Toxicity of melanin-free ink of Sepia officinalis to transformed cell lines: identification of the active factor as tyrosinase (Articolo in rivista)

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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
  • 293 (literal)
Pagina fine
  • 299 (literal)
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  • 308 (literal)
Rivista
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  • L'autore Elio De Nisco ha svolto il prfesente lavoro presso l'ISA in qualità di tesista (literal)
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  • 2 (literal)
Note
  • Pubme (literal)
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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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