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Mamune-Sato R, Tanno Y, Maeyama K, et al. Histidine decarboxylase in human basophilic leukemia (KU-812-F) cells. Characterization and induction by phorbol myristate acetate. Biochem Pharmacol. 1990;40(5):1125-9doi: 10.1016/0006-2952(90)90502-c.
Mamune-Sato, R., Tanno, Y., Maeyama, K., Miura, Y., Takishima, T., Kishi, K., Fukuda, T., & Watanabe, T. (1990). Histidine decarboxylase in human basophilic leukemia (KU-812-F) cells. Characterization and induction by phorbol myristate acetate. Biochemical pharmacology, 40(5), 1125-9. https://doi.org/10.1016/0006-2952(90)90502-c
Mamune-Sato, R, et al. "Histidine decarboxylase in human basophilic leukemia (KU-812-F) cells. Characterization and induction by phorbol myristate acetate." Biochemical pharmacology vol. 40,5 (1990): 1125-9. doi: https://doi.org/10.1016/0006-2952(90)90502-c
Mamune-Sato R, Tanno Y, Maeyama K, Miura Y, Takishima T, Kishi K, Fukuda T, Watanabe T. Histidine decarboxylase in human basophilic leukemia (KU-812-F) cells. Characterization and induction by phorbol myristate acetate. Biochem Pharmacol. 1990 Sep 01;40(5):1125-9. doi: 10.1016/0006-2952(90)90502-c. PMID: 2117926.
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Elsevier Science

Biochem Pharmacol. 1990 Sep 01;40(5):1125-9. doi: 10.1016/0006-2952(90)90502-c.

Histidine decarboxylase in human basophilic leukemia (KU-812-F) cells. Characterization and induction by phorbol myristate acetate.

Biochemical pharmacology

R Mamune-Sato, Y Tanno, K Maeyama, Y Miura, T Takishima, K Kishi, T Fukuda, T Watanabe

Affiliations

  1. First Department of Internal Medicine, Tohoku University School of Medicine, Sendai, Japan.

PMID: 2117926 DOI: 10.1016/0006-2952(90)90502-c

Abstract

The human leukemic cell line KU-812-F is known to differentiate into mature basophil-like cells under serum-free culture conditions. In the present study, the activity of histidine decarboxylase (HDC), a histamine-forming enzyme, in KU-812-F cells was found to be high, ranging from 10 to 57 pmol/min/mg protein. The great variation in HDC activity appeared to be due to different percentages and degrees of maturity of basophil-like cells during differentiation of this cell line. The enzyme was inhibited by alpha-fluoromethylhistidine but not by carbidopa, was unable to form dopamine from L-3,4-dihydroxyphenylalanine, and had a Km value for histidine of 0.27 mM, indicating that it was HDC and not aromatic amino acid decarboxylase. The HDC activity increased 1.8-fold when the cells were stimulated by phorbol myristate acetate, which is known to activate protein kinase C, and this increase was blocked by staurosporine, a potent inhibitor of protein kinase C.

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