Source:http://linkedlifedata.com/resource/pubmed/id/12901867
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2003-8-6
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CASP3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Casp3 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Caspase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Caspases,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidase K,
http://linkedlifedata.com/resource/pubmed/chemical/Melanins,
http://linkedlifedata.com/resource/pubmed/chemical/Monophenol Monooxygenase
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
22
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pubmed:volume |
308
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
293-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12901867-Animals,
pubmed-meshheading:12901867-Apoptosis,
pubmed-meshheading:12901867-Caco-2 Cells,
pubmed-meshheading:12901867-Caspase 3,
pubmed-meshheading:12901867-Caspases,
pubmed-meshheading:12901867-Cell Line, Transformed,
pubmed-meshheading:12901867-Endopeptidase K,
pubmed-meshheading:12901867-Humans,
pubmed-meshheading:12901867-Ink,
pubmed-meshheading:12901867-Jurkat Cells,
pubmed-meshheading:12901867-Melanins,
pubmed-meshheading:12901867-Mollusca,
pubmed-meshheading:12901867-Monophenol Monooxygenase,
pubmed-meshheading:12901867-PC12 Cells,
pubmed-meshheading:12901867-Rats
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pubmed:year |
2003
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pubmed:articleTitle |
Toxicity of melanin-free ink of Sepia officinalis to transformed cell lines: identification of the active factor as tyrosinase.
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pubmed:affiliation |
Institute of Food Science, National Research Council, Avellino, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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