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J Biol Chem, Vol. 274, Issue 14, 9539-9547, April 2, 1999

Tumor Necrosis Factor-alpha Mediates Both Apoptotic Cell Death and Cell Proliferation in a Human Hematopoietic Cell Line Dependent on Mitotic Activity and Receptor Subtype Expression

Gregory T. BaxterDagger , Richard C. Kuo, Orla J. Jupp**, Peter VandenabeeleDagger Dagger , and David J. MacEwan**

From the Dagger  Cornell Nanofabrication Facility, Cornell University, Ithaca, New York 14853, the  Neurosciences Program, Stanford University School of Medicine, Stanford, California 94305, the ** Department of Biomedical Sciences, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD, United Kingdom, and the Dagger Dagger  Department of Molecular Biology, Flanders Interuniversity Institute for Biotechnology, University of Gent, Ledeganckstraat 35, B-9000 Ghent, Belgium

The TF-1 human erythroleukemic cell line exhibits opposing physiological responses toward tumor necrosis factor-alpha (TNF) treatment, dependent upon the mitotic state of the cells. Mitotically active cells in log growth respond to TNF by rapidly undergoing apoptosis whereas TNF exposure stimulates cellular proliferation in mitotically quiescent cells. The concentration-dependent TNF-induced apoptosis was monitored by cellular metabolic activity and confirmed by both DNA epifluorescence and DNA fragmentation. Moreover, these responses could be detected by measuring extracellular acidification activity, enabling rapid prediction (within ~ 1.5 h of TNF treatment) of the fate of the cell in response to TNF. Growth factor resupplementation of quiescent cells, resulting in reactivation of cell cycling, altered TNF action from a proliferative stimulus to an apoptotic signal. Expression levels of the type II TNF receptor subtype (p75TNFR) were found to correlate with sensitivity to TNF-induced apoptosis. Pretreatment of log growth TF-1 cells with a neutralizing anti-p75TNFR monoclonal antibody inhibited TNF-induced apoptosis by greater than 80%. Studies utilizing TNF receptor subtype-specific TNF mutants and neutralizing antisera implicated p75TNFR in TNF-dependent apoptotic signaling. These data show a bifunctional physiological role for TNF in TF-1 cells that is dependent on mitotic activity and controlled by the p75TNFR.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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