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APE/Ref-1 is controlled by both redox and cAMP-dependent mechanisms in rat thyroid cells.

Authors: Tell, G  Pines, A  Pandolfi, M  D'Elia, AV  Donnini, D  Lonigro, R  Manzini, G  Russo, D  Di Loreto, C  Damante, G 
Citation: Tell G, etal., Horm Metab Res 2002 Jun;34(6):303-10.
Pubmed: (View Article at PubMed) PMID:12173070
DOI: Full-text: DOI:10.1055/s-2002-33258

APE/Ref-1 is a multifunctional protein possessing both redox and DNA repair functions. Through its redox activity, APE/Ref-1 controls the DNA-binding function of several transcriptional regulators (AP1, NF-kappaB, p53, Pax proteins). We have previously shown that APE/Ref-1 upregulates the transcriptional activity of the thyroid-specific transcription factor Pax8. In thyroid cells, APE/Ref-1 can be detected both in the nuclear and cytoplasmatic compartments. In this study regulatory mechanisms acting on APE/Ref-1 were revealed using the FRTL-5 cell line. TSH induces both cytoplasm-to-nucleus translocation and neosynthesis of APE/Ref-1 protein. Interestingly, only neosynthesis is dependent on cAMP signalling. In contrast, the cytoplasm-to-nucleus translocation is dependent on redox-mediated mechanisms. Based upon the data shown in this study and in others, a bimodal control of APE/Ref-1 by TSH can be delineated.

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CRRD Object Information
CRRD ID: 634652
Created: 2003-09-08
Species: All species
Last Modified: 2003-09-08
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.