Characterization by Affinity Cross-Linking of a Receptor for Atrial Natriuretic Peptide in Cultured Human Thyroid Cells Associated with Reductions in Both Adenosine 3′5′-Monophosphate Production and Thyroglobulin Secretion*
| Autor: | Sabita Lahiri, Juan C. D’Avis, Leonard Wartofsky, Yueh-Chu L. Tseng, Kenneth D. Burman, Donald F. Sellitti |
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| Rok vydání: | 1990 |
| Předmět: |
medicine.medical_specialty
Endocrinology Diabetes and Metabolism medicine.medical_treatment Clinical Biochemistry Guanosine Monophosphate Thyroid Gland Receptors Cell Surface Biology Peptide hormone Binding Competitive Thyroglobulin Biochemistry Cyclic nucleotide chemistry.chemical_compound Endocrinology Atrial natriuretic peptide Internal medicine Cyclic AMP medicine Humans Receptor Cells Cultured Binding Sites Biochemistry (medical) Thyroid medicine.anatomical_structure chemistry cardiovascular system cAMP-dependent pathway Receptors Atrial Natriuretic Factor Atrial Natriuretic Factor hormones hormone substitutes and hormone antagonists circulatory and respiratory physiology Endocrine gland |
| Zdroj: | The Journal of Clinical Endocrinology & Metabolism. 70:528-533 |
| ISSN: | 1945-7197 0021-972X |
| DOI: | 10.1210/jcem-70-2-528 |
| Popis: | We have previously identified specific atriopeptin (ANP) receptors in cultured human thyroid cells and demonstrated that ANP reduced thyroglobulin (Tg) secretion. In this report the relationship of Tg inhibition to cyclic nucleotide intermediate pathways was explored, and the thyroidal ANP receptor was characterized by affinity cross-linking. Concentrations of Tg, cGMP, and cAMP were measured in medium from thyroid cells cocultured with ANP. ANP significantly inhibited cAMP production at the lower concentration of 0.1 nmol/L and stimulated cGMP levels at a higher concentration of 10 nmol/L. The percentage of inhibition of Tg release over the ANP range of 0.01-10 nmol/L appeared to parallel cAMP, but not cGMP, levels, suggesting that ANP acts via a cAMP pathway in the thyroid. Affinity cross-linking studies characterizing the ANP receptor in thyrocytes and a bovine endothelial cell line known to be cGMP responsive to ANP indicated a single unit ANP receptor of 140 kD coupled to guanylate cyclase in endothelial cells, while a 70-kD receptor was found in thyroid cells which specifically binds to ANP, atriopeptin-I, and atriopeptin-III. These studies in thyrocytes suggest that reduced Tg release may be mediated by a specific single 70-kD ANP receptor associated with an inhibitor cAMP pathway and provide additional insight into the nature of a newly described thyroid-ANP interaction. |
| Databáze: | OpenAIRE |
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