Abstract
Immunocontraception is defined as regulation of fertility by means of immunological processes with the aim of preventing pregnancy. This concept comprises active immunization against an antigenic structure which is a specific and essential component of the reproductive system or the administration of antibodies against this structure.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Donat, H. (1979). Stand and Entwicklungstendenzen immunologischer Kontrazeptionsmethoden. Zbl. Gynäkol., 7, 433
Matangkasombut, P. (1979). New approaches to immunological contraception. Clin. Obstet. Gynecol., 6, 531
Stevens, V. C. (1979). Human chorionic gonadotrophin: properties and potential immunological manipulation for clinical application. Clin. Obstet. Gynecol., 6, 549
Talwar, G. P. (1979). Immunology in reproduction. J. Reprod. Med., 22, 61
Anderson, D. J. and Alexander, N. J. (1983). A new look at antifertility vaccines. Fertil. Steril., 40, 557
Bleil, J. D. and Wassarman, P. M. (1980). Mammalian sperm-egg interaction: identification of a glycoprotein in mouse egg zonae pellucidae possessing receptor activity for sperm. Cell, 20, 873
Dunbar, B. S., Wardrip, N. J. and Hendrick, J. L. (1980). Isolation, physicochemical properties, and the macromolecular composition of the zona pellucida from porcine oocytes. Biochemistry, 19, 356
Sacco, A. G. (1981). Immunocontraception: consideration of the zona pellucida as a target antigen. Obstet. Gynecol. Ann., 10, 1
Aitken, R. J., Rudak, E. A., Richardson, D. W., Dor, J., Djahanbahkch, O. and Templeton, A. A. (1981). The influence of anti-zona and anti-sperm antibodies on sperm-egg interactions. J. Reprod. Fertil., 62, 597
10.Goldberg, E. (1972). Amino acid composition and properties of crystalline lactate dehydrogenase-X from mouse testes. J. Biol. Chem., 247, 2044
Goldberg, E. (1973). Infertility in female rabbits immunized with lactate dehydrogenase X. Science, N.Y., 181, 458
Goldberg, E., Wheat, T. E., Powell, J. E. and Stevens V. C. (1981). Reduction of fertility in female baboons immunized with lactate dehydrogenase C4. Fertil. Steril., 35, 214
Anderson, D. J., Adams, P. H., Hamilton, M. S. and Alexander, N. J. (1983). Antisperm antibodies in mouse vasectomy sera react with embryonal teratocarcinoma. J. Immunol., 131, 2908
Hamilton, M. S. and Anderson, D. J. (1982). Antibodies to antigens on teratocarcinoma cells are associated with parity in mice. Biol. Reprod., 27, 104
Hamilton, M. S., Beer, A. E., May, R. D. and Vitetta, E. S. (1979). The influence of immunization of female mice with F 9 teratocarcinoma cells on their reproductive performance. Transplant. Proc., 11, 1069
Lin, T. M. and Halbert, S. P. (1976). Placental localization of human pregnancy-associated plasma proteins. Science, N. Y., 193, 1249
Tartarinov, Y. S. (1978). Trophoblast-specific beta1 -glycoprotein as a marker for pregnancy and malignancies. Gynecol. Obstet. Invest., 9, 65
Bohn, H. (1978). Pregnancy-specific β1-globulin SP1,. Scand. J. Immunol., 6 (Suppl.), 119
Engvall, E. (1980). Pregnancy-specific β1 -glycoprotein (SP1). Purification and partial characterization. Oncodevelop. Biol. Med., 1, 113
Abdel Ghaffar, A. and Klopper, A. (1980). Separation of two pregnancy-associated proteins with SP, determinants and the conversion of SP1, β to SP1, α. Arch. Gynecol., 230, 95
Griffith, B. W. and Godard, A. (1982). Immunoadsorbent isolation of pregnancy-specific β 1,-glycoprotein from maternal serum. Can. J. Biochem. Cell. Biol., 61, 130
Heikinheimo, M., Saksela, O., Lehtovirta, P., Seppälä, M. and Bohn, H. (1981). Cultured human syncytiotrophoblasts synthesize pregnancy-specific beta-1-glycoprotein (SP1). Acta Pathol. Microbiol. Scand. Sect. C, 89, 139
Chou, J. Y. (1983). Production of pregnancy-specific β,-glycoprotein by human placental cells and human fibroblasts. Oncodevelop. Biol. Med., 4, 319
