Low physiological levels of prostaglandins E2 and F2α improve human sperm functions

2016 ◽  
Vol 28 (4) ◽  
pp. 434 ◽  
Author(s):  
Mariana Rios ◽  
Daniela V. Carreño ◽  
Carolina Oses ◽  
Nelson Barrera ◽  
Bredford Kerr ◽  
...  
Keyword(s):  
Intracellular Calcium ◽  
Sperm Motility ◽  
Acrosome Reaction ◽  
Seminal Fluid ◽  
Human Sperm ◽  
Human Spermatozoa ◽  
Control Solution ◽  
Prostaglandins E2 And F2α ◽  
Motility Parameters ◽  
Sperm Functions

Prostaglandins (PGs) have been reported to be present in the seminal fluid and cervical mucus, affecting different stages of sperm maturation from spermatogenesis to the acrosome reaction. This study assessed the effects of low physiological PGE2 and PGF2α concentrations on human sperm motility and on the ability of the spermatozoa to bind to the zona pellucida (ZP). Human spermatozoa were isolated from seminal samples with normal concentration and motility parameters and incubated with 1 μM PGE2, 1 μM PGF2α or control solution to determine sperm motility and the ability to bind to human ZP. The effects of both PGs on intracellular calcium levels were determined. Incubation for 2 or 18 h with PGE2 or PGF2α resulted in a significant (P < 0.05) increase in the percentage of spermatozoa with progressive motility. In contrast with PGF2α, PGE2 alone induced an increase in sperm intracellular calcium levels; however, the percentage of sperm bound to the human ZP was doubled for both PGs. These results indicate that incubation of human spermatozoa with low physiological levels of PGE2 or PGF2α increases sperm functions and could improve conditions for assisted reproduction protocols.

scholarly journals Role of Angiotensin-(1–7) via MAS receptor in human sperm motility and acrosome reaction

Reproduction ◽  
2020 ◽  
Vol 159 (3) ◽  
pp. 241-249 ◽  
Author(s):  
Asier Valdivia ◽  
Lorea Cortés ◽  
Maider Beitia ◽  
Lide Totorikaguena ◽  
Naiara Agirregoitia ◽  
...  
Keyword(s):  
Sperm Motility ◽  
Acrosome Reaction ◽  
Mrna Level ◽  
Human Sperm ◽  
Human Spermatozoa ◽  
Dependent Manner ◽  
Mas Receptor ◽  
Sperm Mobility ◽  
Specific Antagonist

Rennin-angiotensin system (RAS) has been involved in sperm function, even so, little is known about the implication of one of the RAS axis formed by Ang-(1–7) (angiotensin-(1–7)) and MAS receptor. Hence, in the present work, we focused on elucidating the function of the MAS receptor in human spermatozoa. We analyzed the expression and localization of MAS receptor in human spermatozoa and we observed if its activation is able to modulate the sperm motility of normal motility and/or asthenozoospermic patients, as well as, the acrosome reaction of the spermatozoa. MAS receptor is present in human mature spermatozoa, not only at the mRNA level but also at protein level. MAS is localized at the acrosome region, as well as, in the tail of spermatozoa. The sperm incubation with MAS agonist Ang-(1–7) activates at dose-dependent manner the PI3K/AKT pathway (P < 0.01 vs control) and improves the motility of asthenozoospermic patients (P < 0.01 vs control), which is blocked by the specific antagonist (A779) (P < 0.01), but it do not modulate the acrosome reaction. These findings suggest that the ACE2/Ang-(1–7)/Mas axis may be a useful biochemical tool for the treatment of male infertility related to sperm mobility.

