Synthetic alpha-subunit peptides stimulate testosterone production in vitro by rat Leydig cells
| Autor: | Robert J. Ryan, S A Rizza, M C Charlesworth, L D Erickson, Elizabeth R. Bergert, Daniel J. McCormick |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Male
endocrine system medicine.medical_specialty medicine.drug_class Protein Conformation Molecular Sequence Data Alpha (ethology) Biology Chorionic Gonadotropin Structure-Activity Relationship Endocrinology Internal medicine medicine Animals Testosterone Amino Acid Sequence Binding site Receptor chemistry.chemical_classification Leydig cell Circular Dichroism Cell Membrane Ovary Leydig Cells Rats Inbred Strains Androgen In vitro Peptide Fragments Rats medicine.anatomical_structure chemistry Glycoprotein Hormones alpha Subunit Biological Assay Female Glycoprotein hormones hormone substitutes and hormone antagonists Hormone |
| Zdroj: | Endocrinology. 126(5) |
| ISSN: | 0013-7227 |
| Popis: | The glycoprotein hormones (LH, hCG, FSH, and TSH) have a common 92-amino acid alpha-subunit which is noncovalently linked to a hormone-specific beta-subunit. Synthetic peptides of the alpha-subunit have been shown to inhibit binding of [125I]iodo-hCG to rat ovarian membrane and [125I]iodo-TSH to human thyroid membrane preparations. Synthetic overlapping peptides of the alpha-subunit of hCG were prepared by solid phase techniques and tested in a standard in vitro rat Leydig cell bioassay. Three regions in the alpha-subunit (alpha 1-15, alpha 30-45, and alpha 71-85) were found to stimulate testosterone production. All three regions correlate with inhibition of hCG binding to ovarian receptors, but subtle differences exist between the binding sites and effector sites. These data indicate that the glycoprotein alpha-subunit has intrinsic bioactivity. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|