The inhibition of the oxidation of low density lipoprotein by (+)-Catechin, a naturally occurring flavonoid
| Autor: | G.D. Bell, Andrew M. Salter, H Mangiapane, S Brown, J. E. M. Thomson, David A. White |
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| Rok vydání: | 1992 |
| Předmět: |
Lipoproteins
Flavonoid Biochemistry Catechin Monocytes Mice chemistry.chemical_compound In vivo Animals Humans Cell Line Transformed Flavonoids Pharmacology chemistry.chemical_classification HEPES Macrophages Biological activity Free Radical Scavengers In vitro Lipoproteins LDL chemistry Cell culture Low-density lipoprotein lipids (amino acids peptides and proteins) Endothelium Vascular Oxidation-Reduction |
| Zdroj: | Biochemical Pharmacology. 43:445-450 |
| ISSN: | 0006-2952 |
| DOI: | 10.1016/0006-2952(92)90562-w |
| Popis: | (+)-Catechin inhibited the copper-catalysed oxidation of human low density lipoprotein (LDL) in a dose-dependent manner with complete inhibition at 20 micrograms/mL. The flavonoid at a concentration of 50 micrograms/mL also inhibited oxidation of LDL induced by the mouse transformed macrophage J774, human monocyte-derived macrophages and vascular endothelial cells isolated from human umbilical cords. LDL modified by copper-catalysed or cell-induced oxidation was endocytosed and degraded by human macrophages at a much greater rate than native LDL. LDL reisolated from copper or cell incubations in the presence of (+)-catechin was endocytosed and degraded at rates similar to native LDL. (+)-Catechin appeared to inhibit the uptake and degradation by macrophages of cell-modified LDL. The actions of (+)-catechin on cell-induced oxidation of LDL are consistent with the ability of flavonoids of similar structure to inhibit lipoxygenases and with a role for lipoxygenases in cell-induced modification of LDL in vivo. |
| Databáze: | OpenAIRE |
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