Bovine Seminal Plasma (BSP) Proteins, which Enhance Bull Sperm Binding to Oviductal Epithelium, Respond Differently to Capacitating Conditions.

2010 ◽  
Vol 83 (Suppl_1) ◽  
pp. 490-490
Author(s):  
Pei-hsuan Hung ◽  
Susan S. Suarez
Keyword(s):  
Seminal Plasma ◽  
Sperm Binding ◽  
Oviductal Epithelium ◽  
Bsp Proteins ◽  
Bull Sperm

The endocannabinoid system in bull sperm and bovine oviductal epithelium: role of anandamide in sperm–oviduct interaction

Reproduction ◽  
2009 ◽  
Vol 137 (3) ◽  
pp. 403-414 ◽  
Author(s):  
María Gracia Gervasi ◽  
Maximiliano Rapanelli ◽  
María Laura Ribeiro ◽  
Mariana Farina ◽  
Silvia Billi ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Cannabinoid Receptors ◽  
Fatty Acid Amide Hydrolase ◽  
Acid Amide ◽  
Endocannabinoid System ◽  
Sperm Binding ◽  
Bovine Sperm ◽  
Sperm Release ◽  
Oviductal Epithelium ◽  
Bull Sperm

Anandamide binds to cannabinoid receptors and plays several central and peripheral functions. The aim of this work was to study the possible role for this endocannabinoid in controlling sperm–oviduct interaction in mammals. We observed that bull sperm and bovine oviductal epithelial cells express cannabinoid receptors, CB1 and CB2, and fatty acid amide hydrolase, the enzyme that controls intracellular anandamide levels. A quantitative assay to determine whether anandamide was involved in bovine sperm–oviduct interaction was developed. R(+)-methanandamide, a non-hydrolysable anandamide analog, inhibited sperm binding to and induced sperm release from oviductal epithelia. Selective CB1 antagonists (SR141716A or AM251) completely blocked R(+)-methanandamide effects. However, SR144528, a selective CB2 antagonist, did not exert any effect, indicating that only CB1 was involved in R(+)-methanandamide effect. This effect was not caused by inhibition of the sperm progressive motility or by induction of the acrosome reaction. Overall, our findings indicate for the first time that the endocannabinoid system is present in bovine sperm and oviductal epithelium and that anandamide modulates the sperm–oviduct interaction, by inhibition of sperm binding and induction of sperm release from oviductal epithelial cells, probably by activating CB1 receptors.

scholarly journals Macro- and microelements in serum and seminal plasma as biomarkers for bull sperm cryotolerance

2021 ◽  
Vol 63 (1) ◽  
Author(s):  
Maja Zakošek Pipan ◽  
Petra Zrimšek ◽  
Breda Jakovac Strajn ◽  
Katarina Pavšič Vrtač ◽  
Tanja Knific ◽  
...  
Keyword(s):  
Seminal Plasma ◽  
Semen Quality ◽  
Sperm Quality ◽  
Membrane Integrity ◽  
Quality Characteristics ◽  
Freezing And Thawing ◽  
Additional Tool ◽  
Bull Semen ◽  
Bull Sperm ◽  
Fresh Semen

ABSTRACT Background Wide variation in fertility rates is observed when using frozen bull semen, even when the bulls have met quality standards for semen production. Therefore, a simple and reliable test to assess the freezing potential of bull semen based on the analysis of fresh semen or blood would be of great value. Attention is now turning to assessment of seminal plasma components such as proteins and elements. In the present study, the concentrations of macro- and microelements in fresh bull semen plasma and in serum and their correlation with quality characteristics of fresh semen and with semen quality after freezing and thawing were determined. Ejaculates were collected from 30 mature bulls, and semen volume, concentration, sperm motility, morphology, tail membrane integrity, plasma membrane permeability and DNA fragmentation were determined on the day of collection and after freezing and thawing. The concentrations of macroelements (Na, Mg, K and Ca) and microelements (Cu, Fe, Zn and Se) were determined in the seminal plasma and serum. The semen samples were classified into satisfactory and unsatisfactory groups according to the fresh semen quality. Results Zinc and Se levels measured in serum were associated with almost all fresh and frozen-thawed semen quality characteristics, while Fe levels were associated only with acrosomal defects in fresh semen. Zinc and Fe levels in fresh seminal plasma were associated with various quality characteristics of fresh and frozen-thawed semen, while Se level in fresh seminal plasma was not associated with any of the semen quality characteristics. Conclusions Microelements were shown to be useful as biomarkers involved in the analysis of bull sperm quality and could be used as an additional tool to predict bull semen quality after freezing and thawing. Our results confirm that the analysis of Zn and Se levels in serum and Zn, Cu and Fe levels in fresh seminal plasma can provide information to discriminate between bull semen samples with spermatozoa with high or low cryotolerance.

