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The protein encoded by NPC1L1 is a multi-pass membrane protein. De plus, nous expédions NPC1L1 Anticorps (51) et NPC1L1 Protéines (10) et beaucoup plus de produits pour cette protéine.
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We therefore propose that cholesterol is absorbed by NPC1L1 acting as a membrane transporter and that NPC1L1 is internalized to an endosomal compartment to reduce the absorption of cholesterol.
Decreased mRNA levels of HNF4alpha (Montrer HNF4A Kits ELISA) and SREBP2 (Montrer SREBF2 Kits ELISA) in mice could be involved in the reduction in NPC1L1 expression.
NPC1L1 knockout protects against colitis-associated tumorigenesis.
demonstrate that Niemann-Pick C1-like 1 (NPC1L1) protein, a cholesterol transporter, plays a central role in intestinal VK uptake and modulates the anticoagulant effect of warfarin. In
NPC1L1 may suppress gluconeogenesis by inhibition of FoxO1 (Montrer FOXO1 Kits ELISA) pathways.
DNA methylation in the promoter region of the NPC1L1 gene appears to be a major mechanism underlying differential expression of NPC1L1 along the length of the gastrointestinal tract.
cholesterol and tocopherol uptakes share common pathways in cell culture models, but display different in vivo absorption patterns associated with distinct contributions of SR-BI (Montrer SCARB1 Kits ELISA) and NPC1L1
The clathrin adaptor Numb (Montrer NUMB Kits ELISA) regulates intestinal cholesterol absorption through dynamic interaction with NPC1L1.
Glucose appears to directly modulate NPC1L1 expression via transcriptional mechanisms and the involvement of phosphatase-dependent pathways.
the mechanism of cholesterol sensing by NPC1L1 and proposes a mechanism for selective cholesterol absorption
Cdc42 (Montrer CDC42 Kits ELISA) controls the cholesterol-regulated transport and localization of NPC1L1, and plays a role in cholesterol absorption.
Due to their high affinity for the N-terminal domain of NPC1L1, black and cowpea bean peptides produced in the digestive track have the potential to disrupt interactions between NPC1L1 and membrane proteins that lead to cholesterol absorption
These experiments demonstrate that cholesterol uptake by NPC1L1 does not require endocytosis; moreover, ezetimibe interferes with NPC1L1's cholesterol adsorption activity without blocking NPC1L1 internalization in RH7777 cells.
Novel sequencing techniques are detecting rare variants with larger effect sizes (eg, NPC1L1) , which may further improve on Cardiovascular disease risk prediction.
The results demonstrate that NPC1L1 recognizes alpha-tocopherol via its N-terminal domain and mediates alpha-tocopherol uptake through the same mechanism as cholesterol absorption.
Simultaneously, these data indicate that R174H, V177I and V1284L NPC1L1 variations in high or low LDL-C individuals may not directly influence cholesterol absorption by NPC1L1.
The results of this study identified the association between genetic susceptibility of the NPC1L1 gene and HCV infection, as well as biochemical characteristics of HCV-infected persons in Yunnan, China.
exposure to LDL-C-lowering genetic variants in or near NPC1L1 and other genes was associated with a higher risk of type 2 diabetes. These data provide insights into potential adverse effects of LDL-C-lowering therapy.
Detailed analysis of the role of NPC1L1 mutations in an exceptional responder to ezetimibe. The results point to a complex set of events in which the combined mutations were shown to affect cholesterol uptake in the presence of ezetimibe. Proteomic analysis suggests that the exceptional response may also lie in the nature of interactions with cytosolic proteins.
Study suggests that the G allele of the NPC1L1 polymorphism g1679C>G may be a positive marker of gallstone formation risk.
To study whether human NPC1L1 gene is regulated transcriptionally by LRH-1 (Montrer NR5A2 Kits ELISA), we have analyzed evolutionary conserved regions (ECRs) in HepG2 cells.
The protein encoded by this gene is a multi-pass membrane protein. It contains a conserved N-terminal Niemann-Pick C1 (NPC1) domain and a putative sterol-sensing domain (SSD) which includes a YQRL motif functioning as a plasma membrane to trans-Golgi network transport signal in other proteins. This protein takes up free cholesterol into cells through vesicular endocytosis and plays a critical role in the absorption of intestinal cholesterol. It also has the ability to transport alpha-tocopherol (vitamin E). The drug ezetimibe targets this protein and inhibits the absorption of intestinal cholesterol and alpha-tocopherol. In addition, this protein may play a critical role in regulating lipid metabolism. Polymorphic variations in this gene are associated with plasma total cholesterol and low-density lipoprotein cholesterol (LDL-C) levels and coronary heart disease (CHD) risk. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
, NPC1 (Niemann-Pick disease, type C1, gene)-like 1
, Niemann-Pick C1-like protein 1
, Niemann-Pick C1-like 1 protein
, Niemann-Pick C1-like protein 1-like
, Niemann-Pick disease, type C1
, Niemann-Pick disease, type C1-like 1