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J. Biol. Chem., Vol. 277, Issue 37, 34610-34617, September 13, 2002

This Article Full Text Full Text (PDF) All Versions of this Article: 277/37/34610    most recent M203616200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Mackenzie, G. G. Articles by Oteiza, P. I. Search for Related Content PubMed PubMed Citation Articles by Mackenzie, G. G. Articles by Oteiza, P. I. Social Bookmarking                      What's this?

Low Intracellular Zinc Impairs the Translocation of Activated NF-B to the Nuclei in Human Neuroblastoma IMR-32 Cells^*

Gerardo G. Mackenzie^§, M. Paola Zago^¶, Carl L. Keen^**, and Patricia I. Oteiza

From the  Departamento de Química Biológica, Instituto de Química y Físicoquímica Biológicas (Universidad de Buenos Aires, Consejo Nacional de Investigaciones Científicas y Técnicas), Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, C1113AAD, Buenos Aires, Argentina and the  Departments of Nutrition and ^** Internal Medicine, University of California, Davis, California 95616

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

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