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Nucleic Acids Research, 1992, Vol. 20, No. 5 1061-1068
© 1992

MOLECULAR BIOLOGY

Analysis of proteins binding to the proximal promoter region of two rat serine protease inhibitor genes

Valerie Rossi, Jean Francois Rouayrenc, Laurent Paquereau, Marie Joseé Vilarem and Alphonse Le Cam*

Centre de Pharmacologie Endocrinologie, CNRS-INSERM, rue de la Cardonille 34094 Montpellier cedex 05, France

*To whom correspondence should be addressed

Received December 5, 1991. Revised January 31, 1992. Accepted January 31, 1992.

The three serine protease Inhibitor (SPI) rat genes expressed preferentially In liver share considerable structural features and, nonetheless, are transcriptlonally regulated in completely different manners, more particularly after hypophysectomy or upon acute inflammation. DNase I footprinting and gel mobility shift analyses of the SPI 2.1 and 2.3 proximal promoter regions reveal the presence of three common protein binding sites (1 to 3, 3' to 5') located immediately upstream from the transcription start site. C/EBP, the liver-enriched factor, specifically interacts with site 1 whereas its related proteins (e.g; DBP, LAP/NFIL6) most likely recognize sites 2 and 3. Another ubiquitous unidentified factor also binds to site 2. A liver-specific protein dependent on growth hormone, whose binding is competed out by an ollgonucleotide reproducing an HNF3 motif, interacts exclusively with site 3. The 42 bp sequence which is found only within the SPI 2.3 promoter interacts with two ubiquitous factors, one of which is related to NF{varkappa}B. Acute inflammation does not significantly affect the protein binding patterns observed with the SPI 2.1 or 2.3 proximal promoter sequences. Our results show an apparent discrepancy between the large magnitude of in vivo changes In SPI gene transcription mediated by hormones and the small alterations detected In vitro, in the DNA-protein interactions on the promoters.


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