Cell
Genetics of the LDL receptor: Evidence that the mutations affecting binding and internalization are allelic
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Cited by (96)
Non-coding RNAs in lipid metabolism
2019, Vascular PharmacologyCitation Excerpt :Importantly, post-transcriptional inhibition of MTP expression and VLDL secretion by miR-30c did not result in steatosis in the liver, suggesting that miR-30c might have therapeutic potential as an anti-hyperlipidemic and anti-atherosclerotic agent [96]. The clearance of LDL by the LDLR and the role of LDLR in cardiovascular disease have been extensively studied [101, 102]. Defects in the LDLR are the most common cause of familial hypercholesterolemia (FH) characterized by very high circulating LDL-C levels and premature coronary artery disease [101].
Phlorizin treatment attenuates obesity and related disorders through improving BAT thermogenesis
2016, Journal of Functional FoodsCitation Excerpt :Phlorizin and simvastatin alleviated obesity and its related disorders. Simvastatin is a rate limiting enzyme involved in de novo cholesterol synthesis and effectively reduces serum cholesterol levels through the inhibition of cholesterol synthesis (Goldstein, Brown, & Stone, 1977). It's the most widely prescribed drug to treat hypercholesterolaemia and associated metabolic disorders.
Quantitative fl uorescence imaging reveals point of release for lipoproteins during LDLR-dependent uptake
2013, Journal of Lipid ResearchCitation Excerpt :In support of this possibility, the total LDL fluorescence intensity associated with LDLR-ΔBC cells fell rapidly during the chase with kinetics that mirrored the rate of LDL dissociation from the LDLR-ΔBC (Fig. 5C, D). Published work has shown that a fraction of both LDL and β-VLDL that is internalized by the LDLR is excreted through a process termed retro-endocytosis (23, 33, 34). We tested whether the BC deletion specifically augmented retro-endocytosis of LDL by comparing LDL and β-VLDL degradation and excretion in pulse-chase experiments using 125I-labeled LDL and β-VLDL.
Molecular characterization of proprotein convertase subtilisin/kexin type 9-mediated degradation of the LDLR
2012, Journal of Lipid ResearchCitation Excerpt :Inactivation of ARH in cultured hepatocytes (HuH7 cells) using two different siRNAs also interfered with PCSK9-stimulated LDLR degradation (Fig. 1B), which is consistent with previous findings (10). Previous studies have reported that PCSK9 does not promote LDLR degradation in fibroblasts (10), a cell type that does not require ARH for LDL uptake (32). It has been proposed that DAB2, another related adaptor protein, substitutes for ARH in fibroblasts (33).
Long-term survival of childhood coronary artery disease in a patient severely affected with familial hypercholesterolemia
2004, American Journal of CardiologyGenetic Approaches to Cardiovascular Disease
2004, Molecular Basis of Cardiovascular Disease: A Companion to Braunwald's Heart Disease