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We demonstrate that 4F and Cl/NO2-HDL (show HSD11B1 Proteins) act on scavenger receptor type I (SR-B1) using human aorta endothelial cells (HAEC) and SR-B1 ((-/-)) mouse aortic endothelial cells.
Our results demonstrate that SR-BI functions as an oncogene (show RAB1A Proteins) and promotes progression of clear cell renal cell carcinoma (show MOK Proteins) (ccRCC). SR-BI may serve as a potential prognostic biomarker and therapeutic target for ccRCC.
SCARB1 gene polymorphisms may serve as a potential predictor of treatment responses in chronic hepatitis C patients receiving interferon (show IFNA Proteins)-based therapy
The S112F single amino acid mutation in SR-BI inhibited the infectivity of hepatitis C virus derived from cell culture in a cell culture model by downregulating the expression of the SR-BI protein.
The cell surface receptor SR-BI (scavenger receptor class B member 1), is essential for hepatitis C virus (HCV) entry into hepatocytes. Variations in the gene coding this receptor influence infectivity and viral load. We analyzed these variations to gain a better understanding of inter-individual differences over the course of HCV infection.
The SCARB1AA genotype decreased cardiovascular risk and carrying GA genotype and G allele increased the risk of CAD. AA genotype carriers had higher levels of big-sized HDL (show HSD11B1 Proteins) subfraction.
These findings provide new insights into the role of SR-B1 in cellular cholesterol homeostasis and suggest molecular links between SR-B1-dependent lipid sensing and cell cholesterol and lipid droplet dynamics
Liposomes modified with both apolipoproteins A-I and E were internalized in HepG2 cells in FBS (show FBXO8 Proteins)-depleted culture medium at the same levels as unmodified liposomes in FBS (show FBXO8 Proteins)-containing culture medium, which indicates that apolipoproteins A-I and E were the major serum components involved in liposomal binding to SR-B1 or LDLR (show LDLR Proteins) (or both).
Here we show that inhibition of SR-B1 reduced cell survival, migration and invasion, and cholesterol content in NB cell lines. Additionally analysis of SR-B1 levels in NB patient biopsies using the R2: Genomics Analysis and Visualization Platform showed that high SR-B1 expression correlated with decreased overall and event-free survival.
These findings uncover a novel role for SR-B1 as a contributor to the capture of specific odorants in the nasal cavity of mammals.
In summary, the authors identified NAP1L1 (show NAP1L1 Proteins) as a novel binding partner of hepatitis c virus NS3 and found that the protease domain of NS3 is responsible for interactions with NAP1L1 (show NAP1L1 Proteins). They demonstrated the functional role of NAP1L1 (show NAP1L1 Proteins) in hepatitis c virus entry through regulating the protein expression of SR-B1.
SR-BI-triggered autophagy promoted co-elimination of apoptotic immune cells and dead bacteria but barely influenced bacterial sequestration and survival or inflammasome activation, thus exclusively counteracting damage inflicted by immune responses.
Overexpression of miR-24 inhibited SR-B1 expression by directly targeting SR-B1 3' UTR and repressed high density lipoprotein uptake and steroidogenesis in steroidogenic cells.
These data suggest that a moderate amount of alcohol plays a novel role in reverse cholesterol transport, mainly mediated by PPARgamma (show PPARG Proteins) and SR-B1.
To investigate the pharmacokinetics (PKs) and pharmacodynamics (PDs (show SLC26A4 Proteins)) for ION-353382, an antisense oligonucleotide (ASO) targeting scavenger receptor class B type I (SRB1) mRNA, using alpha-2-macroglobulin (A2M (show A2M Proteins)), murinoglobulin double-knockout (DKO), and wild-type mice
Rutaecarpine was identified to be a candidate that protected ApoE (show APOE Proteins)(-/-) mice from developing atherosclerosis through preferentially promoting activities of ABCA1 (show ABCA1 Proteins) and SR-BI within RCT (show FOXE3 Proteins).
SR-B1 is a silica receptor associated with canonical inflammasome activation.
Our results suggest that LPA-enhanced foam cell formation is mediated by LPA1 (show LPAR1 Proteins)/3 -AKT (show AKT1 Proteins) activation and subsequent SRBI expression.
Luteinization causes upregulation of SR-BI expression, its posttranslational maturation by glycosylation, and insertion into luteal cell membranes.
Aortic endothelial cells transcytose high-density lipoproteins by mechanisms that involve either SR-BI or ABCG1 (show ABCG1 Proteins) but not ABCA1 (show ABCA1 Proteins).
The protein encoded by this gene is a plasma membrane receptor for high density lipoprotein cholesterol (HDL). The encoded protein mediates cholesterol transfer to and from HDL. In addition, this protein is a receptor for hepatitis C virus glycoprotein E2. Two transcript variants encoding different isoforms have been found for this gene.
scavenger receptor class B member 1
, scavenger receptor class B, member 1
, scavenger receptor class B type I
, high density lipoprotein receptor SR-BI
, CD36 and LIMPII analogous 1
, CD36 antigen (collagen type I receptor, thrombospondin receptor)-like 1
, scavenger receptor class B type III
, HDL QTL 1
, scavenger receptor class B1
, CD36 antigen (collagen type I receptor thrombospondin receptor)-like 1 (scavanger receptor class B type 1)
, scavanger receptor class B type 1
, CD36 antigen (collagen type I receptor, thrombospondin receptor-like 1)