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Originally published In Press as doi:10.1074/jbc.M202509200 on July 30, 2002

J. Biol. Chem., Vol. 277, Issue 41, 38579-38588, October 11, 2002
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Localization of Regulatory Elements Mediating Constitutive and Cytokine-stimulated Plasminogen Gene Expression*

Felizabel Garcia BannachDagger §, Ana GutierrezDagger , Bruce J. FowlerDagger , Thomas H. Bugge, Jay L. Degen||, Robert J. Parmer**, and Lindsey A. MilesDagger

From the Dagger  Department of Cell Biology, Division of Vascular Biology, Scripps Research Institute, La Jolla, California 92037, the  Oral and Pharyngeal Cancer Branch, NIDCR, National Institutes of Health, Bethesda, Maryland 20892, || Children's Hospital Research Foundation, Cincinnati, Ohio 45229, and the ** Department of Medicine, University of California and Veterans Administration Medical Center, San Diego, California 92161

The activity of plasmin, the major enzyme responsible for dissolving fibrin clots, is regulated by plasminogen activators, plasminogen activator inhibitors, alpha 2-antiplasmin, and inflammatory mediators. Recent studies suggest that plasmin activity can be regulated also at the level of plasminogen gene expression. In this study, we characterized the murine plasminogen promoter and 5'-flanking region. The major transcription start site was identified at -83 bp relative to the ATG translational initiation codon. A series of 5'-flanking sequences up to 2400 bp upstream of the transcription initiation site were fused to the luciferase reporter gene and transfected into hepatocytic cells. A 106-bp 5'-flanking region of the murine plasminogen gene demonstrated sufficient functional promoter activity in plasminogen-expressing cells. IL-6 treatment stimulated luciferase activity driven by the 5'-flanking region and an intact consensus IL-6-responsive element at -791, was required for maximal stimulation by this cytokine. These results indicate the presence of regulatory elements in the 5'-flanking region of the murine plasminogen promoter that may regulate murine plasminogen gene expression and, hence, plasmin activity.

* This work was supported in part by National Institutes of Health Grants HL-45934 and 38272 (to L. A. M.), HL-50398 (to R. J. P.), and HL-47826 and HL-63194 (to J. L. D.); by a grant from the Department of Veteran Affairs (to R. J. P.); and by grants from the Danish Medical Research Council, the Danish Cancer Research Foundation, and the Danish Plasmid Foundation (to T. H. B.). This is Manuscript 14569-VB from the Scripps Research Institute. Portions of this manuscript were presented at the Second Annual Conference on Arteriosclerosis, Thrombosis, and Vascular Biology, Arlington, VA, May 11-13, 2001.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AY134430.

§ Supported by National Institutes of Health NHLBI Minority Postdoctoral Supplement Research Supplement HL-45934. To whom correspondence should be addressed: Dept. of Cell Biology, Division of Vascular Biology (CVN-26), Scripps Research Inst., 10550 N. Torrey Pines Rd., La Jolla, CA 92037. Tel.: 858-822-5728; Fax: 858-822-0698; E-mail: fbannach@ucsd.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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