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NADPH oxidase is involved in H 2 O 2 ‐induced differentiation of human promyelocytic leukaemia HL‐60 cells
Author(s) -
Lin Changjun,
Wang Huan
Publication year - 2012
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1042/cbi20110290
Subject(s) - apocynin , nadph oxidase , chemistry , mapk/erk pathway , cellular differentiation , microbiology and biotechnology , superoxide , intracellular , reactive oxygen species , extracellular , signal transduction , kinase , biochemistry , biology , enzyme , gene
The expression and activity of NADPH oxidase increase when HL‐60 cells are induced into terminally differentiated cells. However, the function of NADPH oxidase in differentiation is not well elucidated. With 150–500 μM H 2 O 2 inducing differentiation of HL‐60 cells, we measured phagocytosis of latex beads and investigated cell electrophoresis. Two inhibitors of NADPH oxidase, DPI (diphenyleneiodonium) and APO (apocynin), blocked the differentiation potential of cells induced by 200 μM H 2 O 2 . However, H 2 O 2 stimulated the generation of intracellular superoxide (O 2 • − ), which decreased in the presence of the two inhibitors. DPI also inhibited H 2 O 2 ‐induced ERK (extracellular‐signal‐regulated kinase) activation, as detected by Western blotting. Furthermore, PD98059, the inhibitor of the ERK pathway, inhibited the differentiation of HL‐60 cells induced by H 2 O 2 . This shows that H 2 O 2 can activate NADPH oxidase, leading to O 2 • − production, followed by ERK activation and ultimately resulting in the differentiation of HL‐60 cells. The data indicate that NADPH oxidase is an important cell signal regulating cell differentiation.