5-Lipoxygenase is not essential in macrophage-mediated oxidation of low-density lipoprotein
Autor: | Victor M. Darley-Usmar, S Bedwell, Wendy Jessup, Vanessa J. O'Leary |
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Rok vydání: | 1991 |
Předmět: |
Indoles
Benzeneacetamides 4 5-Dihydro-1-(3-(trifluoromethyl)phenyl)-1H-pyrazol-3-amine Oxidative phosphorylation Hydroxamic Acids Biochemistry Antioxidants Mice Lipoxygenase chemistry.chemical_compound Animals Humans Masoprocol Macrophage Lipoxygenase Inhibitors Molecular Biology Cells Cultured chemistry.chemical_classification Arachidonate 5-Lipoxygenase biology Macrophages Biological activity Free Radical Scavengers Cell Biology Butylated Hydroxytoluene 5 8 11 14-Eicosatetraynoic Acid Endocytosis Lipoproteins LDL Enzyme chemistry Low-density lipoprotein Arachidonate 5-lipoxygenase biology.protein lipids (amino acids peptides and proteins) Oxidation-Reduction Research Article Lipoprotein |
Zdroj: | Biochemical Journal. 278:163-169 |
ISSN: | 1470-8728 0264-6021 |
DOI: | 10.1042/bj2780163 |
Popis: | The concentration-dependent effects of a series of lipoxygenase inhibitors and antioxidants on the macrophage-mediated oxidative modification of low-density lipoprotein (LDL) were measured. Their influence on macrophage 5-lipoxygenase pathway activity was also studied over the same concentration range. No correlation between inhibition of 5-lipoxygenase and of macrophage-mediated oxidation of LDL was observed. The capacity of the compounds to prevent cell-mediated modification of LDL could be explained in terms of their activity as either aqueous- or lipid-peroxyl radical scavengers. Two potent 5-lipoxygenase inhibitors (MK 886 and Revlon 5901), which had no radical-scavenging properties, were unable to block LDL modification. It is concluded that 5-lipoxygenase is not essential for LDL oxidation by macrophages. |
Databáze: | OpenAIRE |
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