scholarly journals Species difference in the expression of Fas and Fas ligand in mature mammalian spermatozoa

2017 ◽  
Vol 62 (No. 12) ◽  
pp. 519-526
Author(s):  
Y. Li ◽  
M. Sun ◽  
J. Zhu ◽  
G. Jiao ◽  
J. Lin ◽  
...  
Keyword(s):  
Fas Ligand ◽  
Species Difference ◽  
Female Genital Tract ◽  
Human Spermatozoa ◽  
Whole Body ◽  
Fasl Expression ◽  
Weak Signals ◽  
Boar Spermatozoa ◽  
Mature Spermatozoa ◽  
Mammalian Spermatozoa

Although it has been proposed that the Fas and Fas ligand (FasL) may protect ejaculated spermatozoa against apoptosis induced by lipoperoxidative damage and against lymphocytes present in the female genital tract, studies reported conflicting results on the presence of Fas receptors in ejaculated human spermatozoa. Furthermore, the expression of Fas/FasL on mature spermatozoa has not been observed in several important mammals. Using seven species, we observed the possibility for species difference in Fas/FasL expression on mature spermatozoa by both immunofluorescence microscopy and western blot analysis. Whereas intensive signals of Fas immunolabelling were detected in sperm head and middle piece and weak signals observed in the tail in 86–100% of the mouse, rat, bull, ram, and buck spermatozoa, only weak signals were detected on the whole body of 27% boar spermatozoa and in the head of 21% human spermatozoa. The pattern of FasL localization was identical to that of Fas in spermatozoa from human, mouse, rat, ram, and buck, but boar and bull spermatozoa showed weak and intensive FasL signals, respectively, only in the head. Western blotting further confirmed the Fas and FasL expression in mouse, rat, bull, ram, and buck, but not in human and boar spermatozoa. Taken together, the results revealed a marked species difference in Fas/FasL expression and an extensive co-expression of Fas and FasL among mature mammalian spermatozoa, suggesting that whereas spermatozoa from most species may be protected by Fas/FasL, those from human and boar may not use the Fas system for protection.

scholarly journals The occurrence of polyenoic fatty acids with greater than 22 carbon atoms in mammalian spermatozoa

1986 ◽  
Vol 240 (3) ◽  
pp. 891-895 ◽  
Author(s):  
A Poulos ◽  
P Sharp ◽  
D Johnson ◽  
I White ◽  
A Fellenberg
Keyword(s):  
Fatty Acids ◽  
Fatty Acid Composition ◽  
Fatty Acid ◽  
Unsaturated Fatty Acids ◽  
Carbon Chain ◽  
Human Spermatozoa ◽  
Polyenoic Fatty Acid ◽  
Chain Lengths ◽  
Boar Spermatozoa ◽  
Mammalian Spermatozoa

Fatty acids with carbon chain lengths greater than 22 (VLCFA) have been detected in boar, ram, bull and human spermatozoa. Saturated and mono-unsaturated fatty acids were present in all spermatozoa but, except for human spermatozoa, polyenoic fatty acids were quantitatively the most important components. Marked differences in polyenoic fatty acid composition were observed. Whereas human spermatozoa contain predominantly di-, tri- and tetraenoic fatty acids with up to 32 carbon atoms, boar, ram and bull spermatozoa also contain pentaenoic and/or hexaenoic acids with up to 34 carbon atoms. Human and boar spermatozoa differ markedly from those of the ram and bull in that only n-6 series acids are present.

The Fine Structure of Glycocalyx in Human Spermatozoa. A High Resolution Cytochemical Study

1973 ◽  
Vol 31 ◽  
pp. 640-641
Author(s):  
P. Hernández-Jáuregui ◽  
A. Sosa ◽  
A. González Angulo
Keyword(s):  
Negative Charge ◽  
Iron Hydroxide ◽  
Human Spermatozoa ◽  
Surface Coat ◽  
Cell Surfaces ◽  
Colloidal Iron ◽  
Cytochemical Study ◽  
Specific Permeability ◽  
Extracellular Glycoprotein ◽  
Mammalian Spermatozoa

Glycocalyx is the name given by Bennett to the extracellular glycoprotein coat present in some cell surfaces. It appears to play an important role in cell properties such as antigenicity, cell adhesivity, specific permeability, and ATP ase activity. In the sperm this coat can be directly related to such important phenomena as capacitation and fertilization. The presence of glycocalyx in invertebrate spermatozoa has already been demonstrated. Recently Yanagimachi et al. has determined the negative charges on sperm surfaces of mammalian spermatozoa including man, using colloidal iron hydroxide. No mention was made however of the outer surface coat as composed of substances other than those confering a negative charge. The purpose of this work was therefore to determine the presence of a glycocalyx in human spermatozoa using alcian blue and lanthanum staining.

