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Blood, Vol. 94 No. 6 (September 15), 1999:
pp. 2029-2038
Fibrin Fragment Induction of Plasminogen Activator Inhibitor
Transcription Is Mediated by Activator Protein-1 Through a Highly
Conserved Element
Mitchell A. Olman,
James S. Hagood,
Warren L. Simmons,
Gerald M. Fuller,
Charles Vinson, and
Kimberly E. White
From the Department of Medicine, Division of Pulmonary and Critical
Care Medicine, and the Departments of Pathology, Pediatrics, and Cell
Biology, University of Alabama, Birmingham, AL; and the Laboratory of
Biochemistry, National Cancer Institute, Bethesda, MD.
Plasminogen activator inhibitor type-1 (PAI-1), a serine protease
inhibitor, affects the processes of fibrinolysis, wound healing, and
vascular remodeling. We have demonstrated that PAI-1 transcription is
induced by D dimer, a plasmin proteolytic fragment of fibrin,
supporting its role in negative feedback on peri-cellular proteolysis.
The focus of this study was to define the mechanism of D dimer's
effects on PAI-1 transcription. D dimer increased the binding activity
of the transcription factor activator protein-1 components c-fos/junD
and c-fos mRNA levels in a time- and concentration-dependent manner to
a greater extent than fibrinogen. Both basal and D dimer-induced PAI-1
transcriptional activity were entirely dependent on elements within the
 161 to 48 bp region of the PAI-1 gene in fibroblasts. Mutations within the AP-1-like element (59 to 52 bp) in the PAI-1 gene affected D dimer-induced transcriptional activity, c-fos/junD DNA binding, and basal and c-fos inducible PAI-1
transcriptional activity. Furthermore, expression of either wild-type
or mutant c-fos proteins augmented or diminished the response of the
PAI-1 promoter (161 to +26 bp) to D dimer, respectively. D
dimer-induced binding of c-fos/junD to the highly conserved and unique
AP-1 like element in the PAI-1 gene provides a mechanism whereby
specific fibrin fragments control fibrin persistence at sites of
inflammation, fibrosis, and neoplasia.
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