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Volume 272, Number 13, Issue of March 28, 1997 pp. 8172-8178
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Characterization of the Promoter for the Human Long Pentraxin PTX3
ROLE OF NF-kappa B IN TUMOR NECROSIS FACTOR-alpha AND INTERLEUKIN-1beta REGULATION

(Received for publication, November 19, 1996, and in revised form, January 23, 1997)

Andrea Basile Dagger , Antonio Sica Dagger , Elisabetta d'Aniello Dagger , Ferruccio Breviario Dagger , Gabino Garrido Dagger , Marina Castellano Dagger , Alberto Mantovani Dagger § and Martino Introna Dagger

From the Dagger  Istituto di Ricerche Farmacologiche "Mario Negri," via Eritrea, 62, 20157 Milan, Italy and the § Section of General Pathology and Immunology, University of Brescia, 25123 Brescia, Italy

The "long pentraxins" are an emerging family of genes that have conserved in their carboxy-terminal halves a pentraxin domain homologous to the prototypical acute phase protein pentraxins (C-reactive protein and serum amyloid P component) and acquired novel amino-terminal domains. In this report, a genomic fragment of 1371 nucleotides from the human "long pentraxin" gene PTX3 is characterized as a promoter on tumor necrosis factor-alpha (TNFalpha ) and interleukin (IL)-1beta exposure in transfected 8387 human fibroblasts by chloramphenicol acetyltransferase and RNase protection assays. In the same cells, the PTX3 promoter does not respond to IL-6 stimulation. Furthermore, IL-1beta and TNFalpha responsiveness is not seen in the Hep 3B hepatoma cell line. The minimal promoter contains one NF-kappa B element which is shown to be necessary for induction and able to bind p50 homodimers and p65 heterodimers but not c-Rel. Mutants in this site lose the ability to bind NF-kappa B proteins and to respond to TNFalpha and IL-1beta in functional assays. Sp1- and AP-1 binding sites lying in proximity to the NF-kappa B site do not seem to play a major role for cytokine responsiveness. Finally, cotransfection experiments with expression vectors validate that the natural promoter contains a functional NF-kappa B site.


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