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

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...

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Veröffentlicht in:Biochemical pharmacology 1990-09, Vol.40 (5), p.1125-1129
Hauptverfasser: Ruriko, Mamune-Sato, Yasuo, Tanno, Kazutaka, Maeyama, Yasuko, Miura, Tamotsu, Takishima, Kenji, Kishi, Takeaki, Fukuda, Takehiko, Watanabe
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container_end_page 1129
container_issue 5
container_start_page 1125
container_title Biochemical pharmacology
container_volume 40
creator Ruriko, Mamune-Sato
Yasuo, Tanno
Kazutaka, Maeyama
Yasuko, Miura
Tamotsu, Takishima
Kenji, Kishi
Takeaki, Fukuda
Takehiko, Watanabe
description 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 α-fluoromethylhistidine but not by carbidopa, was unable to form dopamine from l-3, 4-dihydroxyphenylalanine, and had a K m 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.
doi_str_mv 10.1016/0006-2952(90)90502-C
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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 α-fluoromethylhistidine but not by carbidopa, was unable to form dopamine from l-3, 4-dihydroxyphenylalanine, and had a K m 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.</abstract><cop>New York, NY</cop><pub>Elsevier Inc</pub><pmid>2117926</pmid><doi>10.1016/0006-2952(90)90502-C</doi><tpages>5</tpages></addata></record>
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subjects Alkaloids - pharmacology
basophilic leukemia
Biological and medical sciences
Calcimycin - pharmacology
Carboxy-Lyases - metabolism
Carcinogenesis, carcinogens and anticarcinogens
Chemical agents
Cycloheximide - pharmacology
Enzyme Induction - drug effects
Histidine Decarboxylase - metabolism
Humans
Leukemia, Basophilic, Acute - enzymology
Leukemia, Basophilic, Acute - metabolism
Medical sciences
phorbol 12-myristate 13-acetate diester
Protein Kinase C - antagonists & inhibitors
Staurosporine
Tetradecanoylphorbol Acetate - pharmacology
Tumor Cells, Cultured - drug effects
Tumors
title Histidine decarboxylase in human basophilic leukemia (KU-812-F) cells: Characterization and induction by phorbol myristate acetate
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