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Category:Science and technology-related listsInhibitory effects of Picroside II on protein phosphorylation in mouse hepatoma cells.
In mouse hepatoma cells, tumor-promoting phorbol esters can induce the phosphorylation of a number of proteins, including those of 80-, 66-, and 62-kDa molecular weights (PTP-80, -66, and -62) and the non-high-affinity state of phosphatidylinositol (PI) phospholipase C (PIPLC). Here we have investigated the effect of Picroside II (an active component of pomegranate) on the phosphorylation of these proteins. Picroside II (0.01-1 micrograms/ml) inhibited the phorbol ester-induced phosphorylation of PTP-66, -80, and -62, but did not significantly affect the phosphorylation of PIPLC. The protein kinase C inhibitor, H7, caused a concentration-dependent inhibition of the phosphorylation of PTP-80, PTP-66, and PIPLC. Pretreatment with Picroside II (0.1-1 micrograms/ml) prevented the inhibition of PIPLC phosphorylation by H7, but did not alter the inhibitory effect of H7 on the phosphorylation of PTP-80 and -66. The results indicate that the inhibition of the phorbol ester-induced phosphorylation of PTP-66, -80, and -62 by Picroside II is not likely to result from its direct inhibition of protein be359ba680
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