Spermatozoa from a marsupial, the brushtail possum, contain β1,4-galactosyltransferase

2008 ◽  
Vol 20 (3) ◽  
pp. 402 ◽  
Author(s):  
A. G. Braundmeier ◽  
William G. Breed ◽  
D. J. Miller
Keyword(s):  
Molecular Weight ◽  
Zona Pellucida ◽  
Acrosome Reaction ◽  
Brushtail Possum ◽  
Laboratory Mice ◽  
Sperm Surface ◽  
Protein Functions ◽  
Sperm Acrosome Reaction ◽  
Porcine Spermatozoa ◽  
Egg Coat

β1,4-Galactosyltransferase-I (GalTase-I) is one of the key molecules on the sperm surface of eutherian mammals that is likely to be involved in binding to the egg coat, the zona pellucida, to mediate sperm–egg interaction. In laboratory mice, the species for which most data are available, this protein functions as a receptor for the zona pellucida protein ZP3 of the oocyte and, upon binding, triggers the sperm acrosome reaction. In the present study, we investigated the presence and abundance of GalTase-I in epididymal sperm extracts of a marsupial, the brushtail possum, Trichosurus vulpecula. For this, spermatozoa were collected from cauda epididymides and the amount of β1,4-galactosyltransferase activity in washed sperm extracts was compared with that of porcine spermatozoa. Overall β1,4-galactosyltransferase enzyme activity was found to be more abundant in possum sperm extracts than those from porcine spermatozoa (P < 0.05). Immunoblots with an antibody to mouse GalTase-I revealed that the molecular weight of possum spermatozoa GalTase-I was 66 kDa, which is similar to the molecular weight of GalTase-I in spermatozoa from eutherian mammals. The molecular weight of GalTase-I was the same in sperm extracts collected from the caput and cauda epididymides. These results demonstrate that GalTase-I is indeed present in possum spermatozoa and thus it may be a gamete receptor molecule on the sperm surface of marsupials as well as those of eutherian mammals.

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

Sperm from beta 1,4-galactosyltransferase-null mice are refractory to ZP3-induced acrosome reactions and penetrate the zona pellucida poorly

Development ◽  
1997 ◽  
Vol 124 (20) ◽  
pp. 4121-4131 ◽  
Author(s):  
Q. Lu ◽  
B.D. Shur
Keyword(s):  
Acrosome Reaction ◽  
Direct Evidence ◽  
Calcium Ionophore ◽  
Wild Type ◽  
Sperm Surface ◽  
Gamete Recognition ◽  
Dependent Signal ◽  
Relative Inability ◽  
Egg Coat

A variety of sperm surface components have been suggested to mediate gamete recognition by binding to glycoside ligands on the egg coat glycoprotein ZP3. The function of each of these candidate receptors is based upon varying degrees of circumstantial and direct evidence; however, the effects on fertilization of targeted mutations in any of these candidate receptors have not yet been reported. In this paper, we describe the effects of targeted mutations in beta1,4-galactosyltransferase, the best studied of the candidate receptors for ZP3. Surprisingly, galactosyltransferase-null (gt[−/−]) males are fertile; however, sperm from gt(−/−) males bind less radiolabeled ZP3 than wild-type sperm, and are unable to undergo the acrosome reaction in response to either ZP3 or anti-galactosyltransferase antibodies, as do wild-type sperm. In contrast, gt(−/−) sperm undergo the acrosome reaction normally in response to calcium ionophore, which bypasses the requirement for ZP3 binding. The inability of gt(−/−) sperm to undergo a ZP3-induced acrosome reaction renders them physiologically inferior to wild-type sperm, as assayed by their relative inability to penetrate the egg coat and fertilize the oocyte in vitro. Thus, although ZP3 binding and subsequent induction of the acrosome reaction are dispensable for fertilization, they impart a physiological advantage to the fertilizing sperm. A second strain of mice was created that is characterized by a loss of of the long galactosyltransferase isoform responsible for ZP3-dependent signal transduction, but which maintains normal levels of Golgi galactosylation. Sperm from these mice show that the defective sperm-egg interactions in gt(−/−) mice are due directly to a loss of the long galactosyltransferase isoform from the sperm surface and are independent of the state of intracellular galactosylation during spermatogenesis.

