| Autor: |
Forrest, S., Ng, K., Findlay, D., Michelangeli, V., Livesey, S., Partridge, N., Zajac, J., Martin, T., Forrest, S M, Ng, K W, Findlay, D M, Michelangeli, V P, Livesey, S A, Partridge, N C, Zajac, J D, Martin, T J |
| Předmět: |
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| Zdroj: |
Calcified Tissue International; 1985, Vol. 37 Issue 1, p51-56, 6p |
| Abstrakt: |
The clonal cell line UMR 106, which was originally derived from a rat transplantable osteogenic sarcoma with an osteoblastic phenotype, was subcloned after the emergence of a calcitonin-responsive adenylate cyclase was noted in late passages. Detailed studies on the stimulation of adenylate cyclase and activation profile of the cyclic AMP-dependent protein kinase isoenzymes in response to parathyroid hormone (PTH) and salmon calcitonin (SCT) were conducted on two subclones (UMR 106-01 and UMR 106-06). Both subclones responded in an identical manner to PTH, which stimulated adenylate cyclase and activated both isoenzyme I and isoenzyme II of cyclic AMP-dependent protein kinase. In contrast, only UMR 106-06 cells responded to calcitonin. At 3 X 10(-8)M SCT, there was a sevenfold stimulation of adenylate cyclase, 84% activation of isoenzyme I, and 44% activation of isoenzyme II. The activation profiles of the isoenzymes to PTH and SCT in UMR 106-06 were similar. Furthermore, their response to SCT correlates with the presence of specific, saturable binding of 125I-labeled SCT. Binding parameters indicate apparent Kd = 0.8 nM and 6,000 receptors/cell. These data point to a significant phenotypic change having taken place in this clonal cell line with prolonged maintenance in culture, with the emergence of a calcitonin receptor linked to adenylate cyclase and protein kinase activation. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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