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Cell Growth & Differentiation Vol. 10, 307-315, May 1999
© 1999 American Association for Cancer Research

Phorbol Ester-induced Mononuclear Cell Differentiation Is Blocked by the Mitogen-activated Protein Kinase Kinase (MEK) Inhibitor PD980591

Hongchin He, Xiantao Wang, Myriam Gorospe, Nikki J. Holbrook and Michael A. Trush2

Division of Toxicological Sciences, Department of Environmental Health Sciences, School of Hygiene and Public Health, The Johns Hopkins University, Baltimore, Maryland 21205 [H. H., M. A. T.], and Gene Expression and Aging Section, National Institute on Aging, NIH, Baltimore, Maryland 21224 [X. W., M. G., N. J. H.]

The purpose of this study was to evaluate whether the mitogen-activated protein kinase (MAPK) signaling pathway contributes to 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced mononuclear differentiation in the human myeloblastic leukemia ML-1 cells. Upon TPA treatment, the activity of ERK1 and ERK2 rapidly increased, with maximal induction between 1 and 3 h, while ERK2 protein levels remained constant. The activity of JNK1 was also significantly induced, with JNK1 protein levels increasing moderately during exposure to TPA. Treatment of cells with PD98059, a specific inhibitor of mitogen-activated protein kinase kinase (MEK), inhibited TPA-induced ERK2 activity. Furthermore, PD98059 completely blocked the TPA-induced differentiation of ML-1 cells, as assessed by a number of features associated with mononuclear differentiation including changes in morphology, nonspecific esterase activity, phagocytic ability, NADPH oxidase activity, mitochondrial respiration, and c-jun mRNA inducibility. We conclude that activation of the MEK/ERK signaling pathway is necessary for TPA-induced mononuclear cell differentiation.




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Molecular Cancer Research Cell Growth & Differentiation
Copyright © 1999 by the American Association of Cancer Research.