منابع مشابه
Purified NPC1 protein. I. Binding of cholesterol and oxysterols to a 1278-amino acid membrane protein.
The Niemann-Pick, Type C1 protein (NPC1) is required for the transport of lipoprotein-derived cholesterol from lysosomes to endoplasmic reticulum. The 1278-amino acid, polytopic membrane protein has not been purified, and its mechanism of action is unknown. Unexpectedly, we encountered NPC1 in a search for a membrane protein that binds 25-hydroxycholesterol (25-HC) and other oxysterols. A 25-HC...
متن کاملPurified NPC1 protein: II. Localization of sterol binding to a 240-amino acid soluble luminal loop.
Defects in Niemann-Pick, Type C-1 protein (NPC1) cause cholesterol, sphingolipids, phospholipids, and glycolipids to accumulate in lysosomes of liver, spleen, and brain. In cultured fibroblasts, NPC1 deficiency causes lysosomal retention of lipoprotein-derived cholesterol after uptake by receptor-mediated endocytosis. NPC1 contains 1278 amino acids that form 13 membrane-spanning helices and thr...
متن کاملGlycosylation inhibition reduces cholesterol accumulation in NPC1 protein-deficient cells.
Lysosomes are lined with a glycocalyx that protects the limiting membrane from the action of degradative enzymes. We tested the hypothesis that Niemann-Pick type C 1 (NPC1) protein aids the transfer of low density lipoprotein-derived cholesterol across this glycocalyx. A prediction of this model is that cells will be less dependent upon NPC1 if their glycocalyx is decreased in density. Lysosome...
متن کاملPurified Protein Derivative--PPD.
A 55-year-old physician had a PPD made as part of a clinical evaluation. Laboratory tests were unremarkable and PPD, read in 48 hours, showed an area of induration of 18 mm and an erythema of 51 mm (Panel A). A 2 mm punch biopsy was done in the center of the induration 96 hours after the injection. Histopathology showed an intense perivascular cuffing with macrophages and lymphocytes and edema ...
متن کاملNiemann-Pick C1 (NPC1)/NPC1-like1 Chimeras Define Sequences Critical for NPC1’s Function as a Filovirus Entry Receptor
We recently demonstrated that Niemann-Pick C1 (NPC1), a ubiquitous 13-pass cellular membrane protein involved in lysosomal cholesterol transport, is a critical entry receptor for filoviruses. Here we show that Niemann-Pick C1-like1 (NPC1L1), an NPC1 paralog and hepatitis C virus entry factor, lacks filovirus receptor activity. We exploited the structural similarity between NPC1 and NPC1L1 to co...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2008
ISSN: 0021-9258
DOI: 10.1074/jbc.m707944200