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 |
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Sprache: | eng |
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Zusammenfassung: | 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. |
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ISSN: | 0006-2952 1873-2968 |
DOI: | 10.1016/0006-2952(90)90502-C |