Journal articles: 'Spermatozoa Immunology'

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Schumacher, G. F. B. "Immunology of spermatozoa and cervical mucus*." Human Reproduction 3, no. 3 (April 1988): 289–300. http://dx.doi.org/10.1093/oxfordjournals.humrep.a136698.

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Ceballos, Ana, Federico Remes Lenicov, Juan Sabatté, Christian Rodríguez Rodrígues, Mercedes Cabrini, Carolina Jancic, Silvina Raiden, et al. "Spermatozoa capture HIV-1 through heparan sulfate and efficiently transmit the virus to dendritic cells." Journal of Experimental Medicine 206, no. 12 (October 26, 2009): 2717–33. http://dx.doi.org/10.1084/jem.20091579.

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Semen is the main vector for HIV-1 dissemination worldwide. It contains three major sources of infectious virus: free virions, infected leukocytes, and spermatozoa-associated virions. We focused on the interaction of HIV-1 with human spermatozoa and dendritic cells (DCs). We report that heparan sulfate is expressed in spermatozoa and plays an important role in the capture of HIV-1. Spermatozoa-attached virus is efficiently transmitted to DCs, macrophages, and T cells. Interaction of spermatozoa with DCs not only leads to the transmission of HIV-1 and the internalization of the spermatozoa but also results in the phenotypic maturation of DCs and the production of IL-10 but not IL-12p70. At low values of extracellular pH (∼6.5 pH units), similar to those found in the vaginal mucosa after sexual intercourse, the binding of HIV-1 to the spermatozoa and the consequent transmission of HIV-1 to DCs were strongly enhanced. Our observations support the notion that far from being a passive carrier, spermatozoa acting in concert with DCs might affect the early course of sexual transmission of HIV-1 infection.

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Shan, Dan, Samuel Kofi Arhin, Junzhao Zhao, Haitao Xi, Fan Zhang, Chufang Zhu, and Yangyang Hu. "Effects of SLIRP on Sperm Motility and Oxidative Stress." BioMed Research International 2020 (October 13, 2020): 1–5. http://dx.doi.org/10.1155/2020/9060356.

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Background. Deficient spermatozoon motility is one of the main causes of male infertility. However, there are still no accurate and effective treatments in a clinical setting for male asthenospermia. Exploring the genes and mechanism of asthenospermia has become one of the hot topics in reproductive medicine. Our aim is to study the effect of SLRIP on human spermatozoon motility and oxidative stress. Methods. Sperm samples were collected including a normospermia group (60 cases) and an asthenospermia group (50 cases). SLIRP protein expression in spermatozoa was examined by western blotting, and relative mRNA expression of SLIRP in spermatozoa was quantified by reverse transcription polymerase chain reaction. Levels of reactive oxygen species (ROS), adenosine triphosphate (ATP) content, and the activity of manganese superoxide dismutase (MnSOD) in spermatozoa were also measured. Results. The mRNA level and protein expression of SLIRP in the asthenospermia group were significantly reduced compared with those in the normospermia group. The ROS active oxygen level in the asthenospermia group significantly increased; however, the ATP content decreased significantly as well as the activity of MnSOD. Conclusion. SLIRP regulates human male fertility, and SLIRP and sperm progressive motility are positively correlated. The expression of SLIRP is declined, oxidative damage is increased, and energy metabolism is decreased in spermatozoa of asthenospermia patients compared to normospermia participants.

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Malm, Johan, Ole Sørensen, Terese Persson, Margareta Frohm-Nilsson, Bengt Johansson, Anders Bjartell, Hans Lilja, Mona Ståhle-Bäckdahl, Niels Borregaard, and Arne Egesten. "The Human Cationic Antimicrobial Protein (hCAP-18) Is Expressed in the Epithelium of Human Epididymis, Is Present in Seminal Plasma at High Concentrations, and Is Attached to Spermatozoa." Infection and Immunity 68, no. 7 (July 1, 2000): 4297–302. http://dx.doi.org/10.1128/iai.68.7.4297-4302.2000.

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ABSTRACT Innate immunity is important for the integrity of the host against potentially invasive pathogenic microorganisms in the environment. Antibiotic peptides with broad antimicrobial activity are part of the innate immune system. We investigated the presence of the cathelicidin, human cationic antimicrobial protein (hCAP-18), in the male reproductive system. We found strong expression of the hCAP-18 gene by in situ hybridization and hCAP-18 protein, as detected by immunohistochemistry, in the epithelium of the epididymis, but not in the testis. The highest expression in the epididymis was in the caudal part. Western blotting showed a doublet band, the upper part corresponding to the size of hCAP-18 in plasma and neutrophils. Using a specific enzyme-linked immunosorbent assay (ELISA), levels of 86.5 ± 37.8 μg/ml (mean ± standard deviation; range, 41.8 to 142.8 μg/ml; n = 10) were detected in seminal plasma from healthy donors, which is 70-fold higher than the level in blood plasma. Flow cytometry and immunocytochemistry revealed the presence of hCAP-18 on spermatozoa. ELISA measurement showed levels of 196 ng/106 spermatozoa, corresponding to 6.6 × 106 molecules of hCAP-18 per spermatozoon. Our results suggest a key role for hCAP-18 in the antibacterial integrity of the male reproductive system. The attachment of hCAP-18 to spermatozoa may implicate a role for hCAP-18 in conception.

