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Search for other papers by F. JÍLEK in
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Search for other papers by L. VESELSKÝ in
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As on other cell types, some histocompatibility antigens have recently been found on spermatozoa. Vojtíšková (1969), and Vojtíšková, Poláčková & Pokorná (1969) revealed the presence of some H-2 antigens on mouse spermatozoa by using antibody absorption, indirect immunofluorescence and pre-sensitization of recipients with sperm cells to specific skin grafts. Similarly, Goldberg, Aoki, Boyse & Bennett (1970) demonstrated the presence of H-2 antigens and later of H-Y antigen (Goldberg, Boyse, Bennett, Scheid & Carswell, 1971) on mouse spermatozoa by means of a cytotoxic test applied to the spermatozoa. Fellous & Dausset (1970) have published similar results concerning the detection of HL-A antigens on human spermatozoa. Singal, Berry & Naipaul (1971), however, detected HL-A substances in seminal plasma. These antigens on spermatozoa may, therefore, be a phenotypic demonstration of the
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Search for other papers by L. VESELSKÝ in
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Summary.
The protein spectrum of boar seminal plasma is formed mainly by the seminal vesicle fluid proteins, and to a lesser extent by the proteins in the fluids of the cauda epididymidis and prostate.
The proteins of the seminal plasma, the fluids of the cauda epididymidis, prostate, seminal vesicles and the blood serum were divided into five peaks by column chromatography on Sephadex G-100. The proteins of Peak I in boar seminal plasma (mol. wt at least 150,000) were mostly derived from the seminal vesicle fluid and to a small extent from the fluids of the cauda epididymidis and prostate. The proteins of Peak II (mol. wt 120,000) were found in the blood serum only, and those of Peak III (mol. wt 69,000) in the seminal vesicle fluid, the fluid of the cauda epididymidis and the prostate. Peak IV (mol. wt 34,000) was formed by proteins originating mainly from the seminal vesicles and partly from the prostate. The proteins of Peak V (mol. wt 12,000 to 14,000) were derived from the fluids of the cauda epididymidis and the prostate.
These conclusions were confirmed by comparing the activity of acid and alkaline phosphatase and esterase by means of disc electrophoresis on polyacrylamide gel at pH 9·4 and 4·3 and by immunoelectrophoresis of all the fluids and fractions obtained by column chromatography of proteins on Sephadex G-100.
Search for other papers by J. MATOUŠEK in
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Search for other papers by R. STANĚK in
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Search for other papers by L. VESELSKÝ in
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Summary.
The biosynthesis of the aspermatogenic substance in the seminal vesicle fluid of bulls is dependent on the androgen level. The aspermatogenic substance is not present in sexually immature bulls; its synthesis can be evoked, however, by means of testosterone propionate. Castration is followed by a loss of libido and a decline in the production of fluids from the accessory genital glands; injections of testosterone propionate restore libido, the secretion of fluids and their aspermatogenic effect.
The aspermatogenic substance is thermostable, it is not digested by a number of enzymes including proteolytic enzymes, but it must evidently be bound to a protein complex in order to induce aspermatogenesis.
Rabbits developed several antibodies against bull vesicular fluid treated with enzymes, as judged by double diffusion, immunoelectrophoresis and haemagglutination tests. The number and character of the precipitation and haemagglutination antibodies in immunized animals did not differ whether the testes were damaged or undamaged. The fluorescence technique did not detect any binding of antibodies either to epididymal spermatozoa or to histological sections of the testes of rabbits and bulls.
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Search for other papers by J. Dostál in
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Search for other papers by J. Drahorád in
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The repeated deposition of an immunosuppressive fraction isolated from boar vesicular gland secretion into the rectum of healthy male and female mice reduced responses of lymphocytes to mitogens in vitro. Rectal deposition of the immunosuppressive component also led to a decrease in the activity of plaque-forming cells. These findings indicate that repeated rectal deposition of semen may compromise some aspects of the immune system and may be an important cofactor in the development of viral or bacterial infections among homosexual men.
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Search for other papers by V. Jonáková in
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Search for other papers by L. Veselský in
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Search for other papers by E. Töpfer-Petersen in
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A mouse monoclonal antibody against boar acrosin and antiserum prepared to highly purified acrosin in female rabbits were used to detect the antigen in various fluids and tissues of boars using an indirect immunofluorescence technique. A strong reaction was found in fluid and epithelial tissue of the seminal vesicles as well as in the germinal cells in the testis. No immunoreactivity was detected in tissues of the epididymides and other organs of the boar. The antigens present in seminal vesicle fluid of boars were partially purified by column chromatography. It was demonstrated that two antigens differing in molecular mass were present and both possessed protease and amidase activity. The higher molecular mass antigen eluted from a gel filtration column in a volume identical to that of proacrosin. The same result was obtained in polyacrylamide gel electrophoresis in sodium dodecyl sulfate (SDS-PAGE). The low molecular mass antigen was eluted from Sephadex G-75 column together with natural protease inhibitors corresponding in molecular mass to less than 20 kDa. The mobility of the antigen in SDS-PAGE was greater than that of chymotrypsin. It is assumed that the protease from seminal vesicle epithelia resembled acrosin in structure and function. Acrosin may therefore not be specific for spermatozoa.
