hnRNP-A2/B1 modulate collagen prolyl 4-hydroxylase alpha (I) mRNA-stability

doi:10.1074/jbc.M510925200

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Papers In Press, published online ahead of print February 7, 2006
J. Biol. Chem, 10.1074/jbc.M510925200
Submitted on October 6, 2005
Accepted on February 7, 2006

hnRNP-A2/B1 modulate collagen prolyl 4-hydroxylase alpha (I) mRNA-stability

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

Institut für Vegetative Physiologie, Charité, Universitätsmedizin Berlin, Berlin D-10117

Corresponding Author: michael.faehling{at}charite.de

Collagen Prolyl 4-hydroxylase (C-P4H) alpha 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-alpha (I) is regulated at the posttrancriptional level under these conditions. Here we report that the induction of C-P4H-alpha (I) in human fibrosarcoma cells HT1080 by the iron chelator 2,2-Dipyridyl (2,2-DP) is predominantly caused by an enhancement of mRNA stability. This effect is mediated by an increased synthesis and binding of hnRNP-A2/B1, which interact with a (U)16-element located in the 3'-untranslated region of C-P4H-alpha (I) mRNA. Luciferase reporter gene assays depending on C-P4H-alpha (I) 3'UTR and co-transfection with hnRNP-A2/B1 provide evidence that the (U)16-element is necessary and sufficient for posttranscriptional control of C-P4H-alpha (I) synthesis under the analyzed conditions. Further indication for the significance of hnRNP-A2/B1 in C-P4H-alpha (I) induction was obtained by micro array experiments. In a dataset representing 686 independent physiological conditions we found a significant positive correlation between hnRNP-A2/B1 and C-P4H-alpha (I) mRNAs.

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