scholarly journals MIG-23 is involved in sperm migration in Ascaris suum

2021 ◽  
Author(s):  
Xia Wang ◽  
Qiushi Wang ◽  
Ruijun He ◽  
Qi Zhang ◽  
Jin Shan ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Atpase Activity ◽  
Sperm Motility ◽  
Ascaris Suum ◽  
Nucleoside Triphosphate ◽  
Mitochondrial Activity ◽  
Major Sperm Protein ◽  
Sperm Activation ◽  
Sperm Migration ◽  
Sperm Plasma Membrane

Sperm motility acquisition during maturation is essential for successful fertilization.Extracellular adenosine-5'-triphosphate (ATP) level mediation by MIG-23, which is a homolog of human ecto-nucleoside triphosphate diphosphohydrolase (E-NTPDase), was required for major sperm protein filament dynamics and sperm motility in the nematode Ascaris suum. MIG-23 was localized on the sperm plasma membrane. During sperm activation, mitochondrial activity was increased dramatically, and a large amount of ATP was produced and stored in refringent granules (RGs). In addition, a portion of the produced ATP was released to the extracellular space through ATP channels, which were composed of innexins and localized on the sperm plasma membrane. Spermatozoa, instead of spermatids, hydrolyzed exogenous ATP and processed ecto-ATPase activity. MIG-23 contributed to the ecto-ATPase activity of spermatozoa. MIG-23 activity was interrupted, spermatozoa also decreased their ATP hydrolysis activity. Blocking MIG-23 activity resulted in an increase in the depolymerization rate of MSP filaments in pseudopodia, which eventually affected nematode sperm migration. Overall, our data imply that MIG-23, which contributes to the ecto-ATPase activity of spermatozoa, regulates sperm migration by modulating extracellular ATP levels.

Mechanism of human sperm activation by extracellular ATP

1996 ◽  
Vol 270 (6) ◽  
pp. C1709-C1714 ◽  
Author(s):  
C. Foresta ◽  
M. Rossato ◽  
P. Chiozzi ◽  
F. Di Virgilio
Keyword(s):  
Plasma Membrane ◽  
Acrosome Reaction ◽  
Human Sperm ◽  
Extracellular Atp ◽  
Effective Concentration ◽  
Na Channel ◽  
Monovalent Cations ◽  
Sperm Activation ◽  
Gated Channel ◽  
Sperm Plasma Membrane

We have identified the mechanism whereby extracellular ATP (ATPe) triggers the acrosome reaction in human spermatozoa. This nucleotide opens a ligand-gated ion channel expressed on the sperm plasma membrane. ATPe threshold and 50% effective concentration calculated on the total added ATPe are 0.1 and 2 mM, respectively, corresponding to a free ATP concentration (ATP4-) of 3 and 200 microM, respectively. The ATPe-gated channel is selective for monovalent cations (Na+, choline, and methylglucamine), whereas on the contrary, permeability to Ca2+ is negligible. Isosmolar replacement of extracellular Na+ with sucrose fully blocked ATPe-dependent sperm activation, thus suggesting a mandatory role for Na+ influx. These results show that human sperm express an ATPe-gated Na+ channel that might have an important role in sperm activation before egg fertilization.

187 EXPLOITATION OF IN VITRO CAPACITATION FOR NANOPARTICLE INCORPORATION WITHIN MAMMALIAN SPERMATOZOA

2016 ◽  
Vol 28 (2) ◽  
pp. 224
Author(s):  
L. Myles ◽  
C. Durfey ◽  
P. Ryan ◽  
S. Willard ◽  
J. Feugang
Keyword(s):  
Plasma Membrane ◽  
Sperm Motility ◽  
Surface Membrane ◽  
Milk Powder ◽  
Noninvasive Evaluation ◽  
Control Group ◽  
Body Tissues ◽  
Sperm Plasma Membrane

