Source:http://linkedlifedata.com/resource/pubmed/id/16252260
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2005-12-26
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pubmed:abstractText |
Recently, after the identification of ferritin light chain (L-ferritin) gene and protein over-expression in human metastatic melanoma cells, we engineered, starting from the LM metastatic melanoma cell line, clones in which L-ferritin gene expression was down-regulated by the stable expression of a specific antisense construct. The present investigation started from the observation that L-ferritin down-regulated LM cells displayed a less pigmented phenotype, confirmed by a major decrease of total melanin, when compared to control LM cells. This finding was accompanied by a dramatic decrease in tyrosinase activity, which was not paralleled by a concomitant reduction of the amount of tyrosinase specific mRNA. Western blot analysis of tyrosinase in control LM cells displayed a pattern, which corresponds to the progressive glycosylation of the native protein up to the 80 kDa form, considered the functional one. Tyrosinase pattern assayed in L-ferritin down-regulated LM cells showed the remarkable absence of the 80 kDa form and a prevalence of endoglycosidase H (endo H)-sensitive immature (70 kDa) tyrosinase, accumulated in the endoplasmic reticulum (ER), as confirmed by confocal microscopy analysis. These results demonstrate that, in a human metastatic melanoma cell line, the stress condition promoted by L-ferritin down-modulation, can substantially influence proper maturation of tyrosinase.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9541
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 2005 Wiley-Liss, Inc.
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pubmed:issnType |
Print
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pubmed:volume |
206
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
843-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:16252260-Cell Line, Tumor,
pubmed-meshheading:16252260-Down-Regulation,
pubmed-meshheading:16252260-Endoplasmic Reticulum,
pubmed-meshheading:16252260-Ferritins,
pubmed-meshheading:16252260-Golgi Apparatus,
pubmed-meshheading:16252260-Humans,
pubmed-meshheading:16252260-Hypopigmentation,
pubmed-meshheading:16252260-Melanins,
pubmed-meshheading:16252260-Melanoma,
pubmed-meshheading:16252260-Monophenol Monooxygenase,
pubmed-meshheading:16252260-Neoplasm Metastasis,
pubmed-meshheading:16252260-Pigmentation,
pubmed-meshheading:16252260-Protein Biosynthesis,
pubmed-meshheading:16252260-Protein Processing, Post-Translational,
pubmed-meshheading:16252260-Protein Transport,
pubmed-meshheading:16252260-Transcription, Genetic
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pubmed:year |
2006
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pubmed:articleTitle |
Ferritin light chain down-modulation generates depigmentation in human metastatic melanoma cells by influencing tyrosinase maturation.
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pubmed:affiliation |
San Gallicano Dermatological Institute, Via E. Chianesi, Rome, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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