Morita A, Tsao D, Kim Y S
Cancer Res. 1982 Nov;42(11):4540-5.
Treatment of the human rectal cancer cell line HRT-18 with sodium butyrate caused a reversible elevation of alkaline phosphatase activity which was inhibited by cycloheximide and actinomycin D. The alkaline phosphatase in untreated cells was heat stable at neutral pH and inhibited by phenylalanine but not by homoarginine, and 80% of the enzyme activity was precipitated by antibody against human term-placental enzyme. Following butyrate treatment, the enzyme became more sensitive to all the inhibitors tested and more heat stable, compared to the enzyme in control cells. In addition, the butyrate-induced enzyme could be completely precipitated by anti-placental alkaline phosphatase antibody. The electrophoretic pattern of the butyrate-induced enzyme was different from that of control cells. Control HRT-18 cells contained a butyrate-insensitive heat-labile alkaline phosphatase component with an electrophoretic mobility similar to the enzyme from human colon cancer tissues. The alkaline phosphatase from four human colon cancer tissues was of the early placental form, while the enzyme from human normal mucosa was of the intestinal type.
用丁酸钠处理人直肠癌细胞系HRT - 18会导致碱性磷酸酶活性可逆性升高，这种升高受到环己酰亚胺和放线菌素D的抑制。未处理细胞中的碱性磷酸酶在中性pH下对热稳定，受苯丙氨酸抑制但不受高精氨酸抑制，并且80%的酶活性可被抗人足月胎盘酶的抗体沉淀。丁酸钠处理后，与对照细胞中的酶相比，该酶对所有测试抑制剂更敏感且对热更稳定。此外，丁酸钠诱导的酶可被抗胎盘碱性磷酸酶抗体完全沉淀。丁酸钠诱导的酶的电泳图谱与对照细胞不同。对照HRT - 18细胞含有一种对丁酸钠不敏感的热不稳定碱性磷酸酶成分，其电泳迁移率与人结肠癌组织中的酶相似。来自四个人结肠癌组织的碱性磷酸酶是早期胎盘型，而来自人正常黏膜的酶是肠型。
