Abstract
Placental alkaline phosphatase activity and immunoreactivity were inhibited in a parallel fashion in choriocarcinoma cells by tunicamycin, a protein glycosylation inhibitor. Tunicamycin suppressed placental alkaline phosphatase biosynthesis in addition to inhibiting protein glycosylation in general. An anti-placental alkaline phosphatase-precipitable polypeptide of 58,000 daltons was formed in the presence of this antibiotic. The 58,000-dalton polypeptide had a degradation rate similar to that of the glycosylated phosphatase monomer from control cultures. Tunicamycin suppressed placental alkaline phosphatase mRNA activity leading to the observed decrease in biosynthesis.
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