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J Biol Chem, Vol. 275, Issue 16, 11846-11851, April 21, 2000

alpha 1 Adrenergic Agonist Induction of p21waf1/cip1 mRNA Stability in Transfected HepG2 Cells Correlates with the Increased Binding of an AU-rich Element Binding Factor*

Jie LiuDagger , Xuening ShenDagger , Van-Anh Nguyen, George Kunos, and Bin Gao§

From the Department of Pharmacology and Toxicology, Medical College of Virginia, Virginia Commonwealth University, Richmond, Virginia 23298

Stimulation of transfected HepG2 cells (TFG2) with the alpha 1-adrenergic agonist phenylephrine (PE) significantly activated p21waf1/cip1 gene expression without affecting p53 gene expression. Northern blotting and reporter assay demonstrated that this induction was due to PE stimulation of p21waf1/cip1 mRNA stability. To further define the underlying mechanism, we prepared a chloramphenicol acetyltransferase (CAT)-p21waf1/cip1 3'-untranslated region (3'-UTR) hybrid construct by inserting the 3'-UTR of p21waf1/cip1 mRNA just downstream from the CAT coding sequence and transfected it into TFG2 cells. PE treatment enhanced the activity of this construct by 6-fold. Deletion analyses indicated that an AU-rich element (AURE) located between 553 to 625 within the p21waf1/cip1 3'-UTR was required for this induction. RNA gel shift assays demonstrated that this AURE bound an RNA-binding protein. This protein has been purified 5000-fold from PE-treated TFG2 cells by heparin-Sepharose and RNA affinity chromatography. SDS-polyacrylamide gel electrophoresis, UV cross-linking, and Northwestern analyses indicated the molecular mass of this protein as 24 and 52 kDa. Finally, PE treatment markedly enhanced this RNA-protein binding by a p42/44 mitogen-activated protein kinase-dependent mechanism. These data suggest that the AURE located between 553 and 625 within the p21waf1/cip1 mRNA 3'-UTR, which binds an RNA-binding protein, is responsible for PE-induced p21waf1/cip1 mRNA stability.

* This work was supported by National Institutes of Health Grants R29CA72681, R03AA11823, and R01AA12637 (to B. G).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: Box 980613, Richmond, VA 23298. Tel.: 804-828-2126; Fax: 804-828-2117; E-mail: bgao@hsc.vcu.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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