Glyceraldehyde 3-phosphate dehydrogenase is bound to the fibrous sheath of mammalian spermatozoa

1997 ◽  
Vol 110 (15) ◽  
pp. 1821-1829 ◽  
Author(s):  
D. Westhoff ◽  
G. Kamp
Keyword(s):  
Glycolytic Enzyme ◽  
Sperm Maturation ◽  
Short Term ◽  
Fibrous Sheath ◽  
Typical Structure ◽  
Immunogold Staining ◽  
Atp Production ◽  
Principal Piece ◽  
Boar Spermatozoa ◽  
Mammalian Spermatozoa

Evidence is provided that the glycolytic enzyme glyceraldehyde 3-phosphate dehydrogenase is covalently linked to the fibrous sheath. The fibrous sheath is a typical structure of mammalian spermatozoa surrounding the axoneme in the principal piece of the flagellum. More than 90% of boar sperm glyceraldehyde 3-phosphate dehydrogenase activity is sedimented after cell disintegration by centrifugation. Detergents, different salt concentrations or short term incubation with chymotrypsin do not solubilize the enzyme, whereas digestion with trypsin or elastase does. Short term incubation with trypsin (15 minutes) even resulted in an activation of glyceraldehyde 3-phosphate dehydrogenase. Purification on phenyl-Sepharose yielded a homogeneous glyceraldehyde 3-phosphate dehydrogenase as judged from gel electrophoresis SDS-PAGE and native gradient PAGE. The molecular masses are 41.5 and 238 kDa, respectively, suggesting native glyceraldehyde 3-phosphate dehydrogenase to be a hexamer. Rabbit polyclonal antibodies raised to purified glyceraldehyde 3-phosphate dehydrogenase show a high specificity for mammalian spermatozoal glyceraldehyde 3-phosphate dehydrogenase, while other proteins of boar spermatozoa or the muscle glyceraldehyde 3-phosphate dehydrogenase are not labelled. Immunogold staining performed in a post-embedding procedure reveals the localization of glyceraldehyde 3-phosphate dehydrogenase along the fibrous sheath in spermatozoa of boar, bull, rat, stallion and man. Other structures such as the cell membrane, dense fibres, the axoneme or the mitochondria are free of label. During the process of sperm maturation, most of the cytoplasm of the sperm midpiece is removed as droplets during the passage through the epididymis. The labelling of this cytoplasm, in immature boar spermatozoa and in the droplets, indicates that glyceraldehyde 3-phosphate dehydrogenase is completely removed from the midpiece during sperm maturation in the epididymis. The inverse compartmentation of the glycolytic enzyme and mitochondria in the mammalian sperm flagella suggests that ATP-production in the principal piece mainly occurs by glycolysis and in the midpiece by respiration.

scholarly journals Does the Pre-Ovulatory Pig Oviduct Rule Sperm Capacitation In Vivo Mediating Transcriptomics of Catsper Channels?

2020 ◽  
Vol 21 (5) ◽  
pp. 1840 ◽  
Author(s):  
Cristina A. Martinez ◽  
Manuel Alvarez-Rodriguez ◽  
Dominic Wright ◽  
Heriberto Rodriguez-Martinez
Keyword(s):  
Ex Vivo ◽  
Female Genital Tract ◽  
Thermo Fisher Scientific ◽  
Positive Regulators ◽  
Porcine Gene ◽  
Single Fertilization ◽  
Boar Spermatozoa ◽  
Go Terms ◽  
Fisher Scientific