Role of Ca2+ in the IVM of spermatozoa from the sterlet Acipenser ruthenus

2017 ◽  
Vol 29 (7) ◽  
pp. 1319 ◽  
Author(s):  
Olga Bondarenko ◽  
Borys Dzyuba ◽  
Marek Rodina ◽  
Jacky Cosson
Keyword(s):  
Sperm Motility ◽  
Seminal Fluid ◽  
Mature Male ◽  
Sperm Maturation ◽  
Wolffian Duct ◽  
Testicular Spermatozoa ◽  
Acipenser Ruthenus ◽  
Sterlet Acipenser Ruthenus ◽  
Motility Parameters

The role of Ca2+ in sturgeon sperm maturation and motility was investigated. Sperm from mature male sterlets (Acipenser ruthenus) were collected from the Wolffian duct and testis 24 h after hormone induction. Testicular spermatozoa (TS) were incubated in Wolffian duct seminal fluid (WDSF) for 5 min at 20°C and were designated ‘TS after IVM’ (TSM). Sperm motility was activated in media with different ion compositions, with motility parameters analysed from standard video microscopy records. To investigate the role of calcium transport in the IVM process, IVM was performed (5 min at 20°C) in the presence of 2 mM EGTA, 100 µM Verapamil or 100 µM Tetracaine. No motility was observed in the case of TS (10 mM Tris, 25 mM NaCl, 50 mM Sucr with or without the addition of 2 mM EGTA). Both incubation of TS in WDSF and supplementation of the activation medium with Ca2+ led to sperm motility. The minimal Ca2+ concentration required for motility activation of Wolffian duct spermatozoa, TS and TSM was determined (1–2 nM for Wolffian duct spermatozoa and TSM; approximately 0.6 mM for TS). Motility was obtained after the addition of verapamil to the incubation medium during IVM, whereas the addition of EGTA completely suppressed motility, implying Ca2+ involvement in sturgeon sperm maturation. Further studies into the roles of Ca2+ transport in sturgeon sperm maturation and motility are required.

scholarly journals Soluble adenylyl cyclase inhibition prevents human sperm functions essential for fertilization

2021 ◽  
Author(s):  
Melanie Balbach ◽  
Lubna Ghanem ◽  
Thomas Rossetti ◽  
Navpreet Kaur ◽  
Carla Ritagliati ◽  
...  
Keyword(s):  
Adenylyl Cyclase ◽  
Acrosome Reaction ◽  
Human Sperm ◽  
Comprehensive Analysis ◽  
Multiple Points ◽  
Soluble Adenylyl Cyclase ◽  
Mouse Sperm ◽  
On Demand ◽  
Sperm Functions

AbstractSoluble adenylyl cyclase (sAC: ADCY10) is essential for activating dormant sperm. Studies of freshly dissected mouse sperm identified sAC as needed for initiating capacitation and activating motility. We now use an improved sAC inhibitor, TDI-10229, for a comprehensive analysis of sAC function in human sperm. Unlike dissected mouse sperm, human sperm are collected post-ejaculation, after sAC activity has already been stimulated. Even in ejaculated human sperm, TDI-10229 interrupts stimulated motility and capacitation, and it prevents acrosome reaction in capacitated sperm. At present, there are no non-hormonal, pharmacological methods for contraception. Because sAC activity is required post-ejaculation at multiple points during the sperm’s journey to fertilize the oocyte, sAC inhibitors define candidates for non-hormonal, on-demand contraceptives suitable for delivery via intravaginal devices in females.

scholarly journals Sphingomyelin Synthase 2 Participate in the Regulation of Sperm Motility and Apoptosis

Molecules ◽  
2020 ◽  
Vol 25 (18) ◽  
pp. 4231
Author(s):  
Xiatian Li ◽  
Tao Luo ◽  
Hua Li ◽  
Nianlong Yan
Keyword(s):  
Signaling Pathways ◽  
Sperm Motility ◽  
Acrosome Reaction ◽  
Caspase 3 ◽  
Human Sperm ◽  
Erk Signaling ◽  
Sperm Function ◽  
Sphingomyelin Synthase ◽  
Protein Levels ◽  
Penetration Ability

