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Titolo:
Nitric oxide up-regulates ferritin mRNA level in snail neurons
Autore:
Xie, MQ; Hermann, A; Richter, K; Engel, E; Kerschbaum, HH;
Indirizzi:
Salzburg Univ, Inst Zool, Dept Mol Neurobiol & Cellular Physiol, A-5020 Salzburg, Austria Salzburg Univ Salzburg Austria A-5020 Physiol, A-5020 Salzburg, Austria Salzburg Univ, Inst Genet, A-5020 Salzburg, Austria Salzburg Univ Salzburg Austria A-5020 st Genet, A-5020 Salzburg, Austria Austrian Acad Sci, Inst Mol Biol, A-5020 Salzburg, Austria Austrian Acad Sci Salzburg Austria A-5020 Biol, A-5020 Salzburg, Austria
Titolo Testata:
EUROPEAN JOURNAL OF NEUROSCIENCE
fascicolo: 8, volume: 13, anno: 2001,
pagine: 1479 - 1486
SICI:
0953-816X(200104)13:8<1479:NOUFML>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSFERRIN RECEPTOR EXPRESSION; CENTRAL-NERVOUS-SYSTEM; MESSENGER-RNA; LIPID-PEROXIDATION; OXIDATIVE STRESS; CDNA CLONING; IRON; LOCALIZATION; SYNTHASE; PATHWAY;
Keywords:
cytochemistry; Helix pomatia; molecular biology;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Kerschbaum, HH Salzburg Univ, Inst Zool, Dept Mol Neurobiol & Cellular Physiol, Hellbrunnerstr 34, A-5020 Salzburg, Austria Salzburg Univ Hellbrunnerstr 34 Salzburg Austria A-5020 ia
Citazione:
M.Q. Xie et al., "Nitric oxide up-regulates ferritin mRNA level in snail neurons", EUR J NEURO, 13(8), 2001, pp. 1479-1486

Abstract

We cloned and sequenced the ferric ion-binding protein, ferritin, from thenervous system of the pulmonate snail, Helix pomatia. Helix H-ferritin cDNA contains a 519-bp open reading frame (ORF) and predicts an iron-responsive element (IRE) at the 5'-untranslated region (5'-UTR) of the ferritin mRNA. The deduced amino acid sequence revealed 86% similarity with Lymnaea stagnalis ferritin and about 70% similarity with vertebrate H-ferritin. While secreted ferritin isoforms contain a signalling sequence at their N-terminalend, Helix ferritin does not contain this sorting signal indicating that it is restricted to the cytoplasm. The amino acid ligands at positions Glu25, Tyr30, Glu59, Glu60, His63, Glu105 and Gln139 indicate an active ferroxidase site in Helix ferritin. In situ hybridization visualized ferritin mRNA in neuronal cell bodies but not in the neuropil. In contrast, ferritin-immunoreactive protein was localized in cell bodies and neurites. We further demonstrate that the NO donors S-nitroso-N-acetylpenicillamine (SNAP), or hydroxylamine (HA), increase the intracellular ferritin mRNA level by about 55%. In conclusion, our findings show that Helix neurons express an intracellular H-ferritin isoform and suggest that iron and NO metabolism are coupled.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/04/20 alle ore 11:17:39