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.

Effects of oviductal fluid and heparin on fertility and characteristics of porcine spermatozoa

Zygote ◽  
1997 ◽  
Vol 5 (1) ◽  
pp. 61-65 ◽  
Author(s):  
Nam-Hyung Kim ◽  
Billy N. Day ◽  
Joon-Gyo Lim ◽  
Hoon Taek Lee ◽  
Kil Saeng Chung
Keyword(s):  
Zona Pellucida ◽  
Acrosome Reaction ◽  
Time Points ◽  
Sperm Penetration ◽  
The Mean ◽  
Oviductal Fluid ◽  
Porcine Spermatozoa

SummaryThe objective of this study was to determine the effects of oviductal fluid and heparin on sperm penetration and the characteristics of spermatozoa. The addition of oviductal fluid and heparin to the fertilisation medium decreased sperm penetration and the mean number of spermatozoa in penetrated eggs. The number of spermatozoa firmly bound to zona pellucida was also decreased in the presence of oviductal fluid and heparin. Chlortetracycline (CTC) fluorescence patterns were used to determine the incidence of capacitation and the acrosome reaction. The proportion of capacitated and acrosome-free spermatozoa increased when spermatozoa were exposed for 1.5 and 3 h to oviductal fluid and heparin. In contrast heparin alone did not increase the number of capacitated spermatozoa at these time points. These results suggest that factor(s) in oviductal secretions reduce polyspermic fertilisation and the number of spermatozoa that will penetrate porcine oocytes. The reduction of polyspermic penetration by oviductal secretions may be due to a reduced number of spermatozoa in the fertilisation medium with an intact acrosome.

Effect of Epidermal Growth Factor on Mouse Sperm Acrosome Reaction Induced by Zona Pellucida

1994 ◽  
Vol 31 (2-3) ◽  
pp. 116-122 ◽  
Author(s):  
Satoru Furuya ◽  
Yoshihiro Endo ◽  
Mikiko Oba ◽  
Yukari Matsui ◽  
Shuetu Suzuki ◽  
...  
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Zona Pellucida ◽  
Acrosome Reaction ◽  
Mouse Sperm ◽  
Epidermal Growth ◽  
Sperm Acrosome Reaction ◽  
Sperm Acrosome

scholarly journals Calmodulin Antagonists Inhibit T-Type Ca2+ Currents in Mouse Spermatogenic Cells and the Zona Pellucida-Induced Sperm Acrosome Reaction

2001 ◽  
Vol 236 (1) ◽  
pp. 210-219 ◽  
Author(s):  
Ignacio López-González ◽  
Jose L. De La Vega-Beltrán ◽  
Celia M. Santi ◽  
Harvey M. Florman ◽  
Ricardo Felix ◽  
...  
Keyword(s):  
Zona Pellucida ◽  
Acrosome Reaction ◽  
Spermatogenic Cells ◽  
Calmodulin Antagonists ◽  
Sperm Acrosome Reaction ◽  
Sperm Acrosome

scholarly journals Recombinant Human Zona Pellucida Protein ZP3 Produced by Chinese Hamster Ovary Cells Induces the Human Sperm Acrosome Reaction and Promotes Sperm-Egg Fusion

1994 ◽  
Vol 51 (4) ◽  
pp. 607-617 ◽  
Author(s):  
Marcel Van Duin ◽  
Jan E.M. Polman ◽  
Ingeborg T.M. De Breet ◽  
Karin Van Ginneken ◽  
Hans Bunschoten ◽  
...  
Keyword(s):  
Zona Pellucida ◽  
Chinese Hamster Ovary ◽  
Acrosome Reaction ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Human Sperm ◽  
Ovary Cells ◽  
Sperm Acrosome Reaction ◽  
Sperm Acrosome
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