Sphingomylin participates in sperm function in animals, and also regulates the Akt and ERK signaling pathways, both of which are associated with the asthenospermia. Sphingomyelin synthase 2 (SMS2) is involved in the biosynthesis of sphingomylin. To determine the relationship between SMS2 and human sperm function, we analyzed the distribution of SMS2 in human sperm and testes, and SMS2 expression in patients with asthenospermia and normozoospermia; human sperm were treated with anti-SMS2, and the sperm motility, penetration ability into methylcellulose, capacitation and acrosome reaction, and sperm [Ca2+]i imaging were evaluated, while the Akt and ERK pathway and cleaved caspase 3 were also analyzed. Results showed that SMS2 was localized in the testis and human sperm, and the protein levels of normozoospermia were higher than asthenospermia. Inhibition of SMS2 activity significantly decreased sperm motility and penetration ability into methylcellulose, but had no influence on capacitation and acrosome reaction, or on intracellular [Ca2+]i compared to IgG-treated control groups. Moreover, the phosphorylation level of Akt was decreased, whereas the phosphorylation of ERK and cleaved-caspase 3 levels were significantly increased. Taken together, SMS2 can affect sperm motility and penetration ability into methylcellulose, and participate in apoptosis associated with the Akt and ERK signaling pathways.

Vitamin D Is Positively Associated With Sperm Motility and Increases Intracellular Calcium in Human Spermatozoa

2011 ◽  
Vol 66 (9) ◽  
pp. 556-558 ◽  
Author(s):  
Martin B. Jensen ◽  
Poul J. Bjerrum ◽  
Torben E. Jessen ◽  
John E. Nielsen ◽  
Ulla N. Joensen ◽  
...  
Keyword(s):  
Vitamin D ◽  
Intracellular Calcium ◽  
Sperm Motility ◽  
Human Spermatozoa

scholarly journals Hsp90 Modulates Human Sperm Capacitation via the Erk1/2 and p38 MAPK Signaling Pathways

2020 ◽  
Author(s):  
Peibei Sun ◽  
Yayan Wang ◽  
Tian Gao ◽  
Kun Li ◽  
Dongwang Zheng ◽  
...  
Keyword(s):  
Signaling Pathways ◽  
P38 Mapk ◽  
Sperm Motility ◽  
Western Blotting ◽  
Protein Complex ◽  
Acrosome Reaction ◽  
Human Sperm ◽  
Mapk Signaling ◽  
Sperm Capacitation ◽  
Mapk Signaling Pathways

Abstract Background: Heat shock protein 90 (Hsp90) is a highly abundant eukaryotic molecular chaperone that plays important roles in client protein maturation, protein folding and degradation, and signal transduction. Previously, we found that both Hsp90 and its co-chaperone cell division cycle protein 37 (Cdc37) were expressed in human sperm. Hsp90 is known to be involved in human sperm capacitation via unknown underlying mechanism(s). As Cdc37 was a kinase-specific co-chaperone of Hsp90, Hsp90 may regulate human sperm capacitation via other kinases. It has been reported that two major mitogen-activated protein kinases (MAPKs), extracellular signal-regulated kinase 1/2 (Erk1/2) and p38, are expressed in human sperm in the same locations as Hsp90 and Cdc37. Phosphorylated Erk1/2 has been shown to promote sperm hyperactivated motility and acrosome reaction, while phosphorylated p38 inhibits sperm motility. Therefore, in this study we explored whether Hsp90 modulates human sperm capacitation via the Erk1/2 and p38 MAPK signaling pathways. Methods: Human sperm was treated with the Hsp90-specific inhibitor 17-allylamino-17-demethoxygeldanamycin (17-AAG) during capacitation. Computer-assisted sperm analyzer (CASA) was used to detect sperm motility and hyperactivation. The sperm acrosome reaction was analyzed by using fluorescein isothiocyanate-conjugated Pisum sativum agglutinin (PSA-FITC) staining. The interactions between Hsp90, Cdc37, Erk1/2 and p38 were assessed using co-immunoprecipitation (Co-IP) experiments. Western blotting analysis was used to evaluate the levels of protein expression and phosphorylation. Results: Human sperm hyperactivation and acrosome reaction were inhibited by 17-AAG, suggesting that Hsp90 is involved in human sperm capacitation. In addition, Co-IP experiments revealed that 17-AAG reduced the interaction between Hsp90 and Cdc37, leading to the dissociation of Erk1/2 from the Hsp90-Cdc37 protein complex. Western blotting analysis revealed that levels of Erk1/2 and its phosphorylated form were subsequently decreased. Decreasing of Hsp90-Cdc37 complex also affected the interaction between Hsp90 and p38. Nevertheless, p38 dissociated from the Hsp90 protein complex and was activated by autophosphorylation. Conclusions: Taken together, our findings indicate that Hsp90 is involved in human sperm hyperactivation and acrosome reaction. In particular, Hsp90 and its co-chaperone Cdc37 form a protein complex with Erk1/2 and p38 to regulate their kinase activity. These results suggest that Hsp90 regulates human sperm capacitation via the Erk1/2 and p38 MAPK signaling pathways.

