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J Biol Chem, Vol. 274, Issue 41, 28978-28982, October 8, 1999

Activation of Jun N-terminal Kinase/Stress-activated Protein Kinase Pathway by Tumor Necrosis Factor  Leads to Intercellular Adhesion Molecule-1 Expression

Paola De Cesaris, Donatella Starace, Giuseppe Starace^§, Antonio Filippini, Mario Stefanini, and Elio Ziparo

From the Istituto Pasteur-Fondazione Cenci Bolognetti, Department of Histology and Medical Embryology, University of Rome "La Sapienza," 00161 Rome, Italy, the  Department of Experimental Medicine, University of L'Aquila, and ^§ Institute of Experimental Medicine, CNR, Rome, Italy

Tumor necrosis factor  (TNF-) is a cytokine implicated in the pathogenesis of numerous chronic and acute inflammatory conditions. We have previously shown that mouse Sertoli cells respond to TNF- by increasing interleukin-6 production and intercellular adhesion molecule-1 (ICAM-1) expression (1). In this cell type TNF- activates the mitogen-activated protein kinase (MAPK) pathways p42/p44 MAPK, JNK/SAPK, and p38, the last of which is responsible for interleukin-6 production (2). To determine which MAPK signaling pathway is required for TNF- induction of ICAM-1 expression, we have utilized the protein kinase inhibitor dimethylaminopurine, demonstrating that treatment of Sertoli cells with such compound significantly reduced ICAM-1 expression and JNK/SAPK activation. Moreover, dimethylaminopurine treatment increased the expression of MAPK phosphatase-2, providing a possible mechanism of action of this compound. By using agonist antibodies to p55 and to p75 TNF- receptors and both human and mouse TNF-, we demonstrate that both TNF receptors are expressed and that only the p55 receptor is involved in ICAM-1 expression. The p55 receptor activates all of the three pathways, whereas p75 failed to activate any of the MAPKs. Altogether our results demonstrate that TNF- up-regulates ICAM-1 expression through the activation of the JNK/SAPK transduction pathway mediated by the p55 receptor.

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