Spermatozoa need to conduct a series of biochemical changes termed capacitation in order to fertilize. In vivo, capacitation is sequentially achieved during sperm transport and interaction with the female genital tract, by mechanisms yet undisclosed in detail. However, when boar spermatozoa are stored in the tubal reservoir pre-ovulation, most appear to be in a non-capacitated state. This study aimed at deciphering the transcriptomics of capacitation-related genes in the pig pre-ovulatory oviduct, following the entry of semen or of sperm-free seminal plasma (SP). Ex-vivo samples of the utero-tubal junction (UTJ) and isthmus were examined with a microarray chip (GeneChip® Porcine Gene 1.0 ST Array, Thermo Fisher Scientific) followed by bioinformatics for enriched analysis of functional categories (GO terms) and restrictive statistics. The results confirmed that entry of semen or of relative amounts of sperm-free SP modifies gene expression of these segments, pre-ovulation. It further shows that enriched genes are differentially associated with pathways relating to sperm motility, acrosome reaction, single fertilization, and the regulation of signal transduction GO terms. In particular, the pre-ovulation oviduct stimulates the Catsper channels for sperm Ca2+ influx, with AKAPs, CATSPERs, and CABYR genes being positive regulators while PKIs and CRISP1 genes appear to be inhibitors of the process. We postulate that the stimulation of PKIs and CRISP1 genes in the pre-ovulation sperm reservoir/adjacent isthmus, mediated by SP, act to prevent premature massive capacitation prior to ovulation.

scholarly journals Interaction of fas and fas ligand in a rat 36b10 glioma model

2000 ◽  
Vol 8 (4) ◽  
pp. 1-6
Author(s):  
Timothy Ryken ◽  
Bruce Frankel ◽  
Sharon Longo ◽  
Zita Sibenaller
Keyword(s):  
Malignant Glioma ◽  
Cell Line ◽  
Fas Ligand ◽  
Fibroblast Cell ◽  
Fasl Expression ◽  
Rat Glioma ◽  
Significant Toxicity ◽  
Cytotoxicity Studies ◽  
Target Cell Line ◽  
Carrier Cell

Object An experimental model of the fas and fas ligand (fasL) interaction in malignant glioma was developed. Methods Using plasmid-based delivery, 36B10 rat glioma cells were modified to express fas (36B10-fas), and a delivery fibroblast cell line was modified to produce fasL, resulting in the FR-fasL cell line. Evaluation of fas expression was performed with flow cytometry and expression of fasL confirmed by Western blot analysis. Once the cell lines were created and partially characterized, fas-induced cytotoxicity was evaluated using an antibody-mediated assay for 36B10-fas that demonstrated significant toxicity at 24 and 48 hours. To evaluate the potential for activating the fas molecule by using cell-mediated delivery, coculture cytotoxicity studies were performed with a target cell line (36B10-fas) and effector cell line (FR-fasL). Using a series of culture ratios, increasing cytotoxicity was noted, suggesting that activation of the transfected fas receptor by fasL expression on the carrier cell was occurring. Conclusion Based on their experiments, the authors describe a model for evaluating the interaction of fas and fasL in a cellular model of malignant glioma.

Aquaporins in boar spermatozoa. Part II: detection and localisation of aquaglyceroporin 3

2017 ◽  
Vol 29 (4) ◽  
pp. 703 ◽  
Author(s):  
Noelia Prieto-Martínez ◽  
Roser Morató ◽  
Ingrid Vilagran ◽  
Joan E. Rodríguez-Gil ◽  
Sergi Bonet ◽  
...  
Keyword(s):  
Individual Differences ◽  
Western Blot ◽  
Distribution Pattern ◽  
Staining Pattern ◽  
Sperm Quality ◽  
Boar Spermatozoa ◽  
Aquaporin Family ◽  
Water And Solute Transport ◽  
Signal Band ◽  
Mammalian Spermatozoa

The proteins belonging to the aquaporin family play a fundamental role in water and solute transport across biological membranes. While the presence of these proteins has been extensively studied in somatic cells, their function in mammalian spermatozoa has been studied less. The present study was designed to identify and localise aquaglyceroporin 3 (AQP3) in boar spermatozoa. With this purpose, 29 fresh ejaculates from post-pubertal Piétrain boars were classified into two groups based upon their sperm quality and subsequently evaluated through western blot and immunofluorescence assessments. Western blotting showed the specific signal band of AQP3 at 25 kDa, whereas immunofluorescence assessments allowed us to identify two different AQP3 localisation patterns: (1) spermatozoa presenting a clear labelling located only in the mid-piece and (2) spermatozoa exhibiting a distribution pattern in the head and along the entire tail. The first staining pattern was predominant in all studied ejaculates. Despite individual differences in AQP3 content and localisation between boar ejaculates, these differences were not correlated with sperm quality. In conclusion, although AQP3 is present in boar spermatozoa in two different localisation patterns, neither the AQP3 content nor its localisation have been found to be associated with conventional sperm parameters.