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Friberg, J., N. Gleicher, M. Suarez, and E. Confino. "Chlamydia Attached to Spermatozoa." Journal of Infectious Diseases 152, no. 4 (October 1, 1985): 854. http://dx.doi.org/10.1093/infdis/152.4.854.

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Dussaix, E., D. Guetard, C. Dauguet, M. D'Almeida, J. Auer, A. Ellrodt, L. Montagnier, and M. Auroux. "Spermatozoa as potential carriers of HIV." Research in Virology 144 (January 1993): 487–95. http://dx.doi.org/10.1016/s0923-2516(06)80064-6.

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MEINERTZ, HELLE, LARS LINNET, HANS WOLF, and TAGE HJORT. "Antisperm Antibodies on Epididymal Spermatozoa." American Journal of Reproductive Immunology 25, no. 4 (May 1991): 158–62. http://dx.doi.org/10.1111/j.1600-0897.1991.tb01087.x.

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Witkin, Steven S. "Immunoregulatory properties of human spermatozoa." Journal of Reproductive Immunology 15 (July 1989): 164. http://dx.doi.org/10.1016/0165-0378(89)90330-6.

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Gorga, Fernanda, Marilena Galdiero, Elisabetta Buommino, and Emilia Galdiero. "Porins and Lipopolysaccharide Induce Apoptosis in Human Spermatozoa." Clinical Diagnostic Laboratory Immunology 8, no. 1 (January 1, 2001): 206–8. http://dx.doi.org/10.1128/cdli.8.1.206-208.2001.

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ABSTRACT Treatment of human spermatozoa with porins or lipopolysaccharide (LPS) increases spontaneous apoptosis in these cells. Porins and LPS were extracted from Salmonella enterica serovar Typhimurium and Pasteurella multocida and were mixed with human spermatozoa for detection of levels of apoptosis.

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Baldi, Elisabetta, Michaela Luconi, Lorella Bonaccorsi, and Gianni Forti. "Signal transduction pathways in human spermatozoa." Journal of Reproductive Immunology 53, no. 1-2 (January 2002): 121–31. http://dx.doi.org/10.1016/s0165-0378(01)00089-4.

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Rodriguez-Cordoba, S., J. R. Regueiro, and A. Arnaiz-Villena. "HLA-D determinants are expressed on human seminal cells other than spermatozoa but not on purified spermatozoa." Journal of Reproductive Immunology 18, no. 3 (October 1990): 237–45. http://dx.doi.org/10.1016/0165-0378(90)90046-9.

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Johnson, Peter M., Leanne E. Clift, Brian F. Flanagan, Pavel Stopka, and Katerina Dvorakova. "The roles of CD46 on mammalian spermatozoa." Molecular Immunology 44, no. 1-3 (January 2007): 190. http://dx.doi.org/10.1016/j.molimm.2006.07.103.

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Kamada, Shusaku, Sergio Oehninger, Mary C. Mahony, Peter F. Blackmore, Susan E. Lanzendorf, and Gary D. Hodgen. "Does Endothelin-1 Affect Human Spermatozoa Function?" American Journal of Reproductive Immunology 31, no. 2-3 (March 4, 1994): 91–98. http://dx.doi.org/10.1111/j.1600-0897.1994.tb00852.x.

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Rooney, I. A., J. P. Atkinson, E. S. Krul, G. Schonfeld, K. Polakoski, J. E. Saffitz, and B. P. Morgan. "Physiologic relevance of the membrane attack complex inhibitory protein CD59 in human seminal plasma: CD59 is present on extracellular organelles (prostasomes), binds cell membranes, and inhibits complement-mediated lysis." Journal of Experimental Medicine 177, no. 5 (May 1, 1993): 1409–20. http://dx.doi.org/10.1084/jem.177.5.1409.

