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J. Biol. Chem., Vol. 281, Issue 14, 9279-9286, April 7, 2006

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Heterogeneous Nuclear Ribonucleoprotein-A2/B1 Modulate Collagen Prolyl 4-Hydroxylase, (I) mRNA Stability^*

Michael Fähling¹, Ralf Mrowka, Andreas Steege, Peter Martinka, Pontus B. Persson, and Bernd J. Thiele

From the Charité, Universitätsmedizin Berlin, Institut für Vegetative Physiologie, D-10117 Berlin and the Freie Universität Berlin, Institut für Biologie, D-14195 Berlin, Germany

Collagen prolyl 4-hydroxylase (C-P4H) -subunit is of regulatory importance in the assembling of C-P4H tetramers, which are necessary for the hydroxylation of procollagen chains. Change in collagen expression by hypoxia or iron diminishment is a significant issue in extracellular matrix remodeling. It was proposed that C-P4H- (I) is regulated at the posttrancriptional level under these conditions. Here we report that the induction of C-P4H- (I) in human fibrosarcoma cells HT1080 by the iron chelator 2,2-dipyridyl is predominantly caused by an enhancement of mRNA stability. This effect is mediated by an increased synthesis and binding of heterogeneous nuclear ribonucleoprotein (hnRNP)-A2/B1, which interacts with a (U)₁₆ element located in the 3'-untranslated region of C-P4H- (I) mRNA. Luciferase reporter gene assays depending on C-P4H- (I) 3'-untranslated region and co-transfection with hnRNP-A2/B1 provide evidence that the (U)₁₆ element is necessary and sufficient for posttranscriptional control of C-P4H- (I) synthesis under the analyzed conditions. Further indication for the significance of hnRNP-A2/B1 in C-P4H- (I) induction was obtained by micro array experiments. In a data set representing 686 independent physiological conditions, we found a significant positive correlation between hnRNP-A2/B1 and C-P4H- (I) mRNAs.

Received for publication, October 6, 2005 , and in revised form, December 14, 2005.

^* This work was supported by Deutsche Forschungsgemeinschaft (DFG Grants GRK754 and TH459/5) and Bundesministerium für Bildung und Forschung (BMBF Grants NGFN2, KG-CV1.2, and Charité, Core Facility Proteomics). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Charité, Universitätsmedizin Berlin, Institut für Vegetative Physiologie, Tucholskystr. 2, D-10117 Berlin, Germany. Tel.: 49-30-450-528268; Fax: 49-30-450-528972; E-mail: Michael.Faehling{at}charite.de.

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