INHIBITION OF 12-O-TETRADECANOYLPHORBOL-13-ACETATE-STIMULATED (PI)-P-32 INCORPORATION INTO PHOSPHOLIPIDS AND PROTEIN-PHOSPHORYLATION BY 2,7,11-CEMBRATRIENE-4,6-DIOL, AN ANTI-TUMOR-PROMOTING AGENT
INHIBITION OF 12-O-TETRADECANOYLPHORBOL-13-ACETATE-STIMULATED (PI)-P-32 INCORPORATION INTO PHOSPHOLIPIDS AND PROTEIN-PHOSPHORYLATION BY 2,7,11-CEMBRATRIENE-4,6-DIOL, AN ANTI-TUMOR-PROMOTING AGENT
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DOI:
10.1159/000226545
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发表时间:
1988-03-01
期刊:
影响因子:
3.5
通讯作者:
OHNISHI, A
中科院分区:
文献类型:
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作者:
SAITO, Y;NISHINO, H;OHNISHI, A
A possible mechanism of antitumor-promoting activity of .alpha.-2,7,11-cembratriene-4,6-diol (.alpha.-CBT) was studied. .alpha.-CBT inhibited the 32Pi incorporation into phospholipids of HeLa cells stimulated by 12-O-tetradecanolyphorbol-13-acetate (TPA). In contrast to the property to interact with calmodulin of many other antitumor-promoting agents, which were proved to inhibit TPA-stimulated. 32Pi incorporation into phospholipids, .alpha.-CBT did not show any interaction with calmodulin; i.e., the fluorescence of N-phenyl-1-naphthylamine enhanced by binding with Ca+-calmodulin was not influenced by treatment with .alpha.-CBT. TPA-stimulated phosphorylation of 47-kilodation protein, which is phosphorylated by protein kinase C in human platelets, was found to be inhibited by .alpha.-CBT. However, the specific binding of 3H-TPA to mouse epidermal pariculate fraction was not inhibited by treatment with .alpha.-CBT. These results suggest that .alpha.-CBT inhibits the activity of protein kinase C by another mode of action rather than the effect on its receptor site, and that this action and calmodulin-independent inhibitiory effect on phospholipid metabolism of .alpha.-CBT may play a certain role in its antitumor-promoting activity in vivo.