Results 131 to 140 of about 5,194 (173)
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Kinetic investigation of human 5-lipoxygenase with arachidonic acid
Bioorganic & Medicinal Chemistry Letters, 2016Human 5-lipoxygenase (5-LOX) is responsible for the formation of leukotriene (LT)A4, a pivotal intermediate in the biosynthesis of the leukotrienes, a family of proinflammatory lipid mediators. 5-LOX has thus gained attention as a potential drug target. However, details of the kinetic mechanism of 5-LOX are still obscure.
Monica Mittal +7 more
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Studies on arachidonate 5-lipoxygenase of rat basophilic leukemia cells
Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1984Arachidonate 5-lipoxygenase was partially purified from rat basophilic leukemia cells with the aid of ATP as a ligand linked to Sepharose. The enzyme produced predominantly 5-hydroperoxy-6,8,11,14-eicosatetraenoic acid. Calcium ion was required for the enzyme activity (0.1 mM for half maximal activity), and the calcium-dependent reaction was stimulated
M, Furukawa +3 more
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A selective inhibitor of arachidonate 5-lipoxygenase scavenging peroxide activator
Biochemical Pharmacology, 1997A novel compound termed YT-18 (2,3-dihydro-2,4,6,7-tetramethyl-2-[(4-phenyl-1-piperazinyl) methyl]-5-benzofuranamine) selectively inhibited 5-lipoxygenases of porcine leukocytes (IC50 value, 7.5 microM), human leukocytes (1.5 microM), and rat basophilic leukemia cells (14 microM), which are responsible for bioactive leukotriene synthesis.
H, Suzuki, D, Miyauchi, S, Yamamoto
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Optimization of cofactors which regulate RBL-1 arachidonate 5-lipoxygenase
Biochemical and Biophysical Research Communications, 1989The arachidonate lipoxygenase from rat basophilic leukemia cells (RBL-1) is widely utilized as a model to dissect the primary enzymatic reactions leading to leukotriene formation. The purpose of the present study was to optimize the specific activity of 5-lipoxygenase prepared from a high speed supernatant of RBL-1 cell homogenates.
F R, Cochran, M B, Finch-Arietta
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Lipoxin synthesis by arachidonate 5-lipoxygenase purified from porcine leukocytes
Biochemical and Biophysical Research Communications, 1987Arachidonate 5-lipoxygenase purified from porcine leukocytes produced several more polar compounds from 5,15-dihydroperoxy-eicosatetraenoic acid added as such or generated from 15-hydroperoxy acid. These polar products with absorption maxima at 301-302 nm and shoulders at 289 nm and 316-317 nm were identified as 5S,6R,15S-11-cis-lipoxin A and its 6 ...
N, Ueda +3 more
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Arachidonate 5-lipoxygenase of porcine pancreas: its localization in acinar cells
Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1991Arachidonate 5-lipoxygenase has been found so far in various types of leukocyte. When a homogenate of porcine pancreas was incubated with arachidonic acid, 5-hydroxy-6,8,11,14-eicosatetraenoic acid was predominantly produced concomitant with small amounts of compounds derived from leukotriene A4. After differential centrifugation of the homogenate, the
K, Natsui +4 more
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Kinetic Studies on Arachidonate 5-Lipoxygenase from Rat Basophilic Leukemia Cells
Biological Chemistry Hoppe-Seyler, 1988Arachidonate 5-lipoxygenase of a 10,000 x g supernatant from RBL-1 cell homogenate was studied by a continuous assay measuring enzyme-catalysed oxygen consumption. Parallel HPLC and TLC analysis of arachidonic acid metabolites revealed that the oxygen consumption measured is solely due to 5-lipoxygenation of arachidonic acid. Oxygen consumption by this
M, Haurand, L, Flohé
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Colchicine inhibits arachidonate release and 5-lipoxygenase action in alveolar macrophages
American Journal of Physiology-Lung Cellular and Molecular Physiology, 1996Although colchicine is known to inhibit leukotriene synthesis in neutrophils, its effect on other aspects of arachidonic acid (AA) metabolism as well as its mechanism of action are unknown. To address these questions, we investigated the effects of colchicine on resident rat alveolar macrophages (AM), cells that generate a variety of lipoxygenase and ...
M, Peters-Golden +4 more
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Abstract 3458: Dietary Arachidonic Acid, 5-Lipoxygenase and Myocardial Infarction
Circulation, 2007Five-lipoxygenase (5-LO), the rate-limiting enzyme in the biosynthesis of leukotrienes from arachidonic acid, has been associated with the development of atherosclerosis in mouse models, and a 5-LO promoter repeat polymorphism has been implicated in atherosclerosis in humans. To test the effect of the 5-LO polymorphism on risk of MI and whether dietary
Hannia Campos +3 more
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Arachidonic Acid Stimulates Prostate Cancer Cell Growth: Critical Role of 5-Lipoxygenase
Biochemical and Biophysical Research Communications, 1997Arachidonic acid (5,8,11,14-eicosatetraenoic acid), a member of the omega-6 poly-unsaturated fatty acids, was found to be an effective stimulator of human prostate cancer cell growth in vitro at micromolar concentrations. Selective blockade of the different metabolic pathways of arachidonic acid (e.g.
J, Ghosh, C E, Myers
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