The role of galectin-3 in spermatozoa-zona pellucida binding and its association with fertilization in vitro

2019 ◽  
Vol 25 (8) ◽  
pp. 458-470 ◽  
Author(s):  
Si Mei ◽  
Panyu Chen ◽  
Cheuk-Lun Lee ◽  
Weie Zhao ◽  
Ying Wang ◽  
...  
Keyword(s):  
Seminal Plasma ◽  
Zona Pellucida ◽  
Binding Capacity ◽  
Fertilization Rate ◽  
Clinical Samples ◽  
Fertilization In Vitro ◽  
Human Seminal Plasma ◽  
Sperm Surface ◽  
Galectin 3

AbstractHuman spermatozoa can fertilize an oocyte only after post-testicular maturation and capacitation. These processes involve dynamic modification and reorganization of the sperm plasma membrane, which allow them to bind to the zona pellucida (ZP) of the oocyte. Defective sperm-ZP binding is one of the major causes of male subfertility. Galectin-3 is a secretory lectin in human seminal plasma well known for its action on cell adhesion. The aim of this study was to determine the role of galectin-3 in spermatozoa-ZP interaction and its association with fertilization rate in clinical assisted reproduction. Our studies revealed that the acrosomal region of ejaculated and capacitated spermatozoa possess strong galectin-3 immunoreactivity, which is much stronger than that of epididymal spermatozoa. Expression of galectin-3 can also be detected on seminal plasma-derived extracellular vesicles (EVs) and can be transferred to the sperm surface. Blocking of sperm surface galectin-3 function by antibody or carbohydrate substrate reduced the ZP-binding capacity of spermatozoa. Purified galectin-3 is capable of binding to ZP, indicating that galectin-3 may serve as a cross-linking bridge between ZP glycans and sperm surface glycoproteins. Galectin-3 levels in seminal plasma-derived EVs were positively associated with fertilization rates. These results suggest that galectin-3 in EVs is transferred to the sperm surface during post-testicular maturation and plays a crucial role in spermatozoa-ZP binding after capacitation. Reduced galectin-3 expression in seminal plasma-derived EVs may be a cause behind a low fertilization rate. Further studies with more clinical samples are required to confirm the relationship between galectin-3 levels and IVF outcomes.

scholarly journals Role of ascorbic acid in human seminal plasma against the oxidative damage to the sperms

2009 ◽  
Vol 24 (3) ◽  
pp. 312-315 ◽  
Author(s):  
Piyali Das ◽  
A. R. Choudhari ◽  
A. Dhawan ◽  
Ramji Singh
Keyword(s):  
Ascorbic Acid ◽  
Oxidative Damage ◽  
Seminal Plasma ◽  
Human Seminal Plasma

scholarly journals Galectin-3 is a substrate for prostate specific antigen (PSA) in human seminal plasma

The Prostate ◽  
2010 ◽  
Vol 71 (2) ◽  
pp. 197-208 ◽  
Author(s):  
Sarika Saraswati ◽  
Ashley S. Block ◽  
Mari. K. Davidson ◽  
Roger. G. Rank ◽  
Maha Mahadevan ◽  
...  
Keyword(s):  
Prostate Specific Antigen ◽  
Seminal Plasma ◽  
Specific Antigen ◽  
Human Seminal Plasma ◽  
Galectin 3

scholarly journals Effect of Human Seminal Plasma and Mouse Accessory Gland Extracts on Mouse Fertilization in vitro

1984 ◽  
Vol 37 (3) ◽  
pp. 147 ◽  
Author(s):  
P Quinn ◽  
AJ Begley
Keyword(s):  
Seminal Plasma ◽  
Accessory Gland ◽  
Seminal Vesicles ◽  
Fertilization In Vitro ◽  
Human Seminal Plasma ◽  
Vitro Fertilization ◽  
Fertilizing Ability ◽  
Fertilization System ◽  
Mouse In Vitro Fertilization