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Search for other papers by L. Veselský in
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Search for other papers by V. Jonáková in
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Intravenous deposition of the immunosuppressive component, isolated from boar seminal vesicle secretion, led to suppression of primary and secondary antibody response to boar epididymal spermatozoa and to bacterial antigens. The most effective suppression of the immune response was achieved in female mice treated with immunosuppressive component 3 days before the immunization with antigen. The treatment with immunosuppressor 3 days after the immunization resulted in less effective immunosuppression. After the primary immunization, male mice displayed low sensitivity to epididymal spermatozoa. The production of IgG and IgM antibodies to spermatozoa was depressed for a relatively long period in female mice treated with immunosuppressor. The immunosuppressive components of the reproductive gland secretions may protect sperm cells from the adverse effect of the immune system cells and enhance the chance of conception. However, seminal immunosuppressive components may play an unfavourable role by producing a predisposition in the reproductive tract to bacterial or viral infections.
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Search for other papers by B Železná in
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The immunosuppressive fraction (ISF) of boar seminal vesicle fluid was recently demonstrated to inhibit production of T helper (Th)1 cytokines and enhance production of Th2 cytokines. The present study shows the effect of the ISF on leptin concentrations in blood plasma and adipose tissue in mice during pregnancy. The ISF effect on thymus weight during pregnancy is also demonstrated. The leptin concentration in blood plasma and adipose tissue increased and remained high in the latter half of pregnancy. ISF treatment at the beginning of pregnancy significantly lowered the leptin concentration both in blood plasma and adipose tissue of pregnant mice. Thymus involution has been described previously in pregnant mice. ISF treatment compensated for the loss of thymus mass during the whole pregnancy in the ISF-treated mice. The treatment of pregnant mice with ISF did not affect pregnancy and litter size.
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Search for other papers by V. Jonáková in
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Search for other papers by M. L. Sanz in
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Search for other papers by D. Čechová in
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Summary. A highly purified 15 kDa glycoprotein isolated from ejaculated spermatozoa was used to raise antisera in female rabbits. An indirect immunofluorescence technique was used to detect the antigen in the seminal vesicle tissue and on the acrosomes of ejaculated, native and capacitated, boar spermatozoa. No immunoreactivity was detected on cells of the seminiferous tubules (spermatogonia, spermatocytes, and spermatids), on spermatozoa in the ductus epididymis and in cells of the epididymal and testicular tissues. These observations support the view that the 15 kDa protein is produced in the seminal vesicle secretory epithelium, and is attached to the sperm plasma membrane during the exposure of spermatozoa to seminal vesicle compounds. The observations that the antigen remained on the acrosome of ejaculated spermatozoa after capacitation and blocked sperm–oocyte binding in vitro suggest that the antigen plays a role in sperm–egg interactions. The strong immunoreactivity exhibited by cumulus cells after incubation of antisera with the porcine egg surrounded by cumulus cells shows the possible importance of the 15 kDa glycoprotein for contact of spermatozoa with cells of the cumulus oophorus surrounding the egg.
Keywords: zona pellucida; binding proteins; sperm–egg interaction; gamete recognition; boar; indirect immunofluorescence
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Heparin-binding proteins (designated BHB-2–BHB-9) were isolated from boar seminal plasma by affinity chromatography on heparin immobilized on polyacrylamide gel, followed by reverse phase HPLC. According to their N-terminal amino acid sequences, BHB-3–BHB-5 belong to the AQN family of spermadhesins and BHB-7–BHB-9 to the AWN family. BHB-6 is composed of two different proteins. The dominant protein (14 kDa) has the N-terminal amino acid sequence HNKQEGRDHD that is identical to the sequence of human semenogelin at positions 85–94. The minor proteins (16 and 17 kDa) belong to the AWN family of spermadhesins. The 14 kDa HNK protein does not crossreact with antibodies against AQN or AWN spermadhesins. BHB-2 also binds to the acrosome of boar epididymal spermatozoa but has the N-terminal sequence DQH. Therefore, basic protein BHB-2 belongs to a new family of DQH sperm surface proteins that are homologous to the acidic proteins from bull and stallion seminal plasma, to the collagen binding domain II in fibronectin and to the leucocyte cell–cell adhesion regulator, but are not homologous to AQN or AWN spermadhesins. Nevertheless, antiAQN-1 spermadhesin antibodies crossreact strongly with DQH protein. All boar heparin-binding proteins bind concanavalin A indicating their glycoprotein nature, which was proved by the detection of glucosamine and galactosamine residues in their molecules. Furthermore, spermadhesins interact with zona pellucida, protease inhibitors and a polyacrylamide derivative of heparin. Affinity chromatography experiments showed that the DQH protein bound to gelatin–agarose together with the AWN proteins and that the DQH protein and AQN-1 spermadhesin belong to the phosphoryl choline binding proteins.