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We demonstrate here that CD59, an inhibitor of the membrane attack complex (MAC) of the complement system, is present in cell-free seminal plasma (SP) at a concentration of at least 20 micrograms/ml. Analyses by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, Western blotting, and Edman degradation indicated that this protein, SP CD59, was similar, if not identical, to CD59 isolated from erythrocyte (E) membranes (E CD59). Like purified E CD59, SP CD59 also possesses a glycosyl phosphatidyl inositol (GPI) anchor and incorporates into the membranes of heterologous cells where it inhibits lysis by the human MAC. This phenomenon could be demonstrated not only if cells were incubated with purified SP CD59 but also if unfractionated SP were used. Further, CD59 in unfractionated SP bound to washed spermatozoa, increasing their membrane content of the protein. The mechanism by which this protein retains its GPI anchor while apparently present in the fluid phase is of interest and was further investigated. Using the techniques of high-speed centrifugation, fast performance liquid chromatography fractionation, and electron microscopy, we found that all detectable SP CD59 was associated with vesicular extracellular organelles. These organelles, named "prostasomes," were previously known to be present in SP and to interact with spermatozoa, although their function was uncertain. Interaction of heterologous E with prostasomes rendered the cells more resistant to lysis by human MACs. We propose that these organelles represent a pool of CD59 from which protein lost from spermatozoa, perhaps as a result of low level complement attack or of normal membrane turnover, can be replenished.

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Jankovičová, Jana, Zdeňka Neuerová, Petra Sečová, Michaela Bartóková, Filipa Bubeníčková, Kateřina Komrsková, Pavla Postlerová, and Jana Antalíková. "Tetraspanins in mammalian reproduction: spermatozoa, oocytes and embryos." Medical Microbiology and Immunology 209, no. 4 (May 18, 2020): 407–25. http://dx.doi.org/10.1007/s00430-020-00676-0.

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Martin, P. M. V., G. Gresenguet, V. M. Herve, G. Renom, G. Steenman, and A. J. Georges. "Decreased number of spermatozoa in HIV-1-infected individuals." AIDS 6, no. 1 (January 1992): 130. http://dx.doi.org/10.1097/00002030-199201000-00021.

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17

Wang, Mengying, Evgenia Isachenko, Plamen Todorov, Gohar Rahimi, Peter Mallmann, Igor I. Katkov, and Vladimir Isachenko. "Aseptic Technology for Cryoprotectant-Free Vitrification of Human Spermatozoa by Direct Dropping into Clean Liquid Air: Apoptosis, Necrosis, Motility, and Viability." BioMed Research International 2020 (January 25, 2020): 1–7. http://dx.doi.org/10.1155/2020/2934315.

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This study aimed to compare the quality of human spermatozoa vitrified by direct plunging into liquid nitrogen vs. liquid air. Spermatozoa were divided into three groups: fresh spermatozoa (Group F) were used as a control. Spermatozoa suspension (20 μl) was vitrified in open granules by direct dropping into liquid nitrogen (Group LN) or clean liquid air (Group LA). After warming at 37°C, the progressive motility rate of Group F was reduced from 65.9 ± 2.5% to 34.0 ± 1.9% (Group LN) and 38.1 ± 2.3% (Group LA), respectively (P1-2,3 < 0.05). The reductions in viability were 65.6 ± 2.2%, 29.0 ± 1.8%, and 36.6 ± 2.6% for Groups F, LN, and LA, respectively (P1-2,3 < 0.05). Comparing spermatozoa vitrified in liquid nitrogen vs. liquid air, no significant differences were detected in motility (34.0 ± 1.9% vs. 38.1 ± 2.3%), viability (29.0 ± 1.8% vs. 36.6 ± 2.6%), early apoptosis (13.8 ± 1.5% vs. 14.3 ± 1.8%), late apoptosis (45.5 ± 1.8% vs. 43.7 ± 2.2%), and necrosis (19.5 ± 2.0% vs. 15.0 ± 1.8%; p>0.01 for all respective differences). There was a statistical tendency for increasing rates of “progressive motility” and “viability” and decreasing rates of “apoptosis” and “necrosis” when comparing spermatozoa vitrified in liquid air vs. liquid nitrogen. It is concluded that cryoprotectant-free vitrification by the direct dropping of human spermatozoa in a clean cooling agent (liquid air) is a good alternative to the use of nonsterile liquid nitrogen and can be used to cool cells while minimising the risk of microbial contamination.

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Paterson, Margaret, Diana Harkiss, and R. John Aitken. "Identification of ZP binding sites on human spermatozoa." Journal of Reproductive Immunology 34, no. 1 (August 1997): 25–26. http://dx.doi.org/10.1016/s0165-0378(97)90392-2.

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Bronson, Richard, Susan Bronson, Lucila Oula, Weibing Zhang, and Berhane Ghebrehiwet. "Detection of complement C1q receptors on human spermatozoa." Journal of Reproductive Immunology 38, no. 1 (April 1998): 1–14. http://dx.doi.org/10.1016/s0165-0378(98)00006-0.

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Yeung, William S. B., Kai-Fai Lee, Riitta Koistinen, Hannu Koistinen, Markku Seppälä, and Philip C. N. Chiu. "Effects of glycodelins on functional competence of spermatozoa." Journal of Reproductive Immunology 83, no. 1-2 (December 2009): 26–30. http://dx.doi.org/10.1016/j.jri.2009.04.012.

