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• W1990735027 abstract "Wilson disease is a genetic disorder characterized by the accumulation of copper in the body by defective biliary copper excretion. Wilson disease gene product (ATP7B) functions in copper incorporation to ceruloplasmin (Cp) and biliary copper excretion. However, copper metabolism in hepatocytes has been still unclear. Niemann-Pick disease type C (NPC) is a lipid storage disorder and the most commonly mutated gene is NPC1 and its gene product NPC1 is a late endosome protein and regulates intracellular vesicle traffic. In the present study, we induced NPC phenotype and examined the localization of ATP7B and secretion of holo-Cp, a copper-binding mature form of Cp. The vesicle traffic was modulated using U18666A, which induces NPC phenotype, and knock down of NPC1 by RNA interference. ATP7B colocalized with the late endosome markers, but not with the trans-Golgi network markers. U18666A and NPC1 knock down decreased holo-Cp secretion to culture medium, but did not affect the secretion of other secretory proteins. Copper accumulated in the cells after the treatment with U18666A. These findings suggest that ATP7B localizes in the late endosomes and that copper in the late endosomes is transported to the secretory compartment via NPC1-dependent pathway and incorporated into apo-Cp to form holo-Cp." @default.
• W1990735027 created "2016-06-24" @default.
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• W1990735027 date "2009-01-01" @default.
• W1990735027 modified "2023-10-05" @default.
• W1990735027 title "Niemann-Pick C1 protein transports copper to the secretory compartment from late endosomes where ATP7B resides" @default.
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• W1990735027 doi "https://doi.org/10.1016/j.yexcr.2008.10.022" @default.
• W1990735027 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19007772" @default.
• W1990735027 hasPublicationYear "2009" @default.
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