scholarly journals Expression, localization and functions in acrosome reaction and sperm motility of CaV3.1 and CaV3.2 channels in sperm cells: An evaluation from CaV3.1 and CaV3.2 deficient mice

2007 ◽  
Vol 212 (3) ◽  
pp. 753-763 ◽  
Author(s):  
Jessica Escoffier ◽  
Sylvie Boisseau ◽  
Catherine Serres ◽  
Chien-Chang Chen ◽  
Daesoo Kim ◽  
...  
Keyword(s):  
Sperm Motility ◽  
Acrosome Reaction ◽  
Sperm Cells ◽  
Deficient Mice

Molecular basis of adaptive evolution of sperm motility involved in in vivo fertilization of terrestrial animals

Impact ◽  
2020 ◽  
Vol 2020 (6) ◽  
pp. 73-75
Author(s):  
Akihiko Watanabe
Keyword(s):  
Sexual Reproduction ◽  
Sperm Motility ◽  
Asexual Reproduction ◽  
Acrosome Reaction ◽  
Sperm Morphology ◽  
Adaptive Potential ◽  
Selective Pressures ◽  
The Face ◽  
Genetic Profiles

One of the unifying traits of life on this planet is reproduction, or life's ability to make copies of itself. The mode of reproduction has evolved over time, having almost certainly begun with simple asexual reproduction when the ancestral single celled organism divided into two. Since these beginnings' life has tried out numerous strategies, and perhaps one of the most important and successful has been sexual reproduction. This form of reproduction relies on the union of gametes, otherwise known as sperm and egg. Evolutionarily, sexual reproduction allows for greater adaptive potential because the genes of two unique individuals have a chance to recombine and mix in order to produce a new individual. Unlike asexual reproduction which produces genetically-identical clones of the parent individual, sex produces offspring with novel genes and combinations of genes. Therefore, in the face of new selective pressures there is a higher chance that one of these novel genetic profiles will produce an adaptation that is advantageous in the new circumstances. Dr Akihiko Watanabe is a reproductive biologist based in the Department of Biology, Faculty of Science Yamagata University in Japan, he is currently working on three research projects; a comparative study on the signalling pathways for inducing sperm motility and acrosome reaction in amphibians, the mechanism behind the adaptive modification of sperm morphology and motility, and the origin of sperm motility initiating substance (SMIS).

scholarly journals Effects of diadenosine polyphosphates and seminal fluid vesicles on rabbit sperm cells

Reproduction ◽  
2003 ◽  
pp. 827-835 ◽  
Author(s):  
A Minelli ◽  
L Liguori ◽  
I Bellezza ◽  
T Renieri ◽  
C Castellini
Keyword(s):  
High Performance ◽  
Acrosome Reaction ◽  
Seminal Fluid ◽  
Membrane Vesicles ◽  
Fluorescein Isothiocyanate ◽  
Plasma Electron ◽  
Sperm Cells ◽  
Experimental Conditions ◽  
Diadenosine Polyphosphates ◽  
Rabbit Spermatozoa

Membrane vesicles were isolated from rabbit seminal plasma. Electron microscopy analyses showed the presence of numerous small, round vesicles with a diameter of about 70 nm. Determination of enzyme activities was carried out by high performance liquid chromatography and showed that the vesicles can degrade the diadenosine polyphosphates (ApnA), Ap3A and Ap4A and ATP and ADP, but not AMP. Studies of the degradation of diadenosine compounds by the vesicles present in seminal fluid showed an increasing production of AMP as the by-product and a time-dependent generation of dephosphorylated products consistent with the presence of ecto-ATP diphosphophosphatase (ecto-apyrase). In the presence of rabbit spermatozoa, AMP did not accumulate because 5'nucleotidase and adenosine deaminase, present at the surface of sperm cells, transformed AMP into adenosine and inosine. The effects of seminal fluid vesicles and diadenosine compounds on the acquisition of fertilizing capacity by rabbit spermatozoa were evaluated by Pisum sativum agglutinin fluorescein isothiocyanate conjugated staining. The results obtained with uncapacitated spermatozoa showed that the capacitating effector BSA could be substituted efficiently by the addition of diadenosine compounds and vesicles previously incubated for 2 h to the capacitative medium. Under these experimental conditions, the spontaneous acrosome reaction rate was not increased. Capacitated rabbit spermatozoa did not undergo acrosome reaction when l-alpha-lysophosphatidylcholine was substituted by diadenosine compounds previously incubated with vesicles. In conclusion, this study has shown that rabbit seminal fluid vesicles can degrade diadenosine compounds to AMP and that the addition of the vesicles and diadenosine compounds to uncapacitated rabbit spermatozoa favours the acquisition of the fertilizing capacity.

