We cloned and sequenced the ferric ion-binding protein, ferritin, from the nervous 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-terminal end, 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.