http://www.cnr.it/ontology/cnr/individuo/prodotto/ID281206
Epigenetic control of hypoxia inducible factor-1?-dependent expression of placental growth factor in hypoxic conditions (Articolo in rivista)
- Type
- Label
- Epigenetic control of hypoxia inducible factor-1?-dependent expression of placental growth factor in hypoxic conditions (Articolo in rivista) (literal)
- Anno
- 2014-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.4161/epi.27835 (literal)
- Alternative label
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Tudisco L.; Della Ragione F.; Tarallo V.; Apicella I.; D'Esposito M.; Matarazzo M.R.; De Falco S. (literal)
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- DE Falco *Corresponding Author (literal)
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- http://www.scopus.com/inward/record.url?eid=2-s2.0-84899136534&partnerID=q2rCbXpz (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
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- Istituto di Genetica e Biofisica 'Adriano Buzzati-Traverso', National Research Council, Napoli, Italy; Istituto di Ricovero e Cura a Carattere Scientifico Neuromed, Pozzilli, Italy (literal)
- Titolo
- Epigenetic control of hypoxia inducible factor-1?-dependent expression of placental growth factor in hypoxic conditions (literal)
- Abstract
- Hypoxia plays a crucial role in the angiogenic switch, modulating a large set of genes mainly through the activation of hypoxia-inducible factor (HIF) transcriptional complex. Endothelial cells play a central role in new vessels formation and express placental growth factor (PlGF), a member of vascular endothelial growth factor (VEGF) family, mainly involved in pathological angiogenesis. Despite several observations suggest a hypoxia-mediated positive modulation of PlGF, the molecular mechanism governing this regulation has not been fully elucidated. We decided to investigate if epigenetic modifications are involved in hypoxia-induced PlGF expression. We report that PlGF expression was induced in cultured human and mouse endothelial cells exposed to hypoxia (1% O 2), although DNA methylation at the Plgf CpG-island remains unchanged. Remarkably, robust hyperacetylation of histones H3 and H4 was observed in the second intron of Plgf, where hypoxia responsive elements (HREs), never described before, are located. HIF-1?, but not HIF-2?, binds to identified HREs. Noteworthy, only HIF-1? silencing fully inhibited PlGF upregulation. These results formally demonstrate a direct involvement of HIF-1? in the upregulation of PlGF expression in hypoxia through chromatin remodeling of HREs sites. Therefore, PlGF may be considered one of the putative targets of anti-HIF therapeutic applications. (literal)
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