Induction of histidine decarboxylase of rat basophilic leukemia (2H3) cells stimulated by higher oligomeric IgE or phorbol myristate acetate.
Induction of histidine decarboxylase of rat basophilic leukemia (2H3) cells stimulated by higher oligomeric IgE or phorbol myristate acetate.
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由较高寡聚 IgE 或佛波醇肉豆蔻酸酯乙酸酯刺激的大鼠嗜碱性白血病 (2H3) 细胞诱导组氨酸脱羧酶。
DOI:
10.1016/s0006-291x(88)80518-7
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发表时间:
1988
影响因子:
3.1
通讯作者:
Takehiko Watanabe
中科院分区:
文献类型:
--
作者:
Kazutaka Maeyama;Y. Taguchi;M. Sasaki;Hiroshi Wada;M. A. Beaven;Takehiko Watanabe
When rat basophilic leukemia (2H3) cells were stimulated by higher oligomer, the chemically cross-linked oligomers of IgE, in the presence of calcium the activity of histidine decarboxylase (HDC, L-histidine carboxylyase, E.C.4.1.1.22), a histamine-forming enzyme, was increased by 1 hr, reaching maximum activity by 2 hr, and returning to the original level by 8 hr. A similar increase in enzyme activity was observed in cells treated with phorbol myristate acetate (PMA) or oleoyl-acetylglycerol (OAG), which are known activators of protein kinase C. Removal of calcium from medium abolished the increase in HDC activity in response to higher oligomer but not that induced by PMA or OAG, suggesting that the increase in HDC activity may be mediated by protein kinase C. The increase in the HDC activity probably required induction of enzyme synthesis, because it was prevented by cycloheximide.