Abstract

This enzyme activity was examined in bone cells cultured for 8–10 days; the calcium concentration was 1.87 ± 0.05 ( n = 10) mM in the control medium and 0.34 ± 0.02 ( n = 10) mM in the low-calcium medium. The activity was significantly lower in the low-calcium group than in the control ( p < 0.01). The cytosolic fraction decreased more than the membranous fraction. After restoration to a regular calcium environment, the protein kinase C activity recovered rapidly to near the control value. The extent of recovery was greater in the membranous than in the cystolic fraction. These results suggest that the enzyme was inhibited in bone cells placed in a low-calcium environment, while the sensitivity in the membrane was enhanced.

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