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Negative Regulation by Protein Tyrosine Phosphatase of IFN--Dependent Expression of Inducible Nitric Oxide Synthase¹

Instituto de Bioquímica (Consejo Superior de Investigaciones Cientificas-UCM), Facultad de Farmacia, Universidad Complutense de Madrid, Madrid, Spain

Treatment of cultured peritoneal macrophages with IFN- resulted in tyrosine phosphorylation of IB and IBß, NF-B activation, and expression of inducible NO synthase (iNOS). Since tyrosine phosphorylation of IB is sufficient to activate NF-B in Jurkat cells, macrophages were treated with the protein tyrosine phosphatase inhibitor peroxovanadate (POV), which elicited an intense tyrosine phosphorylation of both IB. However, this phosphorylation failed to activate NF-B. Treatment with POV of macrophages stimulated with IFN- or LPS potentiated the degradation of IB and IBß, the activation of NF-B, and the expression of iNOS. Analysis of the iNOS gene promoter activity corresponding to the 5'-flanking region indicated that POV potentiates the cooperation between IFN--activated transcription factors and NF-B. These results indicate that tyrosine phosphorylation of IB is not sufficient to activate NF-B in macrophages and propose a negative role for protein tyrosine phosphatase in the expression of iNOS in response to IFN-.

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