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A more recent version of this article appeared on March 1, 2005

Papers In Press, published online ahead of print December 16, 2004
J. Lipid Res., doi:10.1194/jlr.M400292-JLR200
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Submitted on August 2, 2004
Revised on December 1, 2004
Accepted on December 7, 2004

Activation of the nuclear receptor FXR induces fibrinogen expression: a new role for bile acid signaling

Andrew M. Anisfeld, Heidi R. Kast-Woelbern, Hans Lee, Yanqiao Zhang, Florence Y. Lee, and Peter A. Edwards

Biological Chemistry, UCLA, Los Angeles, CA 90095

Corresponding Author: pedwards{at}mednet.ucla.edu

Three genes, FBGa, ß, and gamma , encode proteins that make up the mature fibrinogen protein complex. The complex is secreted from the liver and plays a key role in coagulation in response to vascular disruption. We identified all three FBG genes in a screen designed to isolate genes that are regulated by the farnesoid X-receptor (FXR, NR1H4). Treatment of human hepatoma cells with either naturally occurring (CDCA) or synthetic (GW4064) FXR ligands resulted in induction of transcripts for all three genes. The induction of FBGß mRNA in response to activated FXR appears to be a primary transcriptional response, as it is blocked by actinomycin-D, but not by cycloheximide. Four FXR isoforms have recently been identified that differ either at their amino terminus and/or by the presence of four amino acids in the hinge region. Interestingly, the activities of the human FBGß promoter-reporter constructs were highly induced by FXR isoforms that lack the four amino acid insert. The observation that all three FBG subunits are induced by specific FXR isoforms, in response to FXR ligands, suggests that bile acids and FXR modulate fibrinolytic activity.


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