Migration and interactions of mammalian gametes occur in deep body tissues after mating, rendering difficult any in situ noninvasive evaluation of their performances with current methods. In our effort to develop an effective and real-time in vivo imaging approach, we have successfully labelled porcine gametes with self-illuminating bioluminescent and red-shifted quantum dot nanoparticles (QD) in our previous studies (Feugang et al. 2012 J. Nanobiotechnol. 10, 45; Feugang et al. 2015, J. Nanobiotechnol. 13, 38). The present effort aimed at investigating whether QD could be incorporated into spermatozoa through induced in vitro capacitation, which increases sperm plasma membrane fluidity. Fresh extended boar semen was placed on top of a Percoll gradient and centrifuged. Purified motile spermatozoa were collected and washed with pre-warmed PBS. Pelleted spermatozoa were resuspended in the modified Tris-buffered medium with BSA fraction-V (1 mg mL–1; modified Tween medium B with milk powder and BSA). Sperm aliquots (108) were supplemented or not (control) with QD only (QD+; 1 nM), QD+caffeine (2 mM), or QD+heparin (10 µg mL–1); with caffeine and heparin being used as routine capacitant agents in fertilization media. All aliquots were incubated at 38.5°C, under 5% CO2 for 0.5, 1, or 3 h. Spermatozoa were then analysed for motility characteristics and imaged for confirmation of QD-sperm interactions (bioluminescence emission) and localization (transmission electron microscope; TEM). Motility data of 5 replicates were analysed with ANOVA-2, and P < 0.05 was set as threshold of significance. Total sperm motility (TSM) significantly improved with the presence of either or both QDs and capacitant agents after 0.5 and 1 h incubations. With exception of the QD+heparin, all other groups had significantly decreased TSM after 3 h of incubation, when compared with TSM at 0.5 and 1 h. Higher proportions of progressive and rapid (≥45 µm s–1) spermatozoa were observed in the presence of both capacitant agents (P < 0.05), and only QD+heparin maintained greater proportions after 3 h. Sperm straight-line velocity significantly increased in the QD+caffeine at 0.5 h and in both QD+caffeine and QD+heparin thereafter. Sperm straightness data were increased by both caffeine and heparin during incubations. Strong bioluminescence signals were observed in spermatozoa incubated with QDs compared to the background signal seen in the control group. The TEM images revealed consistent surface membrane attachment of QDs in all QD+ groups, whereas transmembrane and intra-spermatic localizations were visible in both QD+caffeine and QD+heparin groups. We concluded that supplementations of medium containing QDs with caffeine or heparin allow the crossing of sperm plasma membrane by QD. No toxic effect of QD on sperm motility was observed, which confirmed our previous report using a similar ratio of QDs over spermatozoa. Exploration of efficient incorporation of QD into spermatozoa as a promising approach for noninvasive molecular imaging is still ongoing, as well as further sperm viability assessments. Supported by the NIH grant #5T35OD010432 and USDA-ARS Biophotonics Initiative grant #58–6402–3-0120.

scholarly journals Effects of the addition of docosahexaenoic acid and ?-tocopherol on quality of equine spermatozoa stored at 5°C

2020 ◽  
Vol 41 (1) ◽  
pp. 167 ◽  
Author(s):  
Breno Fernandes Barreto Sampaio ◽  
Bruno Gomes Nogueira ◽  
Maria Inês Lenz Souza ◽  
Eliane Vianna da Costa-e-Silva ◽  
Carmem Estefânia Serra Neto Zúccari
Keyword(s):  
Lipid Peroxidation ◽  
Plasma Membrane ◽  
Docosahexaenoic Acid ◽  
Sperm Motility ◽  
Membrane Integrity ◽  
Control Group ◽  
Mitochondrial Activity ◽  
Membrane Composition ◽  
Artificial Vagina