scholarly journals PACAP-mediated sperm–cumulus cell interaction promotes fertilization

Reproduction ◽  
2011 ◽  
Vol 141 (2) ◽  
pp. 163-171 ◽  
Author(s):  
Ichiro Tanii ◽  
Tadashi Aradate ◽  
Kouhei Matsuda ◽  
Akira Komiya ◽  
Hideki Fuse
Keyword(s):  
Sperm Motility ◽  
Acrosome Reaction ◽  
Cumulus Cell ◽  
Cumulus Cells ◽  
Cell Interaction ◽  
Fertilization Rate ◽  
Type I ◽  
Dependent Manner ◽  
Sperm Penetration

The developing acrosome in spermatids contains pituitary adenylate cyclase-activating polypeptide (PACAP). However, the role of the acrosomal PACAP remains unclear because it has not been detected in mature spermatids and sperm. We reinvestigated whether the sperm acrosome contains PACAP. An antiserum produced against PACAP reacted to the anterior acrosome in epididymal sperm fixed under mild conditions, suggesting that PACAP acts on oocytes and/or cumulus cells at the site of fertilization. Immunolabeling and RT-PCR demonstrated the presence of PACAP type I receptor, a PACAP-specific receptor, in postovulatory cumulus cells. To investigate the role of PACAP in fertilization, we pretreated cumulus–oocyte complexes with the polypeptide. At a low concentration of sperm, the fertilization rate was significantly enhanced by PACAP in a dose-dependent manner. Sperm penetration through the oocyte investment, cumulus layer, and zona pellucida was also enhanced by PACAP. The enhancement was probably due to an enhancement in sperm motility and the zona-induced acrosome reaction, which were stimulated by a cumulus cell-releasing factor. Indeed, PACAP treatment increased the secretion of progesterone from the cumulus–oocyte complexes. These results strongly suggest that in response to PACAP, cumulus cells release a soluble factor that probably stimulates sperm motility and the acrosome reaction, thereby promoting fertilization.

scholarly journals Effects of calpain and Rho-kinase inhibitors on the acrosome reaction and motility of fowl spermatozoa in vitro

Reproduction ◽  
2006 ◽  
Vol 131 (1) ◽  
pp. 71-79 ◽  
Author(s):  
K Ashizawa ◽  
G J Wishart ◽  
S Katayama ◽  
D Takano ◽  
M Maeda ◽  
...  
Keyword(s):  
Sperm Motility ◽  
Acrosome Reaction ◽  
Kinase Inhibitors ◽  
Rho Kinase ◽  
Specific Inhibitor ◽  
Immunoblot Analysis ◽  
Calpain Inhibitor ◽  
Cytoplasmic Matrix ◽  
Sperm Extract

At the avian body temperature of 40 °C, intact fowl spermatozoa require Ca2+for the initiation of motility and a combination of both Ca2+and homogenized inner perivitelline layer (IPVL) together to induce the acrosome reaction. Within the range of 1–100 μmol/l, neither PD 150606 (a Ca2+-dependent calpain inhibitor) nor Y-27632 (an inhibitor of Ca2+-dependent Rho-kinase) were able to inhibit the acrosome reaction induced by the presence of Ca2+and IPVL. However, PD 150606, although not Y-27632, was able to inhibit sperm motility initiated by Ca2+, as well as motility initiated by calyculin A – a specific inhibitor of protein phosphatases, which also initiates sperm motility at 40 °C. The addition of PD 150606 did not reduce the ATP concentrations of intact spermatozoa, nor the motility of demembranated spermatozoa. Immunoblot analysis of sperm extract using a polyclonal antibody against calpain 12 revealed a cross-reacting protein of approximately 80 kDa. These results suggest that Rho-kinase is not involved in the regulation of the acrosome reaction or of motility in fowl spermatozoa. In contrast, calpain appears to be involved in the regulation of flagellar movement, but not izn that of the acrosome reaction. Furthermore, it seems that endogenous calpain is present in the cytoplasmic matrix and/or the plasma membrane, but not retained in the axoneme and/or accessory cytoskeletal components.