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Bandivdekar, Atmaram H., Shilpa M. Velhal, and Vijaya P. Raghavan. "Identification of CD4-independent HIV Receptors on Spermatozoa." American Journal of Reproductive Immunology 50, no. 4 (September 9, 2003): 322–27. http://dx.doi.org/10.1034/j.1600-0897.2003.00096.x.

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Prabha, Vijay, Tanushree Gupta, Siftjit Kaur, Navchetan Kaur, Sushila Kala, and Arvind Singh. "Isolation of a spermatozoal immobilization factor from Staphylococcus aureus filtrates." Canadian Journal of Microbiology 55, no. 7 (July 2009): 874–78. http://dx.doi.org/10.1139/w09-032.

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Staphylococcus aureus isolated from the cervix of an infertile woman was found to cause complete immobilization of human spermatozoa in vitro. Only the cell culture and cell-free supernatant showed immobilization activity, indicating that the sperm immobilization factor might be released extracellularly by the organism because no activity was observed with the washed cells. Heat treatment of the supernatant at 60 °C for 10 min waived its immobilizing activity, indicating that the active component may be a protein. The bioactive molecule from the supernatant was purified to homogeneity by ammonium sulfate precipitation, gel permeation chromatography, and ion exchange chromatography. Sperm immobilization factor (SIF) was found to be an ~20 kDa protein. SIF at a concentration of 10 µg/mL was required to cause 100% immobilization of human spermatozoa after 30 min of incubation at 37 °C, whereas a concentration of 150 µg/mL caused immediate immobilization, and a concentration of 200 µg/mL resulted in instant loss of viability of human spermatozoa, observed by eosin–nigrosin staining. Scanning electron microscopy showed that the treatment of human spermatozoa with SIF caused multiple defects in the head, midpiece, neck, and tail region of human spermatozoa.

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Sansone, Giovanni, Matilde Martino, and Paolo Abrescia. "Binding of free and protein-associated zinc to rat spermatozoa." Comparative Biochemistry and Physiology Part C: Comparative Pharmacology 99, no. 1-2 (January 1991): 113–17. http://dx.doi.org/10.1016/0742-8413(91)90085-8.

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Rennemeier, Claudia, Torsten Frambach, Florian Hennicke, Johannes Dietl, and Peter Staib. "Microbial Quorum-Sensing Molecules Induce Acrosome Loss and Cell Death in Human Spermatozoa." Infection and Immunity 77, no. 11 (August 17, 2009): 4990–97. http://dx.doi.org/10.1128/iai.00586-09.

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ABSTRACT Infertility in men and women is frequently associated with genital contamination by various commensal or uropathogenic microbes. Since many microorganisms are known to release quorum-sensing signals in substantial amounts, we raised the question whether such molecules can directly affect human spermatozoa. Here we show that farnesol and 3-oxododecanoyl-l-homoserine lactone, employed by the opportunistic pathogenic yeast Candida albicans and the gram-negative bacterium Pseudomonas aeruginosa, respectively, induce multiple damage in spermatozoa. A reduction in the motility of spermatozoa coincided in a dose-dependent manner with apoptosis and necrosis at concentrations which were nondeleterious for dendritic cell-like immune cells. Moreover, sublethal doses of both signaling molecules induced premature loss of the acrosome, a cap-like structure of the sperm head which is essential for fertilization. Addressing their mechanism of action, we found that the bacterial molecule, but not the fungal molecule, actively induced the acrosome reaction via a calcium-dependent mechanism. This work uncovers a new facet in the interaction of microorganisms with human gametes and suggests a putative link between microbial communication systems and host infertility.

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Rahman, Md Saidur, Woo-Sung Kwon, and Myung-Geol Pang. "Calcium Influx and Male Fertility in the Context of the Sperm Proteome: An Update." BioMed Research International 2014 (2014): 1–13. http://dx.doi.org/10.1155/2014/841615.

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Freshly ejaculated spermatozoa are incapable or poorly capable of fertilizing an oocyte. The fertilization aptness of spermatozoa depends on the appropriate and time-dependent acquisition of hyperactivation, chemotaxis, capacitation, and the acrosome reaction, where calcium (Ca2+) is extensively involved in almost every step. A literature review showed that several ion channel proteins are likely responsible for regulation of the Ca2+uptake in spermatozoa. Therefore, manipulation of the functions of channel proteins is closely related to Ca2+influx, ultimately affecting male fertility. Recently, it has been shown that, together with different physiological stimuli, protein-protein interaction also modifies the Ca2+influx mechanism in spermatozoa. Modern proteomic analyses have identified several sperm proteins, and, therefore, these findings might provide further insight into understanding the Ca2+influx, protein functions, and regulation of fertility. The objective of this review was to synthesize the published findings on the Ca2+influx mechanism in mammalian spermatozoa and its implications for the regulation of male fertility in the context of sperm proteins. Finally, Pathway Studio (9.0) was used to catalog the sperm proteins that regulate the Ca2+influx signaling by using the information available from the PubMed database following a MedScan Reader (5.0) search.