O-152 Investigation of the relationship of sperm motility and Kisspeptin in subfertile men

2021 ◽  
Vol 36 (Supplement_1) ◽  
Author(s):  
A Kocaman ◽  
B Ayas
Keyword(s):  
Gene Expression ◽  
Intracellular Calcium ◽  
Sperm Motility ◽  
Laser Scanning ◽  
Calcium Release ◽  
Expression Levels ◽  
Significant Difference ◽  
Motility Parameters ◽  
Gene Expression Levels

Abstract Study question Does kisspeptin administration affect the motility parameters in sperm samples of subfertile cases? Summary answer Kisspeptin administration significantly increased gene expression levels related with sperm motility as well as intracellular calcium concentrations. What is known already Sperm motility problems are among the most important causes of male infertility. In recent years, a peptide named kisspeptin has been discovered that may have effects on sperm motility. Kisspeptin is known to trigger calcium release in hypothalamic neurons. In addition, kisspeptin administration increased sperm progressive motility in studies conducted on normozoospermic individuals. Furthermore, it is suggested that kisspeptin protein in seminal plasma is positively associated with semen quality. However, there is no evidence that how kisspeptin can affect sperm in men with infertility problems. Study design, size, duration This basic research study was an in vitro experimental approach involving the use of semen samples from an infertil cases between September to December in 2020. 40 men were included in both control and experimental groups. Participants/materials, setting, methods All analyses were performed on semen samples from 10 normozoospermic (NZ), 10 asthenozoospermic (AZ), 10 oligoasthenozoospermic (OAZ) and 10 oligoastenoteratozoospermic (OATZ) men, aging between (21-40) years. Basal serum and seminal kisspeptin levels were analyzed by ELISA. Sperm were divided into two groups. Kisspeptin-13 administered in vitro. KISS1, KISS1R, CATSPER1, AKAP4 gene expressions analyzed by qRT-PCR using 2−ΔΔCt algorithm. Intracellular calcium concentration was determined with floresence spectroflurometer and laser scanning confocal microscope. Main results and the role of chance The serum kisspeptin level of NZ was significantly higher than other groups (p &lt; 0.05). The semen kisspeptin level was significantly higher than OAZ and OATZ (p &lt; 0.05), but not in NZ (p &gt; 0.05). Also, KISS1 gene expression was higher in AZ compared to other groups (p &lt; 0.05). Biochemical and gene expression analysis of kisspeptin were consistent with each other. There was a significant increase in the expression of CATSPER1 gene in AZ compared to other groups (p &lt; 0.05). Also, AKAP4 gene expression was significantly higher in OATZ compared to other groups (p &lt; 0.05). No significant difference was documented for the expression of KISS1R (p &gt; 0.05). Intracellular calcium was significantly increased in AZ and NZ after kisspeptin administration. The intracellular calcium increase is consistent with increased CATSPER1 gene expression levels in AZ. Kisspeptin administration may have a significant effect on sperm motility parameters. Limitations, reasons for caution The biochemical and gene expression levels of KISS1 were consistent. However, gene expression was explored at the mRNA level for CATSPER1 and AKAP4. The protein expression analyses of these genes may confirm the results. Also, using kisspeptin antagonists may strength the results of intracellular calcium analysis. Wider implications of the findings Kisspeptin treatment for individuals diagnosed with asthenozoospermia may have therapeutic results. KISS1 quantitation may be a determining factor for the subfertility in routine semen analysis. Trial registration number OMU KAEK 2019/462

