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M203616200v1
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Papers In Press, published online ahead of print June 27, 2002
J. Biol. Chem, 10.1074/jbc.M203616200
Submitted on April 15, 2002
Revised on June 25, 2002
Accepted on June 27, 2002

Low intracellular zinc impairs the translocation of activated NF-kappa B to the nuclei in human neuroblastoma IMR-32 cells

Gerardo G. Mackenzie, M. Paola Zago, Carl L. Keen, and Patricia I. Oteiza

Department of Biological Chemistry, University of Buenos Aires, Buenos Aires C1113ADD

Corresponding Author: oteiza{at}qb.ffyb.uba.ar

In the current work, we studied how variations in extracellular zinc concentrations modulate different steps involved in NF-kappa B activation in human neuroblastoma IMR-32 cells. Cells were incubated in media containing varying concentrations of zinc (1.5, 5, 15 and 50 mu M). Within 3h, the intracellular zinc content was lower in cells exposed to 1.5 and 5 mu M, compared to the other groups. Low intracellular zinc concentrations were associated with the activation of NF-kappa B, based on high levels of Ikappa Balpha phosphorylation, low Ikappa Balpha concentrations, and high NF-kappa B binding activity in total cell fractions. However, the active dimer accumulated in the cytosol, as shown by a low ratio of nuclear/cytosolic NF-kappa B binding activity. This altered nuclear translocation was accompanied by a decreased transactivation of an endogenous NF-kappa B-driven gene (ikba) and of a reporter gene (pNF-kappa B-luc). In cells with low intracellular zinc concentrations, a low rate of in vitro tubulin polymerization was measured compared to the other groups. We conclude that low intracellular zinc concentrations induces tubulin depolymerization, which may be one signal for NF-kappa B activation. However, NF-kappa B nuclear translocation is impaired, which inhibits the transactivation of NF-kappa B-driven genes. This could affect cell survival, and be an important factor in certain zinc-deficiency-associated pathologies.


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