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Shahbaaz, Mohd, Awad Saeed Al-Samghan, Arshi Malik, Sarah Afaq, Afaf S. Alwabli, Irfan Ahmad, Mostafa A. Hussien, et al. "Functional and Structural Analysis of Predicted Proteins Obtained from Homo sapiens’ Minisatellite 33.15-Tagged Transcript pAKT-45 Variants." BioMed Research International 2020 (May 27, 2020): 1–9. http://dx.doi.org/10.1155/2020/2562950.

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The spermatozoa are transcriptionally dormant entities which have been recognized to be an archive of mRNA, coding for a variety of functionally crucial cellular proteins. This significant repository of mRNA is predicted to be associated with early embryogenesis and postfertilization. The mRNA transcripts which are tagged with minisatellites have been involved in the regulation of the gene functions as well as their organization. However, very little information is available regarding the expression of the transcripts tagged with minisatellites in spermatozoa. Therefore, in order to understand the functions and the conformational behavior of the proteins expressed from these minisatellite-tagged transcripts, we have performed a detailed in silico analysis using the sequences of the transcripts. The protein predicted from KF274549 showed the functionalities similar to uncharacterized C4orf26 proteins, while that obtained from KF274557 predicted to be a metallophosphoesterase. Furthermore, the structural folds in the structure of these predicted proteins were analyzed by using the homology modeling and their conformational behaviors in the explicit water conditions were analyzed by using the techniques of Molecular Dynamics (MD) simulations. This detailed analysis will facilitate the understanding of these proteins in the spermatozoon region and can be used for uncovering other attributes of the metabolic network.

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Nixon, Brett, and R. John Aitken. "The biological significance of detergent-resistant membranes in spermatozoa." Journal of Reproductive Immunology 83, no. 1-2 (December 2009): 8–13. http://dx.doi.org/10.1016/j.jri.2009.06.258.

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Almeida, Raquel das Neves, Heloisa Antoniella Braz-de-Melo, Igor de Oliveira Santos, Rafael Corrêa, Gary P. Kobinger, and Kelly Grace Magalhaes. "The Cellular Impact of the ZIKA Virus on Male Reproductive Tract Immunology and Physiology." Cells 9, no. 4 (April 18, 2020): 1006. http://dx.doi.org/10.3390/cells9041006.

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Zika virus (ZIKV) has been reported by several groups as an important virus causing pathological damage in the male reproductive tract. ZIKV can infect and persist in testicular somatic and germ cells, as well as spermatozoa, leading to cell death and testicular atrophy. ZIKV has also been detected in semen samples from ZIKV-infected patients. This has huge implications for human reproduction. Global scientific efforts are being applied to understand the mechanisms related to arboviruses persistency, pathogenesis, and host cellular response to suggest a potential target to develop robust antiviral therapeutics and vaccines. Here, we discuss the cellular modulation of the immunologic and physiologic properties of the male reproductive tract environment caused by arboviruses infection, focusing on ZIKV. We also present an overview of the current vaccine effects and therapeutic targets against ZIKV infection that may impact the testis and male fertility.

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Halim, A., K. Abbasi, and H. Festenstein. "The Expression of the HL-A Antigens on Human Spermatozoa." Tissue Antigens 4, no. 1 (October 9, 2008): 1–6. http://dx.doi.org/10.1111/j.1399-0039.1974.tb00218.x.

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Jankovičová, Jana, Zdeňka Neuerová, Petra Sečová, Michaela Bartóková, Filipa Bubeníčková, Kateřina Komrsková, Pavla Postlerová, and Jana Antalíková. "Correction to: Tetraspanins in mammalian reproduction: spermatozoa, oocytes and embryos." Medical Microbiology and Immunology 209, no. 5 (June 20, 2020): 653–55. http://dx.doi.org/10.1007/s00430-020-00686-y.

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Riedel, H. H., K. Wellnitz, and u. L. Mettler. "The influence of monoclonal antibodies against human spermatozoa on the penetration rate of human spermatozoa in the zona-pellucida-free hamster-oocyte system." Journal of Reproductive Immunology 15 (July 1989): 48. http://dx.doi.org/10.1016/0165-0378(89)90115-0.

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Sciamanna, Ilaria, Annalucia Serafino, James A. Shapiro, and Corrado Spadafora. "The active role of spermatozoa in transgenerational inheritance." Proceedings of the Royal Society B: Biological Sciences 286, no. 1909 (August 28, 2019): 20191263. http://dx.doi.org/10.1098/rspb.2019.1263.

