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J Biol Chem, Vol. 275, Issue 5, 3081-3087, February 4, 2000

Tumor Necrosis Factor alpha  Up-regulates in an Autocrine Manner the Synthesis of Plasminogen Activator Inhibitor Type-1 during Induction of Monocytic Differentiation of Human HL-60 Leukemia Cells*

Sophie LopezDagger , Franck Peiretti, Bernadette Bonardo, Irène Juhan-Vague, and Gilles Nalbone§

From the INSERM EPI 99-36, Laboratoire d'Hématologie, Faculté de Médecine, 27 Bd. Jean Moulin, 13385 Marseille Cedex 5, France

Tumor necrosis factor-alpha (TNFalpha ) critically regulates several cellular functions during monocyte/macrophage differentiation. We therefore investigated during the phorbol ester (phorbol 12-myristate 13-acetate (PMA))-induced monocyte/macrophage differentiation of the human HL-60 leukemia cells, if TNFalpha contributed to plasminogen activator inhibitor type-1 (PAI-1) synthesis that is initiated by a protein kinase Cbeta -extracellular signal-regulated kinase 2-dependent pathway (Lopez, S., Peiretti, F., Morange, P., Laouar, A., Fossat, C., Bonardo, B., Huberman, E., Juhan-Vague, I., and Nalbone, G. (1999) Thromb. Haemostasis 81, 415-422). Following PMA treatment, the level of TNFalpha mRNA strongly increased and appeared earlier than PAI-1 mRNA. An anti-TNFalpha antibody significantly inhibited the PMA-induced PAI-1 mRNA and protein levels. The recombinant human TNFalpha , which is inactive on native HL-60 cells in terms of PAI-1 synthesis, optimally potentiates it once HL-60 cells are committed into the differentiation process. The use of 1) the HL-525 cell line, a clone issued from HL-60 cells rendered resistant to PMA-induced differentiation, and 2) the transforming growth factorbeta -1/vitamin D3 differentiative mixture confirmed the relationships between the induction of differentiation and the potency of TNFalpha to up-regulate PAI-1 synthesis. In conclusion, we showed that during the induction of monocyte/macrophage differentiation, TNFalpha and PAI-1 gene expressions are activated and that synthesized TNFalpha up-regulates and prolongs, in an autocrine manner, the synthesis of PAI-1.

* This work was supported by funds of INSERM and Université de la Méditerranée.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Recipient of funds from Groupe d'Etudes en Hémostase et Thrombose-Sanofi and from the Fondation pour la Recherche Médicale.

§ To whom correspondence should be addressed: EPI 99-36, Laboratoire d'Hématologie, Faculté de Médecine, 27 Bd. Jean Moulin, 13385 Marseille Cedex 5, France. Tel.: (33) 4 91 32 45 07; Fax: (33) 4 91 25 43 36; E-mail: Gilles.Nalbone@medecine.univ-mrs.fr.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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