Luteinizing Hormone Receptors: Specific Binding of Human Luteinizing Hormone to Homogenates of Luteinized Rat Ovaries
AUTOR(ES)
Lee, Ching Yung
RESUMO
Binding of human [125I]luteinizing hormone to homogenates of luteinized rat ovaries is dependent upon time, temperature, and pH and is saturable. Injection of human chorionic gonadotropin in vivo or addition of unlabeled human chorionic gonadotropin or human or ovine luteinizing hormone in vitro inhibits binding, whereas follicle stimulating hormone or prolactin is without effect. The dissociation constant for binding of luteinizing hormone receptor is 0.79 nM. The number of binding sites is 94 femtomol/mg of wet weight. NaCl, KCl, MgSO4, and CaCl2 at concentrations below 10 mM have no effect on binding, while all salts significantly inhibit binding at 150 mM. Binding of [125I]luteinizing hormone to its receptors is destroyed by proteolytic enzymes and by phospholipase C and D. The total binding activity is quantitatively recovered in the 2000 × g pellet of the homogenate.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=389811Documentos Relacionados
- Gonadal luteinizing hormone receptors and adenylate cyclase: transfer of functional ovarian luteinizing hormone receptors to adrenal fasciculata cells.
- Similar luteinizing hormone-releasing hormone binding sites in rat anterior pituitary and ovary.
- Targeted overexpression of luteinizing hormone in transgenic mice leads to infertility, polycystic ovaries, and ovarian tumors.
- Trans-activation by thyroid hormone receptors: functional parallels with steroid hormone receptors.
- Insulin-like growth factor-I enhances luteinizing hormone binding to rat ovarian theca-interstitial cells.