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The active uptake of exogenous nucleic acids by spermatozoa of virtually all animal species is a well-established phenomenon whose significance has long been underappreciated. A growing body of published data demonstrates that extracellular vesicles released from mammalian somatic tissues pass an RNA-based flow of information to epididymal spermatozoa, thereby crossing the Weismann barrier. That information is delivered to oocytes at fertilization and affects the fate of the developing progeny. We propose that this essential process of epigenetic transmission depends upon the documented ability of epididymal spermatozoa to bind and internalize foreign nucleic acids in their nuclei. In other words, spermatozoa are not passive vectors of exogenous molecules but rather active participants in essential somatic communication across generations.

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Kay, D. J., and B. Boettcher. "Common Specificities of Auto- and Iso-Antibodies to Human Spermatozoa." American Journal of Reproductive Immunology and Microbiology 8, no. 1 (May 1985): 10–14. http://dx.doi.org/10.1111/j.1600-0897.1985.tb00305.x.

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Chen, Jian, Lawrence Kobilinsky, Hideo Ishizu, and Yuji Yamamoto. "A and B Antigenicity of Human Spermatozoa and Buccal Epithelial Cells." Immunological Investigations 21, no. 4 (January 1992): 343–51. http://dx.doi.org/10.3109/08820139209069374.

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Makino, Yusei, Yuuki Hiradate, Kohei Umezu, Kenshiro Hara, and Kentaro Tanemura. "Expression and Possible Role of Nicotinic Acetylcholine Receptor ε Subunit (AChRe) in Mouse Sperm." Biology 10, no. 1 (January 11, 2021): 46. http://dx.doi.org/10.3390/biology10010046.

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The nicotinic acetylcholine receptor (nAChR) is one of the receptors of acetylcholine (ACh), and nicotine (NIC) acts as an agonist of this receptor. Among the nAChR subunits, we found that the ε subunit (AChRe) had approximately 10 to 1000 times higher level of mRNA expression in mouse testes than the other subunits. In this study, we aimed to elucidate the expression and localization of AChRe in the testes and spermatozoa of mice and clarify the effect of AChRe on sperm function. Immunocytochemistry showed that AChRe was expressed in the murine testes and spermatozoa. We found that AChRe was localized only in elongated spermatids from step 12 onwards in the testes. In spermatozoa, AChRe was localized in the head, especially in the anterior region of the acrosome, but only approximately 50% of spermatozoa showed this immunoreactivity. Additionally, we analyzed the effects of ACh and NIC on sperm acrosome reaction (AR) and found that both ACh and NIC suppressed the AR rate, which was restored by an AChRe-specific antagonist. These results suggest that AChRe may be a regulator of mammalian sperm AR.

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Gable, R. J., J. R. Levinson, H. O. McDevitt, and P. N. Goodfellow. "Assay for Antibody Mediated Cytotoxicity of Mouse Spermatozoa by 86Rubidium Release." Tissue Antigens 13, no. 3 (December 11, 2008): 177–85. http://dx.doi.org/10.1111/j.1399-0039.1979.tb00781.x.

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Wu, Shengru, Wei Guo, Xinyi Li, Yanli Liu, Yulong Li, Xinyu Lei, Junhu Yao, and Xiaojun Yang. "Paternal chronic folate supplementation induced the transgenerational inheritance of acquired developmental and metabolic changes in chickens." Proceedings of the Royal Society B: Biological Sciences 286, no. 1910 (September 11, 2019): 20191653. http://dx.doi.org/10.1098/rspb.2019.1653.

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Increasing evidence indicates that paternal diet can result in metabolic changes in offspring, but the definite mechanism remains unclear in birds. Here, we fed breeder cocks five different diets containing 0, 0.25, 1.25, 2.50 and 5.00 mg kg −1 folate throughout life. Paternal folate supplementation (FS) was beneficial to the growth and organ development of broiler offspring. Most importantly, the lipid and glucose metabolism of breeder cocks and broiler offspring were affected by paternal FS, according to biochemical and metabolomic analyses. We further employed global analyses of hepatic and spermatozoal messenger RNA (mRNA), long non-coding RNA (lncRNA) and micro RNA (miRNA). Some key genes involved in the glycolysis or gluconeogenesis pathway and the PPAR signalling pathway, including PEPCK , ANGPTL4 and THRSP , were regulated by differentially expressed hepatic and spermatozoal miRNAs and lncRNAs in breeder cocks and broiler offspring. Moreover, the expression of ANGPTL4 could also be regulated by differentially expressed miRNAs and lncRNAs in spermatozoa via competitive endogenous RNA (ceRNA) mechanisms. Overall, this model suggests that paternal folate could transgenerationally regulate lipid and glucose metabolism in broiler offspring and the epigenetic transmission may involve altered spermatozoal miRNAs and lncRNAs.

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Munoz, M. G., J. Jeremias, and S. S. Witkin. "Immunology: The 60 kDa heat shock protein in human semen: relationship with antibodies to spermatozoa and Chlamydia trachomatis." Human Reproduction 11, no. 12 (December 1, 1996): 2600–2603. http://dx.doi.org/10.1093/oxfordjournals.humrep.a019177.