The mouse in vitro fertilization system was used to investigate the effect of human seminal plasma (HSP) on the fertilizing ability of mouse spermatozoa. The addition of HSP to freshly collected mouse epididymal spermatozoa decreased their fertilizing ability to 30%, compared with 85-90% for control spermatozoa not exposed to HSP or for spermatozoa that had been exposed to the capacitating system for 55-145 min (which allowed capacitation to occur before the addition of HSP). Human seminal plasma from a vasectomized donor was more effective in retarding the acquisition offertilizing ability in mouse spermatozoa than was seminal plasma from non-vasectomized donors. Huid from the prostate glands and seminal vesicles of mice also reduced the fertilizing ability of freshly collected mouse spermatozoa to 30%.

scholarly journals A role for mouse sperm surface galactosyltransferase in sperm binding to the egg zona pellucida.

1982 ◽  
Vol 95 (2) ◽  
pp. 574-579 ◽  
Author(s):  
B D Shur ◽  
N G Hall
Keyword(s):  
Zona Pellucida ◽  
Milk Protein ◽  
Preceding Paper ◽  
Transferase Activity ◽  
Mouse Sperm ◽  
Sperm Surface ◽  
Galactosyl Transferase ◽  
Sperm Binding ◽  
Beta Galactosidase

Past studies have suggested that mouse sperm surface galactosyltransferase may participate during fertilization by binding N-acetylglucosamine (GlcNAc) residues in the zona pellucida. In this paper, we examined further the role of sperm surface galactosyltransferase in mouse fertilization. Two reagents that specifically perturb sperm surface galactosyltransferase activity both inhibit sperm-zona binding. The presence of the milk protein alpha-lactalbumin specifically modifies the substrate specificity of sperm galactosyltransferase away from GlcNAc and towards glucose and simultaneously inhibits sperm binding to the zona pellucida. Similarly, UDP-dialdehyde inhibits sperm binding to the zona pellucida and sperm surface galactosyl-transferase activity to identical degrees. Of five other sperm enzymes assayed, four are unaffected by UDP-dialdehyde, and one is affected only slightly. Covalent linkage of UDP-dialdehyde to sperm dramatically inhibits binding to eggs, while treatment of eggs with UDP-dialdehyde has no effect on sperm binding. Heat-solubilized or pronase-digested zona pellucida inhibit sperm-zona binding, and they can be glycosylated by sperm with UDP-galactose. Sperm are also able to glycosylate intact zona pellucida with UDP-galactose. Thus, solubilized and intact zona pellucida act as substrates for sperm surface GlcNAc:galactosyltransferases. Finally, pretreatment of eggs with beta-N-acetylglucosaminidase inhibits sperm binding by up to 86%, while under identical conditions, pretreatment with beta-galactosidase increases sperm binding by 55%. These studies, in conjunction with those of the preceding paper dealing with surface galactosyltransferase changes during capacitation, directly suggest that galactosyltransferase is at least one of the components necessary for sperm binding to the zona pellucida.

scholarly journals β-Microseminoprotein in human spermatozoa and its potential role in male fertility

Reproduction ◽  
2008 ◽  
Vol 136 (2) ◽  
pp. 157-166 ◽  
Author(s):  
N Anahí Franchi ◽  
Conrado Avendaño ◽  
Rosa I Molina ◽  
Andrea D Tissera ◽  
Cristina A Maldonado ◽  
...  
Keyword(s):  
Guinea Pig ◽  
Seminal Plasma ◽  
Semen Quality ◽  
Polyclonal Antibodies ◽  
World Health ◽  
Human Seminal Plasma ◽  
Sperm Surface ◽  
Epididymal Spermatozoa ◽  
Health Organization ◽  
Site Binding