Bohn, H. and Weinmann (1974). Immunologische Unterbrechung der Schwangerschaft bei Affen mit Antikörpern gegen das menschliche schwangerschaft-spezifische β1-Glykoprotein (SP1). Arch. Gynäk., 217, 209
Midgley, A. R. Jr. and Pierce, G. B. Jr. (1962). Immunohistochemical localization of human chorionic gonadotropin. J. Exp. Med., 115, 289
Diczfalusy, E. (1953). Chorionic gonadotrophin and oestrogens in the human placenta. Acta Endocrinol., 12, 323
Wide, L. (1962). An immunological method for the assay of human chorionic gonadotrophin. Acta Endocrinol., 70, 1
Braunstein, G. D., Grodin, J. M., Vaitukaitis, J. and Ross, G. T. (1973). Secretory rates of human chorionic gonadotropin by normal trophoblast. Am. J. Obstet. Gynecol., 115, 447
Huot, R. I., Foidart, J.-M. and Stromberg, K. (1979). Effects of culture conditions on the synthesis of human chorionic gonadotropin by placental organ cultures. In vitro, 15, 497
Merz, W. E. (1984). Structure-function relationships of gonadotropins: human choriogonadotropin as a model. In Runnebaum, B., Rabe, T., Kiesel, L. and Merz, W. E. (eds.) Secretion and Action of Gonadotropins. Physiology and Clinic, pp. 59–82. ( Berlin, Heidelberg, New York, Tokyo: Springer-Verlag )
Hilf, G. and Merz, W. E. (1984). Biosynthesis and secretion of hCG and its subunits in placental tissue culture. In Hesch, R. D. and Atkinson, M. (eds.) Peptide Hormones as Mediators in Immunology and Oncology. ( New York: Raven Press )
Hilf, G. and Merz, W. E. (1984). Regulation of placental biosynthesis and secretion of choriogonadotropin. Contracept. Deliv. Syst., 5, 79
Siler-Khodr, T. M., Khodr, G. S., Vickery, B. H. and Nestor, J. J. (1983). Inhibition of hCG, β-hCG and progesterone release from human placenta tissue in vitro by an GnRH antagonist. Life Sci., 32, 2741
Merz, W. E. and Hilf, G. (1984). Influence of LHRH and des-Glyl0-[D-Ala6]-LHRH ethylamide on the biosynthesis of hCG in placental tissue culture. In Schmidt-Gollwitzer and Elger, W. (eds.) Recent Advances in Bioscience. ( Berlin: Walter deGruyter) (In press )
Vaitukaitis, J. L., Ross, G. T., Braunstein, G. D. and Rayford, P. L. (1976). Gonadotropins and their subunits: basic and clinical studies. Rec. Progr. Hormone Res., 32, 289
Baylin, S. B. and Mendelson, G. (1980). Ectopic (inappropriate) hormone production by tumors: Mechanisms involved and the biological and clinical implications. Endocrinol. Rev., 1, 45
Braunstein, G. D., Rasor, J. and Wade, M. E. (1975). Presence in normal tests of a chorionic-gonadotropin like substance distinct from human luteinizing hormone. N. Engl. J. Med., 293, 1339
Chen, H. C., Hodgen, G. D., Matsuura, L. J., Lin, L. J., Gross, E., Reichert, L. E. Jr., Birken, S., Canfield, R. E. and Ross, G. T. (1976). Evidence for a gonadotropin from nonpregnant subjects that has physical, immunological and biological similarities to hCG. Proc. Natl. Acad. Sci. USA, 73, 2885
Masure, H. R., Jaffee, W. L., Sickel, M. A., Birken, S., Canfield, R. E. and Vaitukaitis, J. L. (1981). Characterization of a small molecular size urinary immunoreactive human chorionic gonadotropin (hCG) like substance produced by normal placenta and by hCG-secreting neoplasms. J. Clin. Endocrinol. Metab., 53, 1014
Matsuura, S., Ohashi, M., Chen, H. C., Shownkeen, R. C., Stockell Hartree, A., Reichert, L. E. Jr., Stevens, V. C. and Powell, J. E. (1980). Physicochemical and immunological characterization of an hCG-like substance from human pituitary glands. Nature (London), 286, 740
Suginami, H. and Kawaoi, A. (1982). Immunohistochemical localization of a human chorionic gonadotropin-like substance in the human pituitary gland. J. Clin. Endocrinol. Metab., 55, 1161
Maruo, T., Segal, S. J. and Koide, S.S. (1979). Studies on the apparent choriogonadotropin-like factor in the crab Ovalipes ocellatus. Endocrinology, 104, 932
Maruo, T., Cohen, H., Segal, S. J. and Koide, S.S. (1979). Production of a choriogonadotropin-like factor by a micro-organism. Proc. Natl. Acad. Sci. USA, 76, 6622