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Yang, X. Z., K. Kumamoto, A. Hasegawa, S. Komori, and K. Koyama. "Engulfment of spermatozoa by cumulus cells and the role of CD36." Journal of Reproductive Immunology 88, no. 1 (January 2011): 24–31. http://dx.doi.org/10.1016/j.jri.2010.09.001.

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Sundhey, R., S. P. Ahuja, and B. Singh. "Changes in membrane constituents of cauda spermatozoa of buck () during capacitation." Journal of Reproductive Immunology 15 (July 1989): 62. http://dx.doi.org/10.1016/0165-0378(89)90143-5.

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Vernazza, Pietro. "HAART improves quality of life: should we care about the quality of spermatozoa?" AIDS 22, no. 5 (March 2008): 647–48. http://dx.doi.org/10.1097/qad.0b013e3282f4de4d.

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Kaur, Kiranjeet, and Vijay Prabha. "Sperm Impairment by Sperm Agglutinating Factor Isolated fromEscherichia coli: Receptor Specific Interactions." BioMed Research International 2013 (2013): 1–9. http://dx.doi.org/10.1155/2013/548497.

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Abstract:

In an earlier work done in our laboratory, we have been able to isolate a sperm agglutinating strain ofEscherichia colifrom the semen sample of a male attending infertility clinic. Further, factor responsible for sperm agglutination (SAF) was isolated and purified, and, using SAF as a tool, corresponding SAF binding receptor from human spermatozoa has been purified. Characterization of SAF and SAF binding receptor using MALDI-TOF showed homology to glutamate decarboxylase and MHC class I molecule, respectively. Coincubation of SAF with spermatozoa not only resulted in spermagglutination but could also compromise other sperm parameters, namely, Mg2+dependent ATPase activity and apoptosis. Intravaginal administration of SAF could lead to infertility in Balb/c mice. SAF induced impairment of sperm parameters, and infertility was observed to be due to interaction of SAF with sperm surface receptor component as, when purified receptor was introduced, receptor completely inhibited all the detrimental effects induced by SAF. From these results, it could be concluded that interaction of SAF with spermatozoa is receptor mediated.

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Harding, George B., and Samuel R. Wellhausen. "Flow microfluorometric analysis of murine spermatozoa fails to detect H-2 antigens." Tissue Antigens 40, no. 5 (November 1992): 244–49. http://dx.doi.org/10.1111/j.1399-0039.1992.tb02051.x.

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Nicolini, Franck E., Françoise Huguet, Hélène Labussière-Wallet, Yann Guillermin, Madeleine Etienne, Marie-Pierre Fort, Isabelle Tigaud, et al. "CML Patients Show Sperm Alterations At Diagnosis That Are Not Improved On Tyrosine Kinase Inhibitor Treatment." Blood 120, no. 21 (November 16, 2012): 1669. http://dx.doi.org/10.1182/blood.v120.21.1669.1669.

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Abstract:

