Name | LDLR |
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Synonyms | FH; FHC; LDL receptor; LDLR; Low density lipoprotein receptor; Low density lipoprotein receptor precursor; low density lipoprotein receptor (familial hypercholesterolemia); LDL receptors… |
Name | sodium chlorate |
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CAS | sodium chlorate |
PubMed | Abstract | RScore(About this table) | |
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20056109 | Murray-Taylor FM, Ho YY, Densupsoontorn N, Chang CL, Deckelbaum RJ, Seo T: n-3, but not n-6 lipid particle uptake requires cell surface anchoring. Biochem Biophys Res Commun. 2010 Feb 5;392(2):135-9. Epub 2010 Jan 7. PG removal by sodium chlorate in LDLR+/+ cells substantially reduced n-3 TGRP uptake but had little effect on n-6 TGRP uptake. |
33(0,1,1,3) | Details |
9221767 | Tolar M, Marques MA, Harmony JA, Crutcher KA: Neurotoxicity of the 22 kDa thrombin-cleavage fragment of apolipoprotein E and related synthetic peptides is receptor-mediated. J Neurosci. 1997 Aug 1;17(15):5678-86. Effective inhibitors of neurotoxicity of both the apoE peptides and the apoE fragment include heparan sodium chlorate and heparinase, the low-density lipoprotein (LDL) receptor-related protein receptor-associated protein, and a polyclonal anti-LDL receptor-related protein antibody. |
31(0,1,1,1) | Details |
14585398 | Gao R, Brigstock DR: Low density lipoprotein receptor-related protein (LRP) is a -dependent adhesion receptor for connective tissue growth factor (CTGF) in rat activated hepatic stellate cells. Hepatol Res. 2003 Nov;27(3):214-220. Co-incubation of CTGF with or perturbation of cell surface HSPGs with heparinase or sodium chlorate completely blocked adhesion of activated HSCs to all CTGF isoforms. |
1(0,0,0,1) | Details |
9359432 | Mast AE, Higuchi DA, Huang ZF, Warshawsky I, Schwartz AL, Broze GJ Jr: Glypican-3 is a binding protein on the HepG2 cell surface for tissue factor pathway inhibitor. Biochem J. 1997 Oct 15;327 ( Pt 2):577-83. In addition, when the sulphation of glycosaminoglycans (GAGs) is prevented by growing the HepG2 cells in the presence of 30 mM sodium chlorate, TFPI binding is unaffected, whereas the binding of bovine lipoprotein lipase, a protein known to associate with cell-surface GAGs, falls to 50% of control levels. TFPI is internalized and degraded by HepG2 cells through the low-density-lipoprotein receptor-related protein (LRP) but also binds another molecule present on the cell surface at approx. 10-fold the abundance of LRP [Warshawsky, Broze and Schwartz (1994) Proc. |
1(0,0,0,1) | Details |
10191300 | Dominguez SR, Miller-Auer H, Reardon CA, Meredith SC: Peptide model of a highly conserved, N-terminal domain of apolipoprotein E is able to modulate lipoprotein binding to a member of the class A scavenger receptor family. J Lipid Res. 1999 Apr;40(4):753-63. Peptide models of a highly conserved, N-terminal domain of this protein have been shown to increase the binding of low density lipoprotein (LDL) to fibroblast cell surfaces independently of the low density lipoprotein receptor. |
1(0,0,0,1) | Details |
8728315 | Tam SP, Zhang X, Koschinsky ML: Interaction of a recombinant form of apolipoprotein [a] with human fibroblasts and with the human hepatoma cell line HepG2. J Lipid Res. 1996 Mar;37(3):518-33. The addition of alpha 2-macroglobulin as well as treatment with heparinase, chondroitinase ABC, and sodium chlorate did not decrease total specific binding of r-apo [a], suggesting that neither the low density lipoprotein receptor-related protein nor cell surface proteoglycans are involved in r-apo [a] clearance. |
0(0,0,0,0) | Details |
9837867 | Allen S, Khan S, Tam S, Koschinsky M, Taylor P, Yacoub M: Expression of adhesion molecules by lp (a): a potential novel mechanism for its atherogenicity. FASEB J. 1998 Dec;12(15):1765-76. Addition of alpha2-macroglobulin as well as treatment with heparinase, chondroitinase ABC, and sodium chlorate did not decrease levels of VCAM-1 and E-selectin stimulated by Lp (a), suggesting that neither the low density lipoprotein receptor-related protein nor cell-surface proteoglycans are involved in Lp (a)-induced adhesion molecule production. |
0(0,0,0,0) | Details |
7605368 | Sehayek E, Olivecrona T, Bengtsson-Olivecrona G, Vlodavsky I, Levkovitz H, Avner R, Eisenberg S: Binding to is a major event during catabolism of lipoprotein lipase by HepG2 and other cell cultures. Atherosclerosis. 1995 Apr 7;114(1):1-8. LPL metabolism in HepG2 cells was characterized by a high capacity to degrade the enzyme, an extremely high sensitivity to and was inhibited by 60%-70% after treatment of the cells with sodium chlorate and heparinase (but not chondroitinase). |
0(0,0,0,0) | Details |