Testis developmental related gene 1 (TDRG1) encodes a progressive motility-associated protein in human spermatozoa

2020 ◽  
Author(s):  
Houyang Chen ◽  
Liang Tang ◽  
Qing Hong ◽  
Tingting Pan ◽  
Shiqi Weng ◽  
...  
Keyword(s):  
Sperm Motility ◽  
Conflicts Of Interest ◽  
Human Sperm ◽  
Human Spermatozoa ◽  
Mass Spectrometry Analysis ◽  
Human Testis ◽  
Specific Gene ◽  
Related Gene ◽  
Progressive Motility ◽  
Related Proteins

Abstract STUDY QUESTION Is there an association between the human testis-specific gene, testis developmental related gene 1 (TDRG1) and human sperm motility? SUMMARY ANSWER TDRG1 is associated with asthenozoospermia and involved in regulating human sperm motility. WHAT IS KNOWN ALREADY Many testis-specific proteins potentially regulate spermatogenesis and sperm motility. We have identified a novel human testis-specific gene, TDRG1, which encodes a 100-amino-acid protein localized in the human sperm tail, yet little is known about its role in human spermatozoa. STUDY DESIGN, SIZE, DURATION Sperm samples were obtained from normozoospermic men and asthenozoospermic men who visited the reproductive medical center at Jiangxi Maternal and Child Health Hospital, Nanchang, Jiangxi, China between February 2018 and January 2019. In total, 27 normozoospermic men and 25 asthenozoospermic men were recruited to participate in the study. PARTICIPANTS/MATERIALS, SETTING, METHODS The level of TDRG1 in sperm of normozoospermic and asthenozoospermic men was examined by immunoblotting and immunofluorescence assays. Progressive motility was examined by computer-aided sperm analysis. The correlation between the TDRG1 protein level and progressive motility was analyzed by linear regression. TDRG1 was imported into the sperm of normozoospermic and asthenozoospermic men using a cell-penetrating peptide (CPP)-fused TDRG1 recombinant protein (CPP-TDRG1), and the progressive motility was examined. Also, the altered proteins associated with TDRG1 in asthenozoospermic sperm were detected using label-free quantification method-based quantitative proteomic technology. TDRG1-interacting proteins were identified by co-immunoprecipitation coupled with tandem mass spectrometry analysis. MAIN RESULTS AND THE ROLE OF CHANCE The mean level of TDRG1 was significantly decreased in sperm of asthenozoospermic men compared with normozoospermic men (P &lt; 0.05) and was positively correlated with percentage of progressively motile sperm (r2 = 0.75, P = 0.0001). The introduction of TDRG1 into human sperm, using CPP, significantly increased progressive motility (P &lt; 0.05) and improved the progressive motility of sperm from asthenozoospermic men to the normal level. TDRG1 forms a protein complex with sperm-motility related proteins in human sperm and its downregulation was associated with a decrease in other motility-related proteins. LARGE SCALE DATA N/A. LIMITATIONS, REASONS FOR CAUTION The sample size was limited and larger cohorts are needed for verifying the positive effect of CPP-TDRG1 on human sperm motility. Furthermore, the caution should be paid that a comprehensive safety examination would be performed to evaluate whether CPP-TDRG1 is a possible treatment approach for asthenozoospermia. WIDER IMPLICATIONS OF THE FINDINGS Our results provide new insights into the mechanisms of sperm motility which may contribute to the diagnosis and treatment for asthenozoospermia. STUDY FUNDING/COMPETING INTEREST(S) National Natural Science Foundation of China (81501317 and 81871207 to H.C.; 81771644 to T.L.; 31671204 to X.Z.; 81571432 to Y.T.). The authors have no conflicts of interest to declare.

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