Abstract Abstract 1669 Most epidemiologic studies performed in chronic myelogenous leukemia (CML) relate that the disease occurs preferentially in males with a sex ratio of ∼1.2. In addition, CML can be diagnosed in young adults and masculine fertility is a matter of concern, particularly because tyrosine kinase inhibitors (TKI) may impact on spermatogenesis by a selective inhibition of Src kinases, PDGF-R and c-kit. Sperm cryopreservation is recommended by some authors at diagnosis in males that would expect to have children later on. In a retrospective analysis we have analysed the spermograms of 62 chronic phase (CP) and 2 onset blast crisis (BC) CML males referred to our 3 centres between 2001 and 2012, collected at diagnosis before TKI treatment, and we have compared the results obtained to those of 15 healthy volunteer donors from the cryopreservation bank database, after informed consent. In 10 patients we could collect some data for patients being on imatinib mesylate (IM). CML patients had a median age of 31 (16–48) years, significantly younger than that in the control group of healthy donors: 37 (34–45) years (p=0.001). Sokal scores were 24% high, 27% intermediate and 49% low for evaluable patients (13 patients unknown or not available). The median BCR-ABLIS value at diagnosis was 77.65%. Patients had a median duration of 26 (0–38) days of hydroxyurea prior to commencing any TKI and 65% of evaluable patients had HU before TKI. None of the patients got interferon prior to TKI. The semen cryopreservation was performed within a median of 10 (2–102) days after CML diagnosis and after a median abstinence of 5 (0.5–30) days. The median volume of semen obtained in CML patients was 2.95 (0.5–14.9) ml and 3 (1.4–5.3) ml for normal donors (p=0.3). Williams test showed 72 (0–87)% of necrospermia in patients versus 18 (4–32)% in donors (p=0.00003). The median number of spermatozoa obtained was not different in patients [46 (0.03–200) 106/ml] than that in donors [74 (19.2–253) 106/ml] (p=0.24), as well as the number of spermatozoa per ejaculate observed (p=0.49). The motility of spermatozoa at 30 minutes after collection was not different between patients (median = 47.5%) and donors (median = 50%) (p=0.12), however higher numbers of atypical spermatozoa were observed in patients [median = 77.5 (16–100)%] rather than in donors [median = 45% (22–89)%], p=0.008, and the multiple abnormalities index (MAI) was significantly higher in patients [median = 1.99 (1.14–2.7)] than that in donors [median = 1.33 (1.09–1.55)], p=0.00006. There was no correlation between age at diagnosis, Sokal index and the number of spermatozoa per ml obtained (p=0.7 and 0.21 respectively). Ten CP CML patients had spermograms after a median of 1440 (9–1456) days of IM treatment and the results obtained were compared to i) the results of each individual patient at CP diagnosis and ii) to the results of healthy comparators. In comparison to the characteristics observed at diagnosis, the semen volume (median = 3.1 ml), Williams test (median = 65%), the motility at 30 minutes (median = 37.5%) and the MAI (median = 1.71) were not different (p=ns for all), however, the numbers of spermatozoa (median = 14.9 106/ml and = 37.05 ml per ejaculate) collected on IM were significantly lower (p=0.014 and p=0.045 respectively). The different parameters evaluated on IM were compared to those of normal controls and showed significant alterations. The semen volume was not different (p=0.94), neither the motility of spermatozoa (p=0.24), but the Williams test was highly perturbed on IM [median 65 (24–79)% versus 18 (4–32)% in donors] p=0.00003, as well as the numbers of spermatozoa as 106 per ml, collected on IM [median 14.9 (0.67–179)) versus normal [74 (19.2–253)], p=0.0036 or as 106 per ejaculate collected on IM [median 37.5 (2.68–572.8)) versus normal [149 (30–535.3)], p=0.026. Atypical forms were significantly more abundant on IM [median = 80 (68–90)%] versus healthy controls [median = 45% (22–89)], p=0.0058. Finally, the MAI was severely altered on IM [median = 1.71 (1.61–1.98)] versus normal individuals [median = 1.33 (1.09–1.55)], p=0.00013. In conclusion, this work demonstrates the existence of significant sperm alterations in young males with CML at diagnosis of undetermined origin, prior to any treatment. These alterations persist on IM treatment and little is know about the impact of second generation TKI. Thus the most appropriate approach remains a matter of debate in thus setting. Disclosures: Nicolini: Novartis, Bristol Myers-Squibb, Pfizer, ARIAD, and Teva: Consultancy, Honoraria, Membership on an entity's Board of Directors or advisory committees, Research Funding. Huguet:Novartis, BMS: Speakers Bureau. Michallet:Novartis, Pfizer, Teva, Genzyme, Janssen Cilag, BMS, Merck, Pfizer, Gilead, Alexion: Consultancy, Speakers Bureau. Etienne:Novartis, Pfizer, speaker for Novartis, BMS: Consultancy.

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Mollova, M., M. Ivanova, and J. Peknicova. "Influence of monoclonal antibodies against acrosin from boar spermatozoa on gamete interactions." Journal of Reproductive Immunology 15 (July 1989): 46. http://dx.doi.org/10.1016/0165-0378(89)90111-3.

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Ishev, V. "Antigenic relationships between infections agents in the reproductive tract and human spermatozoa." Journal of Reproductive Immunology 15 (July 1989): 57. http://dx.doi.org/10.1016/0165-0378(89)90134-4.

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Handley, H. H., C. J. Flickinger, and J. C. Herr. "Immunohistochemical localization of Lewis rat post-vasectomy autoimmunogens in spermatozoa and testis." Journal of Reproductive Immunology 15 (July 1989): 104. http://dx.doi.org/10.1016/0165-0378(89)90219-2.

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Bronson, R. A., F. M. Fusi, and H. B. Fleit. "Monoclonal antibodies identify Fcγ receptors on unfertilized human oocytes but not spermatozoa." Journal of Reproductive Immunology 21, no. 3 (April 1992): 293–307. http://dx.doi.org/10.1016/0165-0378(92)90032-y.

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Muciaccia, Barbara, Fabrizio Padula, Loredana Gandini, Andrea Lenzi, and Mario Stefanini. "HIV-1 chemokine co-receptor CCR5 is expressed on the surface of human spermatozoa." AIDS 19, no. 13 (September 2005): 1424–26. http://dx.doi.org/10.1097/01.aids.0000180809.04427.04.

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Pillai, Subbi, Haixiang Jiangi, William E. Roudebush, Huamei Zhang, and Marwan Waheba. "Complement Component 1 Inhibitor (Cl-INH) Like Protein on Murine Spermatozoa: Anti-Cl-INH InhibitsIn VitroFertilization." Autoimmunity 28, no. 2 (January 1998): 69–76. http://dx.doi.org/10.3109/08916939809003869.

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Journal articles on the topic 'Spermatozoa Immunology'

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