http://www.cnr.it/ontology/cnr/individuo/prodotto/ID45533
Toxicity of melanin-free ink of Sepia officinalis to transformed cell lines: identification of the active factor as tyrosinase (Articolo in rivista)
- Type
- Label
- Toxicity of melanin-free ink of Sepia officinalis to transformed cell lines: identification of the active factor as tyrosinase (Articolo in rivista) (literal)
- Anno
- 2003-01-01T00:00:00+01:00 (literal)
- Alternative label
Russo GL, De Nisco E, Fiore G, Di Donato P, d'Ischia M, Palumbo A (2003)
Toxicity of melanin-free ink of Sepia officinalis to transformed cell lines: identification of the active factor as tyrosinase
in Biochemical and biophysical research communications (Print)
(literal)
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- Russo GL, De Nisco E, Fiore G, Di Donato P, d'Ischia M, Palumbo A (literal)
- Pagina inizio
- Pagina fine
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- Rivista
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- L'autore Elio De Nisco ha svolto il prfesente lavoro presso l'ISA in qualità di tesista (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
- Note
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- Institute of Food Science, National Research Council, Avellino, Italy
Zoological Station \"Anton Dohrn\", Naples, Italy
Department of Organic Chemistry and Biochemistry, University of Naples \"Federico II\", Naples, Italy (literal)
- Titolo
- Toxicity of melanin-free ink of Sepia officinalis to transformed cell lines: identification of the active factor as tyrosinase (literal)
- Abstract
- The melanin-free ink of the cephalopod Sepia officinalis is shown to contain a heat labile proteinaceous component toxic to a variety of cell lines, including PC12 cells. Gel filtration chromatography indicated that the toxic component was concentrated in those fractions eluted at a molecular weight higher than 100 kDa and exhibiting the highest tyrosinase activity. SDS-PAGE analysis of the active fractions displayed a single major band migrating at an approximate molecular weight of 100 kDa, identical with that of the single tyrosinase band in the melanin-free ink. These data unambiguously demonstrated the identity of the toxic component with tyrosinase. Treatment of purified Sepia as well as of mushroom tyrosinase with an immobilized version of proteinase K resulted in a parallel loss of tyrosinase activity and cytotoxicity. Sepia apotyrosinase was ineffective in inducing cytotoxicity in PC12 cells. Purified Sepia tyrosinase was found to induce a significant increase in caspase 3 activity in PC12 cells, leading eventually to an irreversible apoptotic process. Overall, these results disclose a hitherto unrecognized property of tyrosinase that may lead to a reappraisal of its biological significance beyond that of a mere pigment producing enzyme. (literal)
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