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Originally published In Press as doi:10.1074/jbc.M910460199 on June 19, 2000

J. Biol. Chem., Vol. 275, Issue 34, 26040-26049, August 25, 2000
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Complex Contribution of the 3'-Untranslated Region to the Expressional Regulation of the Human Inducible Nitric-oxide Synthase Gene
INVOLVEMENT OF THE RNA-BINDING PROTEIN HuR*

Fernando Rodriguez-PascualDagger §, Michael HausdingDagger , Irmgard Ihrig-BiedertDagger , Henry Furneaux, Andrew P. Levy||, Ulrich FörstermannDagger , and Hartmut KleinertDagger **

From the Dagger  Department of Pharmacology, Johannes Gutenberg University, Obere Zahlbacher Strasse 67, D-55101 Mainz, Germany,  Program in Molecular Pharmacology and Therapeutics, Memorial Sloan Kettering Cancer Center, New York, New York 10021, and || Technion Faculty of Medicine, Technion-Israel Institute of Technology, Haifa 31096, Israel

Cytokine stimulation of human DLD-1 cells resulted in a marked expression of nitric-oxide synthase (NOS) II mRNA and protein accompanied by only a moderate increase in transcriptional activity. Also, there was a basal transcription of the NOS II gene, which did not result in measurable NOS II expression. The 3'-untranslated region (3'-UTR) of the NOS II mRNA contains four AUUUA motifs and one AUUUUA motif, known to destabilize the mRNAs of proto-oncogenes, nuclear transcription factors, and cytokines. Luciferase reporter gene constructs containing the NOS II 3'-UTR showed a significantly reduced luciferase activity. The embryonic lethal abnormal vision (ELAV)-like protein HuR was found to bind with high affinity to the adenylate/uridylate-rich elements of the NOS II 3'-UTR. Inhibition of HuR with antisense constructs reduced the cytokine-induced NOS II mRNA, whereas overexpression of HuR potentiated the cytokine-induced NOS II expression. This provides evidence that NOS II expression is regulated at the transcriptional and post-transcriptional level. Binding of HuR to the 3'-UTR of the NOS II mRNA seems to play an essential role in the stabilization of this mRNA.

* This work was supported by Grant 8312-38 62 61 from the Innovation Foundation of the State of Rhineland-Palatinate (to H. K. and U. F.), Grant Kl 1020/4-1 from the Deutsche Forschungsgemeinschaft (to H. K.), and by Project A1 from the Collaborative Research Center SFB 553 (to U. F.).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.

§ Recipient of a Federation of the European Biochemical Societies (FEBS) Long Term Fellowship.

** To whom correspondence should be addressed: Dept. of Pharmacology, Johannes Gutenberg University, Obere Zahlbacher Str. 67, 55101 Mainz, Germany. Tel.: 49 (6131) 393-3245; Fax: 49 (6131) 393-6611; E-mail: kleinert@mail.uni-mainz.de.

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