Activation of cAMP‐dependent phosphorylation pathways is independent of ROS production during mouse sperm capacitation

2021 ◽  
Author(s):  
Gen L. Takei ◽  
Darya A. Tourzani ◽  
Bidur Paudel ◽  
Pablo E. Visconti
Keyword(s):  
Ros Production ◽  
Sperm Capacitation ◽  
Mouse Sperm

scholarly journals Epidermal growth factor alleviates the negative impact of urea on frozen-thawed bovine sperm, but the subsequent developmental competence is compromised

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Rasoul Kowsar ◽  
Shahrzad Ronasi ◽  
Nima Sadeghi ◽  
Khaled Sadeghi ◽  
Akio Miyamoto
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Dna Fragmentation ◽  
Acrosome Reaction ◽  
Developmental Competence ◽  
Ros Production ◽  
Sperm Capacitation ◽  
Bovine Sperm ◽  
Epidermal Growth ◽  
High Level

AbstractUpon insemination, sperm cells are exposed to components of the female reproductive tract (FRT) fluids, such as urea and epidermal growth factor (EGF). It has been shown that both urea and EGF use EGF receptor signaling and produce reactive oxygen species (ROS) that are required at certain levels for sperm capacitation and acrosome reaction. We therefore hypothesized that during bovine sperm capacitation, a high level of urea and EGF could interfere with sperm function through overproduction of ROS. High-level urea (40 mg/dl urea is equal to 18.8 mg/dl of blood urea nitrogen) significantly increased ROS production and TUNEL-positive sperm (sperm DNA fragmentation, sDF) percentage, but decreased HOS test score, progressive motility, acrosome reaction and capacitation. The EGF reversed the negative effects of urea on all sperm parameters, with the exception of ROS production and DNA fragmentation, which were higher in urea-EGF-incubated sperm than in control-sperm. The developmental competence of oocytes inseminated with urea-EGF-incubated sperm was significantly reduced compared to the control. A close association of ROS production or sDF with 0-pronuclear and sperm non-capacitation rates was found in the network analysis. In conclusion, EGF enhanced urea-reduced sperm motility; however, it failed to reduce urea-increased sperm ROS or sDF levels and to enhance subsequent oocyte competence. The data suggests that any study to improve sperm quality should be followed by a follow-up assessment of the fertilization outcome.

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.

Glycolytic Substrates Have Differential Effects on Mouse Sperm Capacitation and Hyperactivation.

2011 ◽  
Vol 85 (Suppl_1) ◽  
pp. 187-187
Author(s):  
Summer G. Goodson ◽  
Yunping Qiu ◽  
Guoxiang Xie ◽  
Wei Jia ◽  
Deborah A. O'Brien
Keyword(s):  
Sperm Capacitation ◽  
Mouse Sperm ◽  
Differential Effects

SNARE Complex Phosphorylation Shows Dynamic Changes During Mouse Sperm Capacitation.

2012 ◽  
Vol 87 (Suppl_1) ◽  
pp. 351-351
Author(s):  
Syed Tahir Abbas Shah ◽  
David J. Miller
Keyword(s):  
Snare Complex ◽  
Sperm Capacitation ◽  
Dynamic Changes ◽  
Mouse Sperm
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