Inhibitory effect of monensin on secretion of tissue plasminogen activator.

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Tissue plasminogen activator (t-PA), which has high affinity to fibrin, is secreted into culture medium from a human melanoma cell line (Bowes). The mechamism of t-PA secretion remains still unclear. Since t-PA is glycoprotein, effect of monensin on the secretion of t-PA was investigated using two series of experiment. In both series, monensin was added to the medium 4 hours before the experiment. In A series, monensin was further added during the experimantal (sampling) period (6 hours). In B series, monensin was not added during the sampling period in order to observe withdrawal effect of monensin. The results showed that, in A series, the secretion of t-PA was markedly depressed in 0.1, 1 and 10μM monensin and the intracellular t-PA was accumulated as twice as control. In B series, the secretion of t-PA was suppressed in a dose-dependent manner, and the intracellular t-PA was accumulated further in 10μM, but decreased in 1μM. Monensin inhibited DNA, RNA, and pretein syntheses in a dose-dependent manner in both A and B series. The effects of monensin on the release of previously produced protein showed that monensin increased protein release. The results obtained in the present study indicated that monensin disturbed intracellular transport system of t-PA in melanoma cell, as well as other glycosylated proteins.
一般社団法人日本血栓止血学会の論文