Plasma membrane composition has impact on phase transition from liquid crystal to gel state of cooled sperm cell. The incorporation of polyunsaturated fatty acids increases its fluidity and can contribute to sperm motility. The aim of this study was to compare the effect of adding docosahexaenoic acid (DHA) and ?-tocopherol (?-Toh) to the cooling extender, singly or combined, to the equine sperm parameters, submitted to cooling, up to 72 hours. Two ejaculates of ten stallions collected with artificial vagina were used, and evaluated for motility, plasma membrane integrity, chromatin fragmentation, mitochondrial activity and lipid peroxidation, according to the following treatments: C; DHA; ?-Toh; DHA/?-Toh; EtOH 100: and EtOH 140 (corresponding to control; 10 ng mL-1 of DHA; 2 mM of ?-Toh; : 10 ng mL-1 of DHA + 2 mM of ?-Toh; 100 µL of ethanol and 140 µL of ethanol respectively). DHA treatment showed higher motility (68.2 ± 12.3; p < 0.05) when compared to control (62.1 ± 16.2), DHA/?-Toh (61.3 ± 12.7) and EtOH (58.1 ± 8.6) groups. In lipid peroxidation assay, the control group showed 2,506.2 ± 796.4 ng of MDA 108 spermatozoa-1, being significantly higher (p < 0.05) than the groups treated with DHA (2,036.0 ± 687.0), ?-Toh (1,890.8 ± 749.5) and DHA/?-Toh (1,821.1 ± 627.2). In conclusion, ?-Toh was effective in diminishing lipid peroxidation of equine sperm subjected to cooling, and DHA improved sperm motility and, in spite of being a polyunsaturated fatty acid with high susceptibility to peroxidation, reduced lipid peroxidation.

Plasma membrane changes during the liquid storage of boar spermatozoa: A comparison of methods

2010 ◽  
Vol 58 (1) ◽  
pp. 105-116 ◽  
Author(s):  
Dariusz Gączarzewicz ◽  
Małgorzata Piasecka ◽  
Jan Udała ◽  
Barbara Błaszczyk ◽  
Tomasz Stankiewicz ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Sperm Motility ◽  
Semen Analysis ◽  
Membrane Integrity ◽  
Live Cells ◽  
Lower Percentage ◽  
Loss Of Function ◽  
Plasma Membrane Integrity ◽  
Sperm Plasma Membrane ◽  
Semen Preservation

Studies were performed on boar semen routinely used at the local artificial insemination (AI) centre. The semen was stored in a Safe Cell Plus commercial extender at 17 °C for nine days. The aim of our research was focused on changes in sperm plasma membrane integrity. The integrity of the sperm plasma membrane and acrosome as well as sperm motility decreased after dilution and during storage of the semen. The highest percentage of live sperm was identified by the eosin-nigrosin method, a lower percentage by the SYBR-14/PI test, and the lowest percentage of live cells was discovered by the hypoosmotic swelling (HOS) test (P < 0.01). There were significant differences between the results of staining methods and sperm motility (P < 0.01). No significant differences were found between the HOS test results and sperm motility. The plasma membrane integrity parameters positively correlated (P < 0.001) with each other and with sperm motility but negatively with aspartate aminotransferase activity. Our findings confirmed that the boar sperm aging changes, which increased during liquid semen preservation, were connected with the loss of function and integrity of the sperm plasma membrane. The employed complementary tests are comprehensive indicators of sperm membrane integrity during long-term semen preservation, and they can help establish the actual number of ‘healthy’ cells. The assays may be used in AI laboratories and should be incorporated into the routine of semen analysis.

scholarly journals Dissecting the PRSS37 interactome and potential mechanisms leading to ADAM3 loss in PRSS37 null sperm

2021 ◽  
Author(s):  
Wenfeng Xiong ◽  
Chunling Shen ◽  
Chaojie Li ◽  
Xiaohong Zhang ◽  
Haoyang Ge ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Plasma Membrane ◽  
Cell Surface ◽  
Male Infertility ◽  
Molecular Chaperones ◽  
Epididymal Sperm ◽  
Sperm Migration ◽  
Sperm Plasma Membrane ◽  
Sperm Membrane ◽  
A Disintegrin And Metalloproteinase