Swaminathan, N. and Bahl, O. P. (1970). Dissociation and recombination of the subunits of human chorionic gonadotropin. Biochem. Biophys. Res. Commun., 40, 422
Canfield, R. E., Morgan, F. J., Kammerman, S., Bell, J. J. and Agosto, G. M. (1971). Studies on human chorionic gonadotropin. Rec. Progr. Hormone Res., 27, 121
Bellisario, R., Carlsen, R. B. and Bahl, O. P. (1973). Human chorionic gonadotropin. Linear amino acid sequence of the a-subunit. J. Biol. Chem., 248, 6796
Carlsen, R. B., Bahl, O. P. and Swaminathan, N. (1973). Human chorionic gonadotropin. Linear amino acid sequence of the β-subunit. J. Biol. Chem., 248, 6810
Birken, S. and Canfield, R. E. (1977). Isolation and amino acid sequence of COON-terminal fragments from the β-subunit of human choriogonadotropin. J. Biol. Chem., 252, 5386
Keutmann, H. T. and Williams (1977). Human chorionic gonadotropin. Amino acid sequence of the hormone-specific COOH-terminal region. J. Biol. Chem., 252, 5392
Kessler, M. J., Reddy, M. S., Shah, R. H. and Bahl, O. P. (1979). Structures of N-glycosidic carbohydrate units of human chorionic gonadotropin. J. Biol. Chem., 254, 7901
Kessler, M. J., Mise, T., Ghai, R. D. and Bahl, O. P. (1979). Structure and location of the O-glycosidic carbohydrate units of human chorionic gonadotropin. J. Biol. Chem., 254, 7909
Pierce, J. G. and Parsons, T. F. (1981). Glycoprotein hormones: structure and function. Ann. Rev. Biochem., 50, 465
Morgan, F.J., Birken, S. and Canfield, R.E. (1975). The amino acid sequence of human chorionic gonadotropin. The α and β subunit. J. Biol. Chem., 250, 5247
Talwar, G. P., Sharma, N. C., Dubey, S. K., Salahuddin, M., Das, C., Ramakrishnan, S., Kumar, S. and Hingorani, V. (1976). Isoimmunization against human chorionic gonadotropin with conjugates of processed β-subunit of the hormone and tetanus toxoid. Proc. Natl. A cad. Sci. USA, 73, 218
Matsuura, S., Ohashi, M., Chen, H. C. and Hodgen, G. D. (1979). A human chorionic gonadotroin-specific antiserum against synthetic peptide analogs to the carboxy-terminal peptide of its β-subunit. Endocrinology, 104, 396
Ramakrishnan, S. and Talwar, G. P. (1980). Immuno-biological studies with beta-subunit of human chorionic gonadotropin and its subfragments. In Segal, S.J. (ed.) Chorionic Gonadotropin, pp. 213–230. ( New York, London: Plenum Press )
Birken, S. and Canfield, R. E. (1980). Chemistry and immunochemistry of human chorionic gonadotropin. In Segal, S.J. (ed.) Chorionic Gonadotropin, pp. 65–86. ( New York, London: Plenum Press )
Dörner, M., Brossmer, R., Hilgenfeldt, U. and Trude, E. (1971). Immunological reactions of antibodies to human chorionic gonadotropin (hCG) with hCG and its chemical derivatives. In Margoulis, M. and Greenwood, F.C. (eds.) Structure-Activity Relationships of Protein and Polypeptide Hormones, pp. 539–541. ( Amsterdam, London, Princeton: Excerpta Medica )
Mori, K. F., Wood, R. J., Hum, V. G. and Botting, H. C. (1978). Acylation of amino groups in human chorionic gonadotropin with acid anhydrides. Mol. Cell. Endocrinol., 11, 285
Ghai, R. D., Mise, T., Pandian, M. R. and Bahl, O. P. (1980). Immunological properties of the β-subunit of human chorionic gonadotropin. I. Effect of chemical and enzymatic modifications. Endocrinology, 107, 1556
Merz, W. E. and Dorner, M. (1983). Iodinated choriogonadotropin (hCG): Biological, physical and immunological investigations. Acta Endocrinol., 253 (Suppl.), 51
Merz, W. E. (1977). Studien zur Beziehung zwischen Struktur und Wirking beim choriogonadotropen Hormon des Menschen. Thesis for Habilitation, pp. 300–332 ( Heidelberg: Fakultät für Naturwissenschaftliche Medizin )
Bahl, O. P., Pandian, M. R. and Ghai, R. D. (1976). Immunological properties of the β-subunit of human chorionic gonadotropin. Biochem. Biophys. Res. Commun., 70, 525
