scholarly journals Suppression effect of seminal vesicle autoantigen on platelet-activating factor-induced mouse sperm capacitation

2007 ◽  
Vol 100 (4) ◽  
pp. 941-951 ◽  
Author(s):  
Yen Hua Huang ◽  
Yee Hsiung Chen ◽  
Chun Mao Lin ◽  
Yi Yun Ciou ◽  
Shin Peih Kuo ◽  
...  
Keyword(s):  
Seminal Vesicle ◽  
Platelet Activating Factor ◽  
Sperm Capacitation ◽  
Mouse Sperm ◽  
Suppression Effect

scholarly journals Seminal vesicle proteins SVS3 and SVS4 facilitate SVS2 effect on sperm capacitation

Reproduction ◽  
2016 ◽  
Vol 152 (4) ◽  
pp. 313-321 ◽  
Author(s):  
Naoya Araki ◽  
Natsuko Kawano ◽  
Woojin Kang ◽  
Kenji Miyado ◽  
Kaoru Yoshida ◽  
...  
Keyword(s):  
Seminal Vesicle ◽  
Reproductive Tract ◽  
Female Reproductive Tract ◽  
The Other ◽  
Sperm Capacitation ◽  
Other Hand ◽  
Sperm Membrane ◽  
Vesicle Secretion ◽  
Mammalian Spermatozoa

Mammalian spermatozoa acquire their fertilizing ability in the female reproductive tract (sperm capacitation). On the other hand, seminal vesicle secretion, which is a major component of seminal plasma, inhibits the initiation of sperm capacitation (capacitation inhibition) and reduces the fertility of the capacitated spermatozoa (decapacitation). There are seven major proteins involved in murine seminal vesicle secretion (SVS1-7), and we have previously shown that SVS2 acts as both a capacitation inhibitor and a decapacitation factor, and is indispensable forin vivofertilization. However, the effects of SVSs other than SVS2 on the sperm have not been elucidated. Since mouseSvs2–Svs6genes evolved by gene duplication belong to the same gene family, it is possible that SVSs other than SVS2 also have some effects on sperm capacitation. In this study, we examined the effects of SVS3 and SVS4 on sperm capacitation. Our results showed that both SVS3 and SVS4 are able to bind to spermatozoa, but SVS3 alone showed no effects on sperm capacitation. On the other hand, SVS4 acted as a capacitation inhibitor, although it did not show decapacitation abilities. Interestingly, SVS3 showed an affinity for SVS2 and it facilitated the effects of SVS2. Interaction of SVS2 and spermatozoa is mediated by the ganglioside GM1 in the sperm membrane; however, both SVS3 and SVS4 had weaker affinities for GM1 than SVS2. Therefore, we suggest that separate processes may cause capacitation inhibition and decapacitation, and SVS3 and SVS4 act on sperm capacitation cooperatively with SVS2.

Effects of platelet activating factor on mouse sperm function

1992 ◽  
Vol 9 (5) ◽  
pp. 447-453 ◽  
Author(s):  
Kazuo Sengoku ◽  
Mutsuo Ishikawa ◽  
Kenichi Tamate ◽  
Tetsuya Shimizu
Keyword(s):  
Platelet Activating Factor ◽  
Sperm Function ◽  
Mouse Sperm

scholarly journals Involvement of a Na+/HCO Cotransporter in Mouse Sperm Capacitation

2002 ◽  
Vol 278 (9) ◽  
pp. 7001-7009 ◽  
Author(s):  
Ignacio A. Demarco ◽  
Felipe Espinosa ◽  
Jennifer Edwards ◽  
Julian Sosnik ◽  
José Luis de la Vega-Beltrán ◽  
...  
Keyword(s):  
Sperm Capacitation ◽  
Mouse Sperm

scholarly journals Sialylation of Asparagine 612 Inhibits Aconitase Activity during Mouse Sperm Capacitation; a Possible Mechanism for the Switch from Oxidative Phosphorylation to Glycolysis

2020 ◽  
Vol 19 (11) ◽  
pp. 1860-1875
Author(s):  
Ana Izabel Silva Balbin Villaverde ◽  
Rachel A. Ogle ◽  
Peter Lewis ◽  
Vincenzo Carbone ◽  
Tony Velkov ◽  
...  
Keyword(s):  
Oxidative Phosphorylation ◽  
Serine Proteases ◽  
Alpha Helix ◽  
Complete Loss ◽  
Loss Of Function ◽  
Sperm Capacitation ◽  
Aconitate Hydratase ◽  
Mouse Sperm ◽  
Cycle Enzyme ◽  
Aconitase Activity