β-Microseminoprotein (MSMB) is one of the most abundant proteins in human seminal plasma. The objectives of this study were: (1) to purify MSMB from seminal plasma (SP) and generate antibodies against the pure protein; (2) to investigate the interaction of MSMB with ejaculated spermatozoa and its possible effect on the spontaneous acrosome reaction (AR); and (3) to quantify MSMB content in SP and examine its relationship with the clinical sperm parameters. MSMB was purified from SP and its presence on the sperm surface was examined by indirect immunofluorescence using a specific polyclonal antibody. The effect of MSMB on the AR was evaluated using guinea pig epididymal spermatozoa as a model. MSMB quantification assay was performed with a two-site binding ELISA using two polyclonal antibodies against MSMB. MSMB was assessed in semen samples from fertile donors (controls) and subfertile patients according to World Health Organization criteria. MSMB was detected on the sperm surface and mainly localized to the acrosomal region of the head and neck. A significant spontaneous AR inhibition was observed when guinea pig epididymal spermatozoa were preincubated with MSMB. Finally, MSMB was significantly increased in subfertile patients when compared with fertile controls (P<0.02). The association of MSMB to the sperm surface, the inhibitor effect on the spontaneous AR and the increased MSMB levels found in SP in subfertile men suggests a relationship between this protein and semen quality and a possible role in the process of fertilization.

scholarly journals Investigation of Galectin-3 Function in the Reproductive Tract by Identification of Binding Ligands in Human Seminal Plasma

2014 ◽  
Vol 72 (4) ◽  
pp. 403-412 ◽  
Author(s):  
Matthew R. Kovak ◽  
Sarika Saraswati ◽  
David J. Schoen ◽  
Alan B. Diekman
Keyword(s):  
Seminal Plasma ◽  
Reproductive Tract ◽  
Human Seminal Plasma ◽  
Galectin 3

scholarly journals Natural Inhibitor of Human Cytomegalovirus in Human Seminal Plasma

2019 ◽  
Vol 93 (6) ◽  
Author(s):  
Sina Lippold ◽  
Berenike Braun ◽  
Franziska Krüger ◽  
Mirja Harms ◽  
Janis A. Müller ◽  
...  
Keyword(s):  
Human Cytomegalovirus ◽  
Seminal Plasma ◽  
Hcmv Infection ◽  
Sexual Transmission ◽  
Human Seminal Plasma ◽  
Glycoprotein Complex ◽  
Immunodeficiency Virus ◽  
Simplex Virus ◽  
Herpes Simplex Virus 2

ABSTRACT Human cytomegalovirus (HCMV) is the most frequent viral cause of congenital infections that can lead to severe birth defects. Although HCMV is frequently detected in semen and thus is potentially sexually transmitted, the role of semen in HCMV transmission is largely unclear. Here we describe that human seminal plasma (SP; the cell-free supernatant of semen) inhibits HCMV infection. The inhibition of HCMV infection was dose dependent and effective for different cell types, virus strains, and semen donors. This inhibitory effect was specific for HCMV, as herpes simplex virus 2 (HSV-2) and human immunodeficiency virus type 1 (HIV-1) infections were enhanced by SP. Mechanistically, SP inhibited infection by interfering with the attachment of virions to cells most likely via an interaction with the trimeric glycoprotein complex gH/gL/gO. Together, our findings suggest that semen contains a factor that potentially limits sexual transmission of HCMV. IMPORTANCE The role of semen in sexual transmission of human cytomegalovirus (HCMV) is currently unclear. This is surprising, as HCMV is frequently detected in this body fluid and infection is of high danger for neonates and pregnant women. In this study, we found that seminal plasma (SP) dose dependently inhibited HCMV infection. The infection inhibition was specific for HCMV, as other viruses, such as human immunodeficiency virus type 1 (HIV-1) and herpes simplex virus 2 (HSV-2), were not inhibited by SP. SP must contain a soluble, heat-resistant factor that limits attachment of HCMV particles to cells, probably by interaction with the trimeric glycoprotein complex gH/gL/gO. This novel virus-host interaction could possibly limit transmission of HCMV via semen during sexual intercourse.

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