scholarly journals Binding of boar spermatozoa to oviductal epithelium in vitro in relation to sperm morphology and storage time

Reproduction ◽  
2006 ◽  
Vol 131 (2) ◽  
pp. 311-318 ◽  
Author(s):  
D Waberski ◽  
F Magnus ◽  
F Ardón ◽  
A M Petrunkina ◽  
K F Weitze ◽  
...  
Keyword(s):  
Semen Quality ◽  
Binding Capacity ◽  
Storage Period ◽  
Sperm Function ◽  
Sperm Binding ◽  
Oviductal Epithelium ◽  
Semen Storage ◽  
Boar Semen ◽  
Boar Spermatozoa

In vitro short-term storage of boar semen for up to 72 h before insemination negatively affects fertility, but this often remains undetected during semen quality assessment. One important sperm function is the ability to form the functional sperm reservoir in the oviduct. In the present study, we used the modified oviductal explant assay to study sperm binding to oviductal epithelium in vitro in diluted boar semen stored for 24 or 72 h. First, we determined the kinetics of in vitro sperm binding to oviductal epithelium in relation to co-incubation time of sperm and oviductal tissue pieces. Then, we studied how the binding of sperm to oviductal epithelium was affected by in vitro semen storage and by differences among individual boars. Sperm binding after different incubation times was significantly higher when semen was stored 24 h than after 72-h storage (P < 0.05), and peaked at 30–90 min of incubation. Sperm binding differed between boars (n = 44), and was negatively correlated to the percentage of sperm with cytoplasmic droplets (R = −0.51, P < 0.001). There were no significant changes in motility, acrosome integrity and propidium iodide stainability during the 72-h storage period. However, sperm-binding indices were significantly lower after 72 h in vitro storage than after 24-h storage in sperm from boars with normal semen quality (P < 0.05); in contrast, the binding capacity of sperm from boars with higher percentages of morphologically altered sperm remained at a low level. The sperm-binding capacity of sperm from four of the five boars with known subfertility was lower than the mean binding index minus one standard deviation of the boar population studied here. It is concluded that changes in the plasma membrane associated with in vitro ageing reduce the ability of stored boar sperm to bind to the oviductal epithelium. This study shows the potential of sperm–oviduct binding as a tool to assess both male fertility and changes in sperm function associated with in vitro ageing.

180. CHARACTERIZATION AND FUNCTION OF THE BULL SPERM PROTEIN Spam1: TWO DISTINCT ISOFORMS WITH DISTINCT ROLES

2009 ◽  
Vol 21 (9) ◽  
pp. 98
Author(s):  
G. Morin ◽  
R. Sullivan ◽  
I. Laflamme ◽  
C. Robert ◽  
P. Leclerc
Keyword(s):  
Transmembrane Domain ◽  
Inhibitory Effect ◽  
Anterior Region ◽  
Protein Orientation ◽  
Sperm Protein ◽  
Sperm Binding ◽  
Glycosylation Sites ◽  
Sperm Membrane ◽  
Bull Sperm ◽  
And Function

