Protein Tyrosine Kinase Modulates Parathyroid Hormone Induced Cyclic AMP Production in Rat Osteosarcoma MSK Cells.

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We examined the osteoblastic and oncological properties of the established rat osteosarcoma cell line MSK with respect to 1) cyclic AMP (cAMP) production and alkaline phosphatase (ALPase) activity, and 2) the interaction of protein tyrosine kinase activity with parathyroid hormone (PTH)-response. The ALPase activity increased with time in culture medium and was reduced by PTH in a dose dependent manner. The content of cAMP in the cells was dose-dependently increased with the addition of PTH and conspicously enhanced to a maximum of 180 times at 5 min with 0.2 mM 3-isobutyl-1-methyl-xanthine. This response was suppressed by 6-hour pretreatment of the cells with 1, 25 dehydroxyvitamin D3. Responses to other bone metabolic hormones such as calcitonin and prostaglandin E2 were negligible compared to the controls.<BR>MSK cells possessed significantly high protein tyrosine kinase (PTK) activity, which was inhibited dose-dependently by ST638 (ST), a PTK specific inhibitor, both in cells <I>in vitro</I> and in the membrane fraction component of the cells. PTH itself did not elevate the PTK activity.
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