Radioligand binding studies reveal marked species differences in the vasopressin V1 receptor of rat, rhesus and human tissues
| Autor: | Roger M. Freidinger, Douglas J. Pettibone, Peter D. Williams, B. V. Clineschmidt, Maribeth T. Kishel, Carla J. Woyden, Mark G. Bock, Daniel F. Veber |
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| Rok vydání: | 1992 |
| Předmět: |
Male
Vasopressin medicine.medical_specialty Receptors Vasopressin Uterus Binding Competitive General Biochemistry Genetics and Molecular Biology Radioligand Assay Species Specificity biology.animal Internal medicine medicine Animals Humans Primate General Pharmacology Toxicology and Pharmaceutics Binding site Vasopressin receptor Binding Sites Receptors Angiotensin biology Human liver urogenital system Rats Inbred Strains General Medicine Macaca mulatta Rats Arginine Vasopressin medicine.anatomical_structure Endocrinology Radioligand binding Liver In utero Female Oligopeptides hormones hormone substitutes and hormone antagonists |
| Zdroj: | Life sciences. 50(25) |
| ISSN: | 0024-3205 |
| Popis: | The [ 3 H]arginine-vasopressin ([ 3 H]AVP) binding site in rat, rhesus and human liver and nonpregnant human uterus was characterized and contrasted. [ 3 H]AVP bound with high affinity (K i values, 0.2–0.6 nM) to preparations of all tissues studied. Competition binding studies using a series of compounds from three structural classes indicate a marked species difference between the rat and primate liver AVP-V 1 site. This site in rhesus and human liver however, is essentially identical, indicating that the rhesus liver is an appropriate surrogate for human tissue. These studies also indicate that the AVP-V 1 site of nonpregnant human uterus and human liver is equivalent. |
| Databáze: | OpenAIRE |
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