Induction of H-ferritin Synthesis by Oxalomalate is Regulated at Both the Transcriptional and Post-transcriptional Levels.
From: Dipartimento di Farmacologia Sperimentale, Facoltà di Farmacia, Università di Napoli Federico II, via D. Montesano 49, I-80131 Napoli, Italy. rsantama@unina.it
Biochimica et biophysica acta
- Publish Date: Aug 2006
- ISSN: 0006-3002
- Volume: 1763
- Issue: 8
- Pages: 815-22
- Medium: Print
- Language: English
- Citation (JAMA): Santamaria Rita, Bevilacqua Maria Assunta, Maffettone Carmen, et al. Induction of H-ferritin Synthesis by Oxalomalate is Regulated at Both the Transcriptional and Post-transcriptional Levels.. Biochim. Biophys. Acta Aug 2006;1763:815-22
Abstract
Ferritin gene expression is complex and is controlled at transcriptional level in response to a variety of stimuli such as hormones, cytokines and cAMP. Iron, hemin and several compounds, chemically different, also activate the transcription of the ferritin gene. Ferritin biosynthesis is mainly regulated at post-transcriptional level by iron regulatory proteins (IRP1 and IRP2). We previously reported that oxalomalate, a competitive inhibitor of aconitase, remarkably decreases the IRP1 RNA-binding activity and induces a significant increase of ferritin expression. Here, we examined in cells cultured in presence of OMA the IRP1 intracellular content, ferritin biosynthesis and the transcriptional efficiency of H-ferritin gene promoter. Our results demonstrate a peculiar role of OMA that rapidly inactivates IRP1 without affecting IRP1 protein content and subsequently activates H-ferritin gene transcription leading to an overall increase of ferritin biosynthesis. We conclude that OMA regulates H-ferritin biosynthesis acting early at the post-transcriptional level and later on at transcriptional level.
Mesh Headings (Keywords): 3T3-L1 Cells, Animals, Base Sequence, DNA, Ferritins, Iron Regulatory Protein 1, Kinetics, Mice, Oxalates, RNA, Messenger, Transcription, Genetic
Check for Full Text / PubMed Unique Identifier (PMID): 16828896
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