Mori, K. F., Hum, V. G. and Botting, H. G. (1977). Partial reduction with dithiothreitol of disulfide bonds in human chorionic gonadotropin. Mol. Cell. Endocrinol., 6, 181
Brossmer, R., Dörner, M., Hilgenfeldt, U., Leidenberger, F. and Trude, E. (1971). Chemical modification of human chorionic gonadotropin and its biological and immunological characterization. FEBS Lett., 15, 36
Brossmer, R. and Merz, W. E. (1976). Carbohydrates and the biological function of gonadotropic hormones. In James, V.H.T. (ed.) Proceedings of the V International Congress of Endocrinology. Vol. 1, pp. 92–98. ( Amsterdam: Excerpta Medica )
Pandian, M. R., Mitra, R. and Bahl, O. P. (1980). Immunological properties of human chorionic gonadotropin (hCG). II. Properties of a hCG-specific antibody prepared against a chemical analog of the β-subunit. Endocrinology, 107, 1564
Bahl, O. P. and Moyle W. R. (1978). Role of carbohydrate in the action of gonadotropins. In Birnbaumer, L. and O’Malley B. W. (eds.) Receptors and Hormone Action. Vol. III, pp. 261–289. ( New York, San Francisco, London: Academic Press )
Merz, W. E. and Merkel, U. (1984). Proteolytic degradation of native hCG: possible implications for hormone structure and tumor diagnosis. Acta Endocrinol., 264 (Suppl.), 54
Merz, W. E. and Dörner, M. (1979). Studies of the specific role of the subunits of choriogonadotropin for biological, immunological and physical properties of the hormone. Digestion of choriogonadotropin and its isolated subunits with serine carboxypeptidase. Hoppe-Seyler’s Z. Physiol. Chem., 360, 1783
Mori, F. K. (1970). Antigenic structure of human gonadotropins: Importance of protein moiety to the antigenic structure of human chorionic gonadotropin. Endocrinology, 86, 97
Merz, W. E. and Dörner, M. (1984). Investigations on structure-function relationships of human choriogonadotropin with shortened COOH-terminus of the α-subunit portion. I. Receptor binding and immunological properties. Biochim. Biophys. Acta, 844, 62
Parlow, A. F. and Shome, B. (1975). A highly immunoreactive peptide fragment of human luteinizing hormone alpha subunit, discerned with a new,‘sequence-specific’ radioimmunoassay. J. Clin. Endocrinol. Metab., 41, 195
Merz, W. E. (1979). Study of the specific role of the subunits of choriogonadotropin for biological, immunological and physical properties of the hormone. Digestion of the α-subunit with carboxypeptidase A. Eur. J. Biochem., 101, 541
Merz, W. E. (1980). Properties of chymotrypsin- and trypsin-digested α-subunit of choriogonadotropin. Hoppe-Seyler’s Z. Physiol. Chem., 361, 302
Stevens, V. C. (1973). Immunization of female baboons with hapten-coupled gonadotropins. Obstet. Gynecol., 42, 496
Nash, H., Talwar, G. P., Segal, S., Luukkainen, T., Johansson, E.D.B., Vasquez, J., Coutinho, E. and Sundaram, K. (1980). Observations on the antigenicity and clinical effects of a candidate antipregnancy vaccine: β-subunit of human chorionic gonadotropin linked to tetanus toxoid. Fertil. Steril., 34, 328
Tandon, A., Das, C., Jailkhani, B. L., Amitabh Gaur, Sehgal, S., Gopinath, G. and Talwar, G. P. (1984). Effects on pregnancy in mice of passive immunization against ovine LH and human chorionic gonadotrophin. J. Reprod. Fertil., 70, 369
Das, C., Talwar, G. P., Ramakrishnan, S., Salahuddin, M., Kmar, S. and Hingorani, V. (1978). Discriminatory effect of anti Pr-β-hCG-TT antibodies on the neutralization of the biological activity of placental and pituitary gonadotropins. Contraception, 18, 35
Amr, S., Wehman, R. E., Birken, S., Canfield, R. E. and Nisula, B. C. (1983). Characterization of a carboxyterminal peptide fragment of the human choriogonadotropin β-subunit excreted in the urine of a woman with choriocarcinoma. J. Clin. Invest., 71, 329
Swaminathan, N. and Braunstein, G. D. (1978). Location of major antigenic sites of the β-subunit of human chorionic gonadotropin. Biochemistry, 17, 5832
