Yc. Li et al., Luteolin-inhibited arylamine N-acetyltransferase activity and DNA-2-aminofluorene adduct in human and mouse leukemia cells, FOOD CHEM T, 39(7), 2001, pp. 641-647
N-Acetyltransferase enzyme is an important enzyme in the first step of aryl
amine compounds metabolism. Luteolin has been shown to exit antibacterial a
nd antineoplastic activity. The purpose of this present study is to evaluat
e the question of whether luteolin could affect arylamine N-acetyltransfera
se (NAT) activity and DNA-2-aminofluorene adduct formation in human (HL-60)
and mouse (L1210) leukemia cells. By using HPLC, N-acetylation of 2-aminof
luorene wase determined. Luteolin displayed a dose-dependent inhibition to
cytosolic NAT activity and intact human and mice leukemia cells. Time-cours
e experiments showed that N-acetylation or 2-aminofluorene measured from in
tact human and mice leukemia cells were inhibited by luteolin for up to 24
hours. Using standard steady-state kinetic analysis, it was demonstrated th
at luteolin was a possible uncompetitive inhibitor to NAT activity in cytos
ols. The DNA-2-aminofluorene adduct formation in human and mouse leukemia c
ells were inhibited by luteolin. This report is the first demonstration to
show that luteolin affects human and mice leukemia cells NAT activity and D
NA-2-aminofluorene on adduct formation. (C) 2001 Elsevier Science Ltd. All
rights reserved.