SR-BIScavenger Receptor Class B Type I (vitamin E transport)
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It has been documented that both [alpha]1 (large HDL) and [alpha]2 (medium HDL) particles participate in cell cholesterol efflux via the SR-BI pathway (21, 22); therefore, correct measurement of these HDL subfractions is important for assessing HDL functionality.
These pathways include two ABC-transporters, ABCA1 and ABCG1, along with SR-BI and passive aqueous diffusion [125].
Figure 3 shows CYP7A1, ABCG8, NPC1L1, HMG-CoAR, SREBP-1c, ABCA1, and SR-BI mRNA levels in the liver determined by qRT-PCR.
Leptin induces the hepatic high density lipoprotein receptor scavenger receptor B type I (SR-BI) but not cholesterol 7alpha-hydroxylase (Cyp7a1) in leptin-deficient (ob/ob) mice.
Consistent with our expectations, gene analysis and protein detection consistently showed that pioglitazone strongly inhibited the expression of SR-BI in the liver.
Although the DiI-HDL uptake is significantly higher in infected WT hepatocytes compared to the SR-BI-/- counterparts (P < 0.01), Ad-ATPase-B1 infection increased DiI-HDL uptake similarly in both groups (Table 1), suggesting that the lack of SR-BI does not affect ATPase-B1 function.
It is believed that SR-BI has a role in host defense [58] because of the upregulation of its expression during phagocytic and dendritic differentiation of monocytes and because of the suppression of its expression in monocytes and macrophages, exposed to proinflammatory stimuli [59].
SR-BI is a receptor for high-density lipoproteins (HDL) that are commonly referred to as 'good cholesterol' because they help transport cholesterol out of the arteries and back to the liver for excretion.
When cultures were more than 90% confluent, cells were pretreated for 1 hr with 10 [micro]M block lipid transport-1 (BLT-1) in MEM containing 0.5% FAF-BSA, to inhibit SR-BI. Control cells were treated with the DMSO vehicle.
Conversely, cholesterol efflux is mediated by SR-BI and ATP-binding cassette (ABC) transporters such as ABCA1 and ABCG1 [5-10].