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Blood, Vol. 95 No. 7 (April 1), 2000:
pp. 2391-2396
Butyrate-induced erythroid differentiation of human K562
leukemia cells involves inhibition of ERK and activation of p38 MAP
kinase pathways
Olaf Witt,
Katrin Sand, and
Arnulf Pekrun
From the Children's Hospital, University of Göttingen,
Göttingen, Germany.
Butyrate induces cytodifferentiation in many tumor cells of
different origin, suggesting that an as yet unidentified common mechanism inherent to malignant cells is the target of butyrate action.
This study determined the role of different mitogen-activated protein
(MAP) kinase signal transduction pathways in butyrate-induced erythroid
differentiation of K562 human leukemia cells. Using a panel of
anti-ERK, JNK, and p38 phosphospecific antibodies, the study showed
that phosphorylation of ERK and JNK is decreased following treatment of
cells with butyrate, whereas phosphorylation of p38 is increased.
In contrast, a K562 subline defective in butyrate-mediated
induction of erythroid differentiation did not reveal these changes in
phosphorylation patterns. Inhibition of ERK activity by UO126 induces
erythroid differentiation and acts synergistically with butyrate on
hemoglobin synthesis and inhibition of cell proliferation, whereas
inhibition of p38 activity by SB203580 completely abolished
induction of hemoglobin expression by butyrate. Taken together,
our data suggest a model in which butyrate induces erythroid differentiation of K562 cells by inhibition of ERK and activation of p38 signal transduction pathways.
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