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J.Health Sci., 50(3), 296-300, 2004
Activation of a 36-kDa Myelin Basic Protein Kinase during
Cadmium-Induced Apoptosis in Human Leukemia HL-60 Cells
Masuo Kondoh,a Yoshiteru
Watanabe,a and Masao Sato*, b
aDepartment of Pharmaceutics and Biopharmaceutics, Showa
Pharmaceutical University, 3165-3,
Higashi-tamagawa-gakuen, Machida, Tokyo 194-8543, Japan and
bDepartment of Public Health, Faculty of Pharmaceutical Sciences, Tokushima
Bunri University, 180, Bouji, Nishihama, Yamashiro-cho,
Tokushima 770-8514, Japan
Cadmium (Cd) is a well-known modulator of
intracellular signal transduction including
mitogen-activated protein kinases and protein kinase C. In this
study, we investigated activation of a kinase using
myelin basic protein (MBP) as a substrate during
Cd-induced apoptosis in human leukemia HL-60 cells. To
detect a kinase during Cd-induced apoptosis in HL-60
cells, we performed an in-gel kinase assay using MBP
as a substrate and found that Cd induced the
activation of a kinase with an apparent molecular mass of
36 kDa. The time-course of appearance of DNA ladders induced by Cd was consistent with that of
activation of this kinase. The kinetics of activation of p36
MBP kinase was different from that of p38 mitogen-activated protein kinase (p38MAPK). Activation of p36
MBP kinase was also observed with kinetics distinct
from that of activation of p38MAPK during mercuric
chloride-induced apoptosis. This is the first report on
activation of p36 MBP kinase during Cd- or Hg-induced apoptosis.
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