A disintegrin and metalloproteinase 3 (ADAM3) is a sperm membrane protein critical for sperm migration from the uterus into the oviduct and sperm-egg binding in mice. Disruption of PRSS37 results in male infertility concurrent with the absence of mature ADAM3 from cauda epididymal sperm. However, how PRSS37 modulates ADAM3 maturation remains largely unclear. Here, we determine PRSS37 interactome by GFP immunoprecipitation coupled with mass spectrometry in PRSS37-EGFP knock-in mice. Three molecular chaperones (CLGN, CALR3 and PDILT) and three ADAM proteins (ADAM2, ADAM6B and ADAM4) were identified to be interacting with PRSS37. Coincidently, five of them (except ADAM4) have been reported to interact with precursor ADAM3 and regulate its maturation. We further demonstrated that PRSS37 also interacts directly with precursor ADAM3 and its deficiency impedes the association between PDILT and ADAM3. This could contribute to improper translocation of ADAM3 to the germ cell surface, leading to ADAM3 loss in PRSS37 null mature sperm. The understanding of the maturation mechanisms of pivotal sperm plasma membrane proteins will pave the way toward novel strategies for contraception and treatment of unexplained male infertility.

scholarly journals ATPases, ion exchangers and human sperm motility

Reproduction ◽  
2015 ◽  
Vol 149 (5) ◽  
pp. 475-484 ◽  
Author(s):  
Rubén D Peralta-Arias ◽  
Carmen Y Vívenes ◽  
María I Camejo ◽  
Sandy Piñero ◽  
Teresa Proverbio ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Atpase Activity ◽  
Sperm Motility ◽  
Plasma Membranes ◽  
Semen Analysis ◽  
Human Sperm ◽  
The Other ◽  
Computer Assisted ◽  
Acidic Ph ◽  
Α Subunit

Human sperm has several mechanisms to control its ionic milieu, such as the Na,K-ATPase (NKA), the Ca-ATPase of the plasma membrane (PMCA), the Na+/Ca2+-exchanger (NCX) and the Na+/H+-exchanger (NHE). On the other hand, the dynein-ATPase is the intracellular motor for sperm motility. In this work, we evaluated NKA, PMCA, NHE, NCX and dynein-ATPase activities in human sperm and investigated their correlation with sperm motility. Sperm motility was measured by Computer Assisted Semen Analysis. It was found that the NKA activity is inhibited by ouabain with twoKi(7.9×10−9and 9.8×10−5 M), which is consistent with the presence of two isoforms of α subunit of the NKA in the sperm plasma membranes (α1 and α4), being α4 more sensitive to ouabain. The decrease in NKA activity is associated with a reduction in sperm motility. In addition, sperm motility was evaluated in the presence of known inhibitors of NHE, PMCA and NCX, such as amiloride, eosin, and KB-R7943, respectively, as well as in the presence of nigericin after incubation with ouabain. Amiloride, eosin and KB-R7943 significantly reduced sperm motility. Nigericin reversed the effect of ouabain and amiloride on sperm motility. Dynein-ATPase activity was inhibited by acidic pH and micromolar concentrations of Ca2+. We explain our results in terms of inhibition of the dynein-ATPase in the presence of higher cytosolic H+and Ca2+, and therefore inhibition of sperm motility.

scholarly journals Lipid composition of the canine sperm plasma membrane as markers of sperm motility

2016 ◽  
Vol 52 ◽  
pp. 208-213 ◽  
Author(s):  
CF Lucio ◽  
MM Brito ◽  
DSR Angrimani ◽  
KRA Belaz ◽  
D Morais ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Sperm Motility ◽  
Lipid Composition ◽  
Sperm Plasma Membrane
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