We identified an 80 kDa bull sperm protein (p80) that possesses homology with the Sperm adhesion molecule 1 (Spam1), a GPI-anchored glycoprotein conserved amongst mammals that is required for fertilization. Since bovine Spam1 had not been identified, the aim of this project was to determine if p80 is the bovine Spam1 and to test the hypothesis that it plays a role in gamete interaction during bovine fertilization. Amino acid sequence deduced from 3`/5`Race confirmed that homology between p80 and Spam1 in various species ranged from 47 to 61%.It also revealed specific differences including the absence of a GPI-anchor, the presence of a transmembrane domain, and N- and O- glycosylation sites. By generating and characterising antibodies against p80 N- and C-terminal domains, the protein orientation in the sperm membrane was evaluated. We identified two populations of p80 on the sperm head: one internalised in the anterior region and the second localised on the post-acrosomal region with its hyaluronidase domain exposed to the extracellular environment. Proteomic and immunologic analyses revealed that the p80 post-acrosomal population is a shorter isoform originating from the epididymis while the full length p80 located on the anterior region originates from the testis. Finally, the potential function of p80 during the sperm/zp interaction was evaluated by sperm/zona pellucida (zp) binding assay. The C-terminal extremity of p80 was implicated in sperm binding to the zp by antibody and native protein competition. Furthermore, glycosylation was not required during this interaction since deglycosylated p80 in the incubation medium had the same inhibitory effect on zona binding as the native p80. Collectively, the results demonstrated that p80 is the bovine Spam1, and that two isoforms are present on bull sperm. The hyaluronidase activity of the post-acrosomal isoform is required for cumulus penetration, while the other one participates in sperm/zp binding during fertilization.

scholarly journals Equine seminal plasma reduces sperm binding to polymorphonuclear neutrophils (PMNs) and improves the fertility of fresh semen inseminated into inflamed uteri

Reproduction ◽  
2004 ◽  
Vol 127 (5) ◽  
pp. 593-600 ◽  
Author(s):  
A S Alghamdi ◽  
D N Foster ◽  
M H T Troedsson
Keyword(s):  
Seminal Plasma ◽  
Skim Milk ◽  
Polymorphonuclear Neutrophils ◽  
Proteinase K ◽  
Polymorphonuclear Neutrophil ◽  
Sperm Binding ◽  
Uterine Inflammation ◽  
Semen Extender ◽  
Uterine Secretions

Seminal plasma (SP) is known to have immunosuppressive properties in several species. Equine SP has been reported to reduce or inhibit chemotaxis, phagocytosis and complement activity in vitro. The type and amount of the SP component that suppresses sperm–polymorphonuclear neutrophil (PMN) binding in vitro was determined, and the effect of such suppression on the fertility of mares inseminated in the presence of uterine inflammation, was analyzed. Sperm cells were suspended in either SP, semen extender or a mixture of both, and each was mixed with PMN-rich uterine secretions collected at 12 h after artificial insemination (AI). SP reduced binding between spermatozoa and PMNs significantly (P < 0.05). Fertile spermatozoa were suspended in SP or semen extender and used to inseminate mares 12 h after the induction of uterine inflammation. The pregnancy rate was normal (77%) when spermatozoa were suspended in SP, but was dramatically reduced to only 5% when spermatozoa were suspended in extender. The proteins from SP, blood plasma (BP) and a skim-milk-based semen extender (skim milk extender, SME) were precipitated by ammonium sulfate, resuspended in PBS and dialyzed. The effect of the precipitated proteins on sperm–PMN binding was compared with fresh, untreated SP. Both fresh SP, and isolated SP proteins reduced sperm–PMN binding (P < 0.001). Conversely, proteins isolated from either BP or SME did not reduce sperm–PMN binding. The different concentrations of SP proteins used showed a dose-dependent suppression of sperm–PMN binding. Concentrations of 1 mg/ml SP protein significantly reduced sperm–PMN binding and 6 mg/ml reduced the binding to a level similar to that observed with fresh whole SP (P < 0.001). Finally, SP protein digested with proteinase K resulted in the complete loss of SP suppressive activity confirming that the effective component is a proteinaceous substance.

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