The Role of Carbohydrate in the Biological Function of Human Chorionic Gonadotropin

  • Om P. Bahl
  • Leopold März
  • William R. Moyle
Part of the Current Topics in Molecular Endocrinology book series (CTME, volume 1)


The binding sites or the so-called receptors for polypeptide and glycoprotein hormones such as insulin (1), glucagon (2), adrenocorticotropin (3), human chorionic gonadotropin (4–6), luteinizing hormone (7–9), and follicle stimulating hormone (10, 11) are located on the plasma membranes of the target cells. The binding is characterized by the high degree of affinity and hormonal specificity, which suggests that the binding sites must have highly specific chemical structures. It is not clearly understood whether all of the sites are equivalent. Moyle and Ramachandran have suggested the presence of more than one type of receptor on Leydig cells for LH with different affinities for the hormone; the sites which induce steroidogenesis have higher affinity than those which stimulate the accumulation of cyclic AMP (12). That the receptors are protein in nature is indicated by their properties after solubilization from the corpora lutea or interstitial tissue from testes with nonionic detergents (13). It is not known, however, whether the receptors are composed of one or several proteins or if any prosthetic groups such as lipids or polysaccharides are also present. The precise chemical elucidation of the receptors must await until all of its components are identified and purified.


Sialic Acid Leydig Cell Human Chorionic Gonadotropin Mannose Residue Specific Chemical Structure 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Cuatrecasas, P., Proc. Nat. Acad. Sci. 63: 450, 1969.PubMedCrossRefGoogle Scholar
  2. 2.
    Rodbell, M., Krans, H. M. J., Pohl, S. L., and Birnbaumer, L., J. Biol. Chem. 246: 1861, 1971.PubMedGoogle Scholar
  3. 3.
    Lefkowitz, R. J., Roth, J., and Pastan, I., Science 170: 633, 1970.PubMedCrossRefGoogle Scholar
  4. 4.
    Catt, K. J., Tsuruhara, T., and Dufau, M. L., Biochim. Biophys. Acta 279: 194, 1972.PubMedCrossRefGoogle Scholar
  5. 5.
    Danzo, B. J., Biochim. Biophys. Acta 304: 560, 1973.PubMedCrossRefGoogle Scholar
  6. 6.
    Saxena, B. B., and Rao, Ch. V., Biochim. Biophys. Acta 313: 372, 1973.PubMedCrossRefGoogle Scholar
  7. 7.
    De Krester, D. M., Catt, K. J., and Paulsen, C. A., Endocrinology 80: 332, 1971.Google Scholar
  8. 8.
    Lee, C. Y. and Ryan, R. J., Endocrinology 89: 1515, 1971.PubMedCrossRefGoogle Scholar
  9. 9.
    Lee, C. Y. and Ryan, R. J., Biochemistry 12: 4609, 1973.PubMedCrossRefGoogle Scholar
  10. 10.
    Means, A. R. and Vaitukaitis, J. L., Endocrinology 90: 39, 1972.PubMedCrossRefGoogle Scholar
  11. 11.
    Bhalla, V. K. and Reichert, L. E., J. Biol. Chem. 249: 43, 1974.PubMedGoogle Scholar
  12. 12.
    Moyle, W. R. and Ramachandran, J., Endocrinology 93: 127, 1973.PubMedCrossRefGoogle Scholar
  13. 13.
    Dufau, M. L., Charreau, E. H., and Catt, K. J., J. Biol. Chem. 248: 6973, 1973.PubMedGoogle Scholar
  14. 14.
    Tsuruhara, T., Dufau, M. L., Hickman, J., and Catt, K. J., Endocrinology 91: 296, 1972.PubMedCrossRefGoogle Scholar
  15. 15.
    Eylar, E. H., J. Theor. Biol. 10: 89, 1965.CrossRefGoogle Scholar
  16. 16.
    Morell, A. G., Gregoriadis, G., Scheinberg, H. I., Hickman, J., and Ashwell, G., J. Biol. Chem. 246: 1461, 1971.PubMedGoogle Scholar
  17. 17.
    Van Hall, E. V., Vaitukaitis, J. L., Ross, G. T., Hickman, J. W., and Ashwell, G., Endocrinology 88: 456, 1971.PubMedCrossRefGoogle Scholar
  18. 18.
    Bahl, O. P., J. Biol. Chem. 244: 565, 1969.Google Scholar
  19. 19.
    Bahl, O. P., in Hormonal Proteins and Peptides, Li, C. H. (ed.), Academic Press, p. 171–199, 1973.Google Scholar
  20. 20.
    Bellisario, R., Carlsen, R. B., and Bahl, O. P., J. Biol. Chem. 248: 6797, 1973.Google Scholar
  21. 21.
    Carlsen, R. B., Bahl, O. P., and Swaminathan, N., J. Biol. Chem. 248: 6810, 1973.PubMedGoogle Scholar
  22. 22.
    Bahl, O. P., J. Biol. Chem. 244: 575, 1969.PubMedGoogle Scholar
  23. 23.
    Greenwood, F. C., Hunter, W. M., and Glover, J. S., Biochem. J. 89: 114, 1963.PubMedGoogle Scholar
  24. 24.
    Ray, T. K., Biochim. Biophys. Acta 196: 1, 1970.PubMedCrossRefGoogle Scholar
  25. 25.
    Kornfeld, S. and Kornfeld, R., in Glycoproteins of Blood Cells and Plasma, Gameison, G. A and Greenwalt, T. J. (eds.), J. B. Lippincott Co., p. 50–67, 1971.Google Scholar
  26. 26.
    Gilman, A. G., Proc. Nat. Acad. Sci. 67: 305, 1970.PubMedCrossRefGoogle Scholar
  27. 27.
    Dufau, M. L., Catt, K. J., and Tsuruhara, T., Endocrinology 90: 1032, 1972.PubMedCrossRefGoogle Scholar
  28. 28.
    Bahl, O. P. and Agrawal, K. M. L., J. Biol. Chem. 244: 2970, 1969.PubMedGoogle Scholar
  29. 29.
    Matta, K. L. and Bahl, O. P., J. Biol. Chem. 247: 1780, 1972.PubMedGoogle Scholar
  30. 30.
    Yen, P. S. and Ballou, C. E., J. Biol. Chem. 248: 8316, 1973.PubMedGoogle Scholar

Copyright information

© Plenum Press, New York 1974

Authors and Affiliations

  • Om P. Bahl
    • 1
    • 2
  • Leopold März
    • 1
    • 2
  • William R. Moyle
    • 1
    • 2
  1. 1.Department of BiochemistryState University of New York at BuffaloBuffaloUSA
  2. 2.Laboratory of Human Reproduction and Reproductive BiologyHarvard Medical SchoolBostonUSA

Personalised recommendations