After ejaculation, mammalian spermatozoa must undergo a process known as capacitation in order to successfully fertilize the oocyte. Several post-translational modifications occur during capacitation, including sialylation, which despite being limited to a few proteins, seems to be essential for proper sperm-oocyte interaction. Regardless of its importance, to date, no single study has ever identified nor quantified which glycoproteins bearing terminal sialic acid (Sia) are altered during capacitation. Here we characterize sialylation during mouse sperm capacitation. Using tandem MS coupled with liquid chromatography (LC–MS/MS), we found 142 nonreductant peptides, with 9 of them showing potential modifications on their sialylated oligosaccharides during capacitation. As such, N-linked sialoglycopeptides from C4b-binding protein, endothelial lipase (EL), serine proteases 39 and 52, testis-expressed protein 101 and zonadhesin were reduced following capacitation. In contrast, mitochondrial aconitate hydratase (aconitase; ACO2), a TCA cycle enzyme, was the only protein to show an increase in Sia content during capacitation. Interestingly, although the loss of Sia within EL (N62) was accompanied by a reduction in its phospholipase A1 activity, a decrease in the activity of ACO2 (i.e. stereospecific isomerization of citrate to isocitrate) occurred when sialylation increased (N612). The latter was confirmed by N612D recombinant protein tagged with both His and GFP. The replacement of Sia for the negatively charged Aspartic acid in the N612D mutant caused complete loss of aconitase activity compared with the WT. Computer modeling show that N612 sits atop the catalytic site of ACO2. The introduction of Sia causes a large conformational change in the alpha helix, essentially, distorting the active site, leading to complete loss of function. These findings suggest that the switch from oxidative phosphorylation, over to glycolysis that occurs during capacitation may come about through sialylation of ACO2.

scholarly journals Inhibition of Mouse Sperm Capacitation by Ethanol

1982 ◽  
Vol 27 (4) ◽  
pp. 833-840 ◽  
Author(s):  
Robert A. Anderson ◽  
Jakkidi M. Reddy ◽  
Cathy Joyce ◽  
Brian R. Willis ◽  
Hans Van der Ven ◽  
...  
Keyword(s):  
Sperm Capacitation ◽  
Mouse Sperm

Levels of sulfogalactosylglycerolipid in capacitated motile and immotile mouse spermatozoa

1990 ◽  
Vol 68 (2) ◽  
pp. 528-535 ◽  
Author(s):  
Nongnuj Tanphaichitr ◽  
Jacqueline Smith ◽  
Morris Kates
Keyword(s):  
Sperm Motility ◽  
Culture Medium ◽  
Mature Male ◽  
Percoll Gradient ◽  
Direct Relation ◽  
Sperm Capacitation ◽  
Epididymal Sperm ◽  
Pellet Fraction ◽  
Mouse Sperm ◽  
Time Point

The purpose of this study was to determine whether sulfogalactosylglycerolipid (SGG) was desulfated during mouse sperm capacitation. Levels of [35S]SGG were determined in freshly retrieved caudal epididymal sperm, motile capacitated sperm, and immotile sperm, after feeding mature male mice with [35S]sulfate-laced chow for 32 days. Caudal epididymal sperm and coisolated epididymal cells were separated into pellet and interphase fractions by centrifugation through a two-step Percoll gradient (45 and 90%). Upon resuspension in Krebs–Ringer bicarbonate medium supplemented with 0.4% bovine serum albumin, the Percoll-gradient pellet fraction consisted mainly of motile capacitated sperm, whereas the interphase fraction comprised largely immotile sperm and fragmented epididymal epithelial cells. The level of [35S]SGG in the Percoll-gradient-pelleted sperm appeared to be much higher than that in the Percoll-gradient interphase sperm. Percoll-gradient-pelleted sperm were further incubated in the culture medium for 2 h. The level of [35S]SGG showed little or no change after 1 h, but was reduced appreciably after 2 h. At this time point, sperm motility was also decreased. Reduction of sperm SGG is correlated with sperm immotility and (or) senescence and may have no direct relation to the capacitation process.Key words: sulfogalactosylglycerolipid, sperm motility, sperm capacitation.

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