Matsuura, S., Chen, H.-C., and Hodgen, G. D. (1978). Antibodies to the carboxyl-terminal fragment of human chorionic gonadotropin β-subunit: characterization of antibody recognition sites using synthetic peptide analogues. Biochemistry, 17, 575
Rocklin, R. E., Kitzmiller, J. L. and Kaye, M. D. (1979). Immunobiology of the maternalfetal relationship. Ann. Rev. Med., 30, 375
Murgita, R. A. and Wigzell, H. (1981). Regulation of the immune functions in the fetus and the newborn. Progr. Allergy, 29, 54
Siiteri, P. K. and Stites, D. P. (1982). Immunologic and endocrine interrelationships in pregnancy. Biol. Reprod., 26, 1
Pattillo, R. A. (1981). Histocompatibility antigens in pregnancy, abortions, infertility, preeclampsia, and trophoblast neoplasms. Progr. Clin. Biol. Res., 70, 259
Faulk, W. P., Hsi, B.-L., McIntyre, J. A., Yeh, C.-J.G. and Muchielli (1982). Antigens of human extra-embryonic membranes. J. Reprod. Fertil., 31 (Suppl.), 181
Faulk, W. P. and McIntyre, J. A. (1983). Immunological studies of human trophoblast: markers, subsets and functions. Immunol. Rev., 75, 139
Lala, P. K., Chatterjee-Hasrouni, S., Kearns, M., Montgomery, B. and Colavincenzo, V. (1983). Immunobiology of the feto-maternal interface. Immunol. Rev., 75, 87
Kaye, M. D. and Jones, W. R. (1971). Effect of human chorionic gonadotropin on in vitro lymphocyte transformation. Am. J. Obstet. Gynecol., 109, 1029
Adcock, E. W., III, Teasdale, F., August, C. S., Cox, S., Meschia, G., Battaglia, F. C. and Naughton, M.A. (1973). Human chorionic gonadotropin: its possible role in maternal lymphocyte suppression. Science, N. Y., 181, 845
Contractor, S. F. and Davies, H. (1973). Effect of human chorionic somatomammotrophin and human chorionic gonadotrophin on phytohaemagglutinin-induced lymphocyte transformation. Nature New Biol., 243, 284
Teasdale, F., Adcock, E. W. III, August, C. S., Cox, S., Battaglia, F. C. and Naughton, M. A. (1973). Human chorionic gonadotropin: Inhibitory effect on mixed lymphocyte cultures. Gynecol. Obstet. Invest., 4, 263
Gundert, D., Merz, W. E., Hilgenfeldt, U. and Brossmer, R. (1975). Inability of highly purified preparations of human chorionic gonadotropin to inhibit the phytohaemagglutinin-induced stimulation of lymphocytes. FEBS Lett., 53, 309
Caldwell, J. L., Stites, D. P. and Fudenberg, H. H. (1975). Human chorionic gonadotropin: effects of crude and purified preparations on lymphocyte responses to phytohemagglutinin and allogeneic stimulation. J. Immunol., 115, 1249
Bean, M. A., Salser, J. S., Newman, M., Stahl, K. and Balis, M. E. (1977). Human chorionic gonadotropin: Doubtful role as an inhibitor of cell-mediated immunity. Cancer Immunol. Immunother., 2, 85
Merz, W. E., Schmidt, W., Hilgenfeldt, U., Schackerf, K. and Lenhard, V. (1977). Isolation of substances from crude preparations of human chorionic gonadotropin (hCG) which strongly inhibit the transformation of lymphocytes. Z. ImmunForsch., 152, 286
Merz, W. E., Schmidt, W. and Lehnhard, V. (1979). Separation of the gonadotropic activity of crude choriogonadotropin from the inhibitory effect on lymphocyte transformation. Hoppe-Seyler’s Z. Physiol. Chem., 30, 1433
Schmidt, W., Merz, W. E., Lehnhard, V. and Kubli, F. (1981). Effects of crude and purified human chorionic gonadotropin on lymphocyte response. Gynecol. Obstet. Invest., 12, 132
Editor information
Rights and permissions
Copyright information
© 1985 MTP Press Limited
About this chapter
Cite this chapter
Merz, W.E. (1985). Biochemical aspects of a contraception model based on immunological properties of proteohormones. In: Runnebaum, B., Rabe, T., Kiesel, L. (eds) Future Aspects in Contraception. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-4916-4_25
Download citation
DOI: https://doi.org/10.1007/978-94-009-4916-4_25
Publisher Name: Springer, Dordrecht
Print ISBN: 978-94-010-8678-3
Online ISBN: 978-94-009-4916-4
eBook Packages: Springer Book Archive