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Originally published In Press as doi:10.1074/jbc.M213027200 on February 10, 2003

J. Biol. Chem., Vol. 278, Issue 16, 13912-13918, April 18, 2003
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Inherent Instability of Plasminogen Activator Inhibitor Type 2 mRNA Is Regulated by Tristetraprolin*

Hong YuDagger , Stan StasinopoulosDagger , Peter Leedman§, and Robert L. Medcalf

From the Department of Medicine, Monash University, Box Hill Hospital, Box Hill 3128, Victoria Australia and the § Laboratory for Cancer Medicine, Centre for Medical Research, School of Medicine and Pharmacology, Royal Perth Hospital Unit, Western Australian Institute for Medical Research, the University of Western Australia, Perth 6000 Western Australia, Australia

Plasminogen activator inhibitor type 2 (PAI-2) is a serine protease inhibitor that is subject to regulation at the post-transcriptional level. At least two mRNA instability elements reside within the PAI-2 transcript; one in the coding region and another within the 3'-untranslated region (UTR). For the latter, a functional AU-rich motif (ARE) has been identified that provides a binding site for a number of cellular proteins, including the mRNA stability protein, HuR. In this study, we used the yeast three-hybrid system to screen a human leukocyte cDNA library to identify other proteins that associate with the PAI-2 ARE. This screen identified tristetraprolin (TTP) as a PAI-2 mRNA ARE-binding protein. UV cross-linking and immunoprecipitation experiments showed that TTP expressed in HEK293 cells could associate with the PAI-2 ARE in vitro. Co-transfection of plasmids expressing TTP and PAI-2 in HEK293 cells resulted in an increase in the decay rate of PAI-2 mRNA and loss of PAI-2 protein in a process that was dependent upon the PAI-2 3'-UTR. The 29-nt PAI-2 AU-rich element alone was also capable of conferring TTP-dependent mRNA instability to a reporter transcript. The extent of PAI-2 mRNA stability was remarkably sensitive to TTP since TTP-dependent PAI-2 mRNA decay occurred at TTP levels that were below Western blot detection limits. This study identifies TTP as a functional PAI-2 ARE-binding protein that modulates the post-transcriptional regulation of the PAI-2 gene.

* This study was supported by grants obtained from the National Health and Medical Research Council of Australia (to R. L. M.).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.

Dagger These authors contributed equally to this work.

To whom correspondence should be addressed: Monash University Dept. of Medicine, Box Hill Hospital, Box Hill 3128 Victoria, Australia. Tel.: 61-3-9895-0318; Fax: 61-3-9895-0332; E-mail: Robert.Medcalf@med.monash.edu.au.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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