Unprotected freezing of human spermatozoa exerts a detrimental effect on their oocyte activating capacity and chromosome integrity

Zygote ◽  
1996 ◽  
Vol 4 (04) ◽  
pp. 263-268 ◽  
Author(s):  
Andrei V. Rybouchkin ◽  
Paul De Sutter ◽  
Marc Dhont
Keyword(s):  
Assisted Reproduction ◽  
Detrimental Effect ◽  
Chromosomal Abnormalities ◽  
Ethanol Solution ◽  
Human Spermatozoa ◽  
Physical Factors ◽  
Reproductive Characteristics ◽  
Chromosome Integrity ◽  
The Stability ◽  
Mammalian Spermatozoa

SummaryThe influence of unprotected freezing of mammalian spermatozoa on their oocyte activating capacity and chromosome integrity is unknown. However, this type of sperm treatment has been used in assisted reproduction by intracytoplasmic sperm injection in cattle and humans. The mouse oocyte injection test was used to analyse the influence of unprotected freezing of human spermatozoa on their reproductive characteristics. Mouse oocytes were microinjected with intact human spermatozoa or spermatozoa treated with two cycles of unprotected freeze-thawing. Oocytes surviving the injection were either cultured without further treatment or exposed to ethanol solution to induce parthenogenetic activation. Both injected and activated oocytes were used for sperm chromosome analysis. The results revealed a significant reduction in oocyte activating capacity and a tenfold increase in the incidence of structural chromosomal abnormalities in human spermatozoa treated by unprotected freezing. We conclude that unprotected freezing of human spermatozoa has a detrimental effect on their reproductive characteristics. Our data also provide a new perspective on the stability of mammalian spermatozoa to physical factors and demonstrate the importance of detailed analysis of the stability of sperm structures for successful development of new approaches in assisted reproduction.

scholarly journals Regulation of FAS Ligand Expression during Activation-Induced Cell Death in T Cells by p38 Mitogen-Activated Protein Kinase and C-Jun Nh2-Terminal Kinase

2000 ◽  
Vol 191 (6) ◽  
pp. 1017-1030 ◽  
Author(s):  
Jian Zhang ◽  
Jian-Xin Gao ◽  
Kostantin Salojin ◽  
Qing Shao ◽  
Marsha Grattan ◽  
...  
Keyword(s):  
T Cells ◽  
Cell Death ◽  
T Cell ◽  
Protein Kinase ◽  
P38 Mapk ◽  
Fas Ligand ◽  
Mitogen Activated Protein Kinase ◽  
Fasl Expression ◽  
Activation Induced Cell Death ◽  
Mitogen Activated Protein

Activation-induced cell death (AICD) is a mechanism of peripheral T cell tolerance that depends upon an interaction between Fas and Fas ligand (FasL). Although c-Jun NH2-terminal kinase (JNK) and p38 mitogen-activated protein kinase (MAPK) may be involved in apoptosis in various cell types, the mode of regulation of FasL expression during AICD in T cells by these two MAPKs is incompletely understood. To investigate the regulatory roles of these two MAPKs, we analyzed the kinetics of TCR-induced p38 MAPK and JNK activity and their regulation of FasL expression and AICD. We report that both JNK and p38 MAPK regulate AICD in T cells. Our data suggest a novel model of T cell AICD in which p38 MAPK acts early to initiate FasL expression and the Fas-mediated activation of caspases. Subsequently, caspases stimulate JNK to further upregulate FasL expression. Thus, p38 MAPK and downstream JNK converge to regulate FasL expression at different times after T cell receptor stimulation to elicit maximum AICD.

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