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

Biochemical Pharmacology
R Mamune-SatoT Watanabe

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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Citations

Dec 7, 2002·Chemical Record : an Official Publication of the Chemical Society of Japan ... [et Al.]·Takehiko Watanabe, Hiroshi Ohtsu
Jan 6, 2009·The Journal of Allergy and Clinical Immunology·Laura MaintzNatalija Novak
Aug 22, 2000·The Journal of Investigative Dermatology·M Haak-FrendschoA Falus
Dec 13, 2017·Theoretical Biology & Medical Modelling·Janet BestMichael Reed
Dec 22, 1995·The Journal of Biological Chemistry·K YatsunamiT Higuchi
Aug 12, 1998·The American Journal of Physiology·C A ZahnowD E Millhorn

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