scholarly journals Cooling of equine semen at 16°C for 36 hours with addition of different glutathione concentrations

2015 ◽  
Vol 36 (6) ◽  
pp. 3699
Author(s):  
Rodrigo Arruda de Oliveira ◽  
Marco Antônio De Oliveira Viu ◽  
Maria Lúcia Gambarini
Keyword(s):  
Lipid Peroxidation ◽  
Sperm Motility ◽  
Membrane Integrity ◽  
Membrane Lipid ◽  
Sperm Cells ◽  
Sperm Viability ◽  
Membrane Lipid Peroxidation ◽  
Acrosomal Membrane ◽  
In Vitro Effects

Handling equine semen during the refrigeration process reduces sperm viability, and consequently causes membrane lipid peroxidation, among other challenges. The present study aimed to evaluate the in vitro effects of glutathione (control, 1. 0, 1. 5, and 2. 5 mM) on equine semen in a refrigeration protocol of 16ºC for 36 hours. The following variables were evaluated after 0, 12, 24, and 36 hours refrigeration: total sperm motility, vigor, viability, and plasma and acrosomal membrane integrity. Motility was higher with 2. 5mM of glutathione (57. 8 ± 7. 3) after 12 hours of refrigeration compared to the control (53. 2 ± 8. 3) (P < 0. 05). After 36 hours of refrigeration, motility was higher with 1. 5 mM (43. 4 ± 12. 7) and 2. 5mM glutathione (45. 5 ± 6. 2), than it was with 1mM glutathione (38. 2 ± 9) and the control (35. 5 ± 18. 4) (P < 0. 05), respectively. Vigor was highest with 1. 5mM glutathione (3. 7 ± 0. 3) after 36 hours compared to the control (3. 2 ± 1. 1), (P < 0. 05). Viability differed between control and 1mM treatments (79. 5 ± 1. 8) only after 24 hours (75. 5 ± 9. 7) (P < 0. 05). Throughout the investigation, no significant differences were noted in plasma and acrosomal membrane integrity (P > 0. 05). The 1. 5 and 2. 5mM glutathione levels were more efficient in protecting sperm cells and yielded higher total motility values after 36 hours of refrigeration.

scholarly journals Testicular Morphology and Sperm Motility in Cultured African Catfish (Clarias gariepinus) at Different Stages of Development

2016 ◽  
Vol 8 (3) ◽  
pp. 281-285 ◽  
Author(s):  
Chidozie Nwabuisi OKOYE ◽  
Udensi Maduabuchi IGWEBUIKE ◽  
Anietie Francis UDOUMOH ◽  
Chinadindu Tochukwu OKEREKE
Keyword(s):  
Sperm Motility ◽  
Clarias Gariepinus ◽  
Body Cavity ◽  
The Body ◽  
Sperm Cells ◽  
African Catfish ◽  
Testicular Weight ◽  
Testicular Morphology ◽  
The Mean ◽  
Somatic Index

Testicular morphology and sperm motility were evaluated in cultured Clarias gariepinus (n = 25) purposively assigned to five groups according to their age. The results showed that the testes were paired, elongated, dorso-ventrally flattened structures, situated in the caudal aspects of the body cavity. The mean length of both right and left testes increased linearly with age, being significantly (p < 0.05) higher at 6 months than at 4 and 5 months of age, and also significantly (p < 0.05) higher at 8 months than at 6 months of age, while the mean weight and organo-somatic index of the catfish testes increased linearly until 6 months of age, after which no significant (p > 0.05) increase in the testicular weight and organo-somatic index was observed. Unidirectional progressive movement of spermatozoa was detected in the milt of C. gariepinus at 6, 7 and 8 months of age, but sperm cells were non-motile at 4 and 5 months of age. Histological sections showed seminiferous lobules, whose germinal epithelia were characterized by many cysts enclosing clones of sperm cells. Each cyst enclosed a clone of sperm cells at an identical stage of spermatogenesis. Spermatids and spermatozoa were present in the lumen of the seminiferous lobule. The obtained results indicate that the morphology of the testes of C. gariepinus is similar to the testes of members of the order Siluriformes, but sexual maturity and production of motile spermatozoa may be achieved at 6 months of age in the African catfish.

