Inhibition of protein phosphatase 1 decreases PTH secretion from isolated dispersed parathyroid cells
| Autor: | Jean F. Schaefer, Steven S. Rhee, Lisa M. Matovcik, Barbara K. Kinder, Edgar F. da Cruz e Silva |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
medicine.medical_specialty
Cell Membrane Permeability Phosphatase Parathyroid hormone Biology Biochemistry Parathyroid Glands chemistry.chemical_compound Endocrinology Protein Phosphatase 1 Internal medicine Okadaic Acid Phosphoprotein Phosphatases medicine Animals Humans Secretion Molecular Biology Protein phosphatase 1 Parathyroid chief cell Okadaic acid Molecular biology chemistry Parathyroid Hormone Streptolysins Parathyroid hormone secretion Calcium Cattle Cell fractionation hormones hormone substitutes and hormone antagonists Subcellular Fractions |
| Zdroj: | Molecular and Cellular Endocrinology. 154:171-177 |
| ISSN: | 0303-7207 |
| Popis: | To investigate the regulation of parathyroid hormone secretion by phosphatases we examined the effect of okadaic acid, a selective inhibitor of protein phosphatases (PP)-1 and -2A, on isolated, dispersed parathyroid cells. Okadaic acid inhibited secretion from intact bovine, intact human and streptolysin-O permeabilized bovine cells. Approximately 10(-6) M okadaic acid resulted in a 50% decrease in parathyroid hormone (PTH) secretion from both intact and permeabilized cells, consistent with PP-1 being the target of inhibition. Upon subcellular fractionation, PP-1 overlapped but was not identical to either PTH, a marker of the secretory granule, or Na+/K+-ATPase, a plasma membrane marker. In summary, PP-1 activity is involved in Ca2+-dependent but not basal PTH secretion. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect