Source:http://linkedlifedata.com/resource/pubmed/id/16199032
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
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| pubmed:dateCreated |
2006-1-30
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| pubmed:abstractText |
The processing and trafficking of tyrosinase, a melanosomal protein essential for pigmentation, was investigated in a human epithelial 293 cell line that stably expresses the protein. The effects of the pink-eyed dilution (p) gene product, in which mutations result in oculocutaneous albinism type 2 (OCA2), on the processing and trafficking of tyrosinase in this cell line were studied. The majority of tyrosinase was retained in the endoplasmic reticulum-Golgi intermediate compartment and the early Golgi compartment in the 293 cells expressing the protein. Coexpression of p could partially correct the mistrafficking of tyrosinase in 293 cells. Tyrosinase was targeted to the late endosomal and lysosomal compartments after treatment of the cells with compounds that correct the tyrosinase mistrafficking in albino melanocytes, most likely through altering intracellular pH, while the substrate tyrosine had no effect on the processing of tyrosinase. Remarkably, this heterologous expression system recapitulates the defective processing and mistrafficking of tyrosinase observed in OCA2 albino melanocytes and certain amelanotic melanoma cells. Coexpression of other melanosomal proteins in this heterologous system may further aid our understanding of the details of normal and pathologic processing of melanosomal proteins.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Melanins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Monophenol Monooxygenase,
http://linkedlifedata.com/resource/pubmed/chemical/OCA2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine
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| pubmed:status |
MEDLINE
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| pubmed:month |
Mar
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| pubmed:issn |
0014-4835
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
82
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
519-28
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:16199032-Albinism, Oculocutaneous,
pubmed-meshheading:16199032-Biological Transport,
pubmed-meshheading:16199032-Blotting, Western,
pubmed-meshheading:16199032-Cell Line,
pubmed-meshheading:16199032-Endoplasmic Reticulum,
pubmed-meshheading:16199032-Endosomes,
pubmed-meshheading:16199032-Epithelial Cells,
pubmed-meshheading:16199032-Gene Expression,
pubmed-meshheading:16199032-Golgi Apparatus,
pubmed-meshheading:16199032-Humans,
pubmed-meshheading:16199032-Hydrogen-Ion Concentration,
pubmed-meshheading:16199032-Intracellular Fluid,
pubmed-meshheading:16199032-Lysosomes,
pubmed-meshheading:16199032-Melanins,
pubmed-meshheading:16199032-Membrane Transport Proteins,
pubmed-meshheading:16199032-Microscopy, Fluorescence,
pubmed-meshheading:16199032-Monophenol Monooxygenase,
pubmed-meshheading:16199032-Pigment Epithelium of Eye,
pubmed-meshheading:16199032-Transfection,
pubmed-meshheading:16199032-Tyrosine
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| pubmed:year |
2006
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| pubmed:articleTitle |
Heterologous expression of tyrosinase recapitulates the misprocessing and mistrafficking in oculocutaneous albinism type 2: effects of altering intracellular pH and pink-eyed dilution gene expression.
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| pubmed:affiliation |
The Ronald O. Perelman Department of Dermatology and Cell Biology, New York University School of Medicine, Dermatology Room H-100, NYU School of Medicine, 560 First Avenue, New York, NY 10016, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, N.I.H., Extramural
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