse oocytes and mature eggs were removed using acid Tyrode’s solution, chymotrypsin or mechanical shearing. Indirect immunofluorescence using the mZP3 monoclonal antibody (mAb) IE-10 demonstrated strong continuous staining over the entire surface of immature oocytes and weak microvillar staining on ovulated eggs, regardless of the method of zona removal. Interestingly, in mature eggs, increased fluorescence intensity was observed following artificial activation and fertilisation, whereas little to no fluorescence was observed in degenerated eggs. The surface localisation of ZP3 on mature eggs was supported by the finding that the IE-10 mAb immunoprecipitated an approximate 75-kDa protein from lysates of biotinylated zona-free eggs. To further investigate the specificity of the localisation of mZP3 to the oolemma, indirect immunofluorescence was performed using the IE-10 mAb on both CV-1 and CHO cells transfected with full-length recombinant mZP3 (re-mZP3). Plasma membrane targeting of the expressed re-mZP3 protein was observed in both cell lines. The membrane association of re-mZP3 was confirmed by the finding that biotinylated re-mZP3 (approximately 75 kDa) is immunoprecipitated from the hydrophobic phase of Triton X-114 extracts of transfected cells following phase partitioning. Immunoprecipitation assays also demonstrated that surface re-mZP3 was released from transfected CV-1 in a time-dependent manner. These results demonstrate that ZP3 is specifically associated with the surface of mature eggs and its subsequent release from the cell surface may represent one mechanism by which ZP3 is secreted. Furthermore, the increase in ZP3 surface expression following fertilisation suggests that ZP3 may have a functional role during sperm–oolemma binding and fusion. These results also validate the usefulness of using the 2D proteomic approach to identify and characterise egg-surface proteins.

scholarly journals Glycodelin-A interacts with fucosyltransferase on human sperm plasma membrane to inhibit spermatozoa-zona pellucida binding

2006 ◽  
Vol 120 (1) ◽  
pp. 33-44 ◽  
Author(s):  
P. C. N. Chiu ◽  
M.-K. Chung ◽  
R. Koistinen ◽  
H. Koistinen ◽  
M. Seppala ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Zona Pellucida ◽  
Human Sperm ◽  
Sperm Plasma Membrane ◽  
Glycodelin A

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)

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.

Evidence for a binding site on the sperm plasma membrane which recognizes the murine zona pellucida: A binding site on the sperm plasma membrane

1986 ◽  
Vol 14 (3) ◽  
pp. 235-243 ◽  
Author(s):  
Gary R. Poirier ◽  
Roderick Robinson ◽  
Richard Richardson ◽  
Kathy Hinds ◽  
Deborah Clayton
Keyword(s):  
Plasma Membrane ◽  
Binding Site ◽  
Zona Pellucida ◽  
Sperm Plasma Membrane
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