scholarly journals Melatonin Effect on Cryopreserved Sperm Cells of Crioulo Stallions

2020 ◽  
Vol 5 (2) ◽  
pp. 1-8
Author(s):  
Eraldo L Zanella
Keyword(s):  
Plasma Membrane ◽  
Sperm Motility ◽  
Membrane Integrity ◽  
Male Gamete ◽  
The Body ◽  
Cellular Damage ◽  
Ros Generation ◽  
Sperm Cells ◽  
Beneficial Effects ◽  
Endogenous Antioxidant

The freezing/thawing process of spermatozoa can cause cellular damage to the male gamete, decreasing the fertilization potential due to the increase in the production of reactive oxygen species (ROS). Melatonin is a potent endogenous antioxidant that protects the body against the damage caused by ROS. This study has evaluated different melatonin concentrations on the sperm viability of cryopreserved semen of Crioulo stallions. For that, three ejaculates were collected from five stallions diluted in a commercial extender followed by centrifugation and resuspension in a commercial freezing extender supplemented with 0; 1.25; 2.5. 5mM of Melatonin before the cryopreservation process. After thawing, the evaluation was performed assessing motility and flow cytometry evaluations: the plasma membrane integrity (PI), the integrity of the acrosomal membrane (FITC-PNA), mitochondrial membrane potential (JC1), and ROS generation (DCF-DA). Our results showed that sperm motility in the group without Melatonin and the 1.25mM group did not show the difference; however, the groups 2.5mM and 5mM presented a reduction in sperm motility. The 1.25 mM concentration was able to protect the plasma membrane during the cryopreservation process, in addition to showing a significant reduction in the production of ROS and increasing the percentage of sperm with integral acrosome. It can also be seen that high concentrations of Melatonin did not show beneficial effects. In conclusion, the addition of 1.25 mM of the Melatonin in Crioulo sperm cells showed to have a protective effect on the sperm cell during cryopreservation.

scholarly journals Expression and function of ras proto-oncogene proteins in human sperm cells

1992 ◽  
Vol 102 (3) ◽  
pp. 487-494 ◽  
Author(s):  
R.K. Naz ◽  
K. Ahmad ◽  
P. Kaplan
Keyword(s):  
Sperm Cell ◽  
Acrosome Reaction ◽  
Cell Function ◽  
Beat Frequency ◽  
Human Sperm ◽  
Sperm Cells ◽  
Ras Protein ◽  
Head Displacement ◽  
Sperm Penetration ◽  
And Function

The presence and role of c-ras proteins were investigated in mature human sperm cells. The v-H-ras monoclonal antibody (mAb) against the c-ras protein, p21, reacted specifically with the acrosomal region of methanol-fixed as well as unfixed-live capacitated and non-capacitated human sperm cell in the indirect immunofluorescence technique. The v-H-ras mAb predominantly recognized c-ras protein of 21 kDa on the Western blot of lithium diiodosalicylate (LIS)-solubilized human sperm preparation. The incubation of sperm cells with v-H-ras mAb affected the sperm cell function in the human sperm penetration assay. The antibody significantly reduced the acrosome reaction and release of acrosin activity from the sperm cells. There was no effect of the mAb on percentage motility, although the mAb significantly affected various motility characteristics such as linearity, amplitude of lateral head displacement (ALH) and beat frequency, the motility parameters involved in the hyperactivation phenomenon of sperm cells leading to capacitation and acrosome reaction. These results suggest that the c-ras or c-ras-like proteins are present in mature sperm cell and may have a role in capacitation and/or acrosome reaction of human sperm cell.

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.

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