Probing Human Follicle Stimulating Hormone with Monoclonal Antibodies and Synthetic Peptides
The antigenic topography of the closely related molecules human follicle stimulating hormone (hFSH), human chorionic gonadotropin (hCG), and human luteinizing hormone (hLH) was previously elucidated (1–3) with extensively characterized monoclonal antibodies (MCA) against hFSH (1), hCG (4), bovine LH (bLH) (5), and the free subunits of hCG (6). The structural similarities of the glycoprotein hormones are well established (7); they all consist of 2 subunits designated α and β. In humans, the former is encoded by a single gene and is thus identical for each member of this family, whereas the latter is different from hormone to hormone and is therefore known to mediate biological specificity. Schematic epitope maps were taken as a basis for the alignment of antigenic and receptor interaction domains. The aim of the present study was to localize epitopes on hFSH at the amino acid sequence level with synthetic peptides and to describe the biological role they may play. We focused on the question of whether and, if so, in which way MCA and synthetic peptides interfere with hFSH receptor (hFSH-R) interaction.
KeywordsHuman Chorionic Gonadotropin Glycoprotein Hormone Amino Acid Sequence Level Human Follicle Entire Amino Acid Sequence
Unable to display preview. Download preview PDF.
- 1.Berger P, Panmoung W, Khaschabi D, Mayregger B, Wick G. Antigenic features of human follicle stimulating hormone delineated by monoclonal antibodies and construction of an immunoradiometric assay (IRMA). Endocrinology 1988; 123: 2351.Google Scholar
- 4.Kotler R, Berger P, Wick G. Monoclonal antibodies against human chorionic gonadotropin (hCG): I. production, specificity, and intramolecular binding sites. Am J Reprod Immunol 1982;2:212.322Google Scholar
- 9.Moyle WR, Ehrlich PH, Canfield RE. Use of monoclonal antibodies to subunits of human chorionic gonadotropin to examine the orientation of the hormone in its complex with receptor. Proc Natl Acad Sci USA 1982; 79: 2245.Google Scholar