The Antigenic Structure of the Human Glycoprotein Hormone α-Subunit. I. Characterization of Anti-α Monoclonal Antibodies*
| Autor: | Robert J. Ryan, Elizabeth R. Bergert, M C Charlesworth, H. Hojo, T. Vutyavanich, Daniel J. McCormick |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
endocrine system
medicine.medical_specialty Receptor complex medicine.drug_class Radioimmunoassay Thyrotropin Enzyme-Linked Immunosorbent Assay Biology Monoclonal antibody Chorionic Gonadotropin Epitope Epitopes Mice Radioligand Assay Receptors Gonadotropin Endocrinology Antigen Cell surface receptor Internal medicine medicine Animals Receptor chemistry.chemical_classification Mice Inbred BALB C Ovary Antibodies Monoclonal Luteinizing Hormone Molecular biology Rats chemistry Glycoprotein Hormones alpha Subunit Female Follicle Stimulating Hormone Gonadotropin Glycoprotein |
| Zdroj: | Endocrinology. 127:2977-2984 |
| ISSN: | 1945-7170 0013-7227 |
| DOI: | 10.1210/endo-127-6-2977 |
| Popis: | The glycoprotein hormones CG, LH, FSH, and TSH are composed of two noncovalently linked subunits, alpha and beta. The beta-subunit confers hormone specificity, while the alpha-subunit is homologous within a species. To help in determining the antigenic structure of the common alpha-subunit, six monoclonal antibodies (mAbs) to the free or heterodimeric alpha-subunit of human (h) gonadotropic hormones have been prepared and, along with two previously isolated mAbs, have been characterized for binding specificity to alpha- and beta-subunits and the human glycoprotein hormones, CG, LH, FSH, and TSH. Each mAb was derived from hybidomas of FO myeloma cells fused with spleen cells from mice immunized with free alpha-subunit, hCG or hFSH. mAbs A101, A102, and E512 were specific for the alpha-subunit but showed the highest affinity for the intact hormone; K2.18, K94.6, E501, E502, and E511 were specific for free alpha. All of the antibodies inhibited binding of 125I-hCG to luteal membrane receptor, and 125I-labeled mAbs did not recognize hCG/receptor complex. Characterization by two-site binding assays using alpha, hCG, or hFSH as antigen revealed that all the mAbs bind to unique sites on alpha which may be overlapping, and which are modified in the intact hormone. The antigenic sites for mAbs E502, E511, and K2.18 are at least partially linear because they bind to reduced, carboxymethylated alpha. |
| Databáze: | OpenAIRE |
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