Results 141 to 150 of about 3,171 (185)
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Journal of Lipid Mediators and Cell Signalling, 1995
In this article, it has been attempted to review data primarily on the activation of human 5-lipoxygenase, in vitro and in the cell. First, structural properties and enzyme activities are described. This is followed by the activating factors: Ca2+, membranes, ATP, and lipid hydroperoxide.
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In this article, it has been attempted to review data primarily on the activation of human 5-lipoxygenase, in vitro and in the cell. First, structural properties and enzyme activities are described. This is followed by the activating factors: Ca2+, membranes, ATP, and lipid hydroperoxide.
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Platelet-Type Arachidonate 12-Lipoxygenase
1996In human platelets arachidonic acid is released from membrane phospholipids by the catalysis of phosopholipase A2, and then oxygenated either by cyclooxygenase or by 12-lipoxygenase. It is well known that the cyclooxygenase pathway leads to the synthesis of pro-aggregatory and vasoconstrictive thromboxane A2.
M, Nakamura +5 more
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Arachidonate lipoxygenase in blood platelets
Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1975Abstract Blood platelets contain a lipoxygenase which converts eicosapolyenoic acids with at least two cis double bonds at the 8- and 11-position into l -12-hydroperoxy acids. The enzyme responsible is found in the supernatant of broken platelets.
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Arachidonate lipoxygenase activity in human fetal lung
European Journal of Pharmacology, 1982The results are suggestive of the presence of lipoxygenase activity in human fetal lung. Since human fetal lung produces PG's and since the lipoxygenase products, HETE and its labile hydroperoxy precursor, HPETE have been proposed as potentially important mediators for many biological activities, the formation of these compounds including PGs early in ...
Saeed, Sheikh A., Mitchell, Murray D.
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Arachidonate 5-lipoxygenase and its new inhibitors
Journal of Allergy and Clinical Immunology, 1984The 5-lipoxygenases of guinea pig peritoneal polymorphonuclear leukocytes and of rat basophilic leukemia cells have been solubilized, purified partially by affinity chromatography, and shown to convert arachidonic acid principally to 5-hydroperoxy-6,8,11,14- eicosatetraenoic acid.
S, Yamamoto +4 more
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Flavonoids: Potent inhibitors of arachidonate 5-lipoxygenase
Biochemical and Biophysical Research Communications, 1983Various flavonoids were found to be relatively selective inhibitors of arachidonate 5-lipoxygenase which initiates the biosynthesis of leukotrienes with the activity of slow reacting substance of anaphylaxis. Cirsiliol (3',4',5-trihydroxy-6,7-dimethoxyflavone) was most potent, and the enzyme partially purified from rat basophilic leukemia cells was ...
T, Yoshimoto +4 more
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Lipoxygenase Metabolism of Arachidonic Acid in Brain
Journal of Neurochemistry, 1985Abstract: When blood‐free mouse brain slices were incubated with exogenous radiolabeled arachidonic acid, gas chromatography/mass spectrometry confirmed that the major radioactive lipoxygenase enzyme product of arachidonic acid was 12‐hydroxy‐5,8,10,14‐eicosatetraenoic acid (12‐HETE), with lesser amounts of 5‐hydroxy‐6,8,11,14‐eicosatetraenoic acid ...
S A, Adesuyi +3 more
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Chapter 20. Arachidonate Lipoxygenase
1981Publisher Summary Lipoxygenases are enzymes that catalyze the hydroperoxidation of polyunsaturated fatty acids, esters, alcohols, and others containing a cis-cis-1,4-pentadiene system; the products contain 1-hydroperoxy-2,4-trans, cispentadiene fragments.
Denis M. Bailey, Lawrence W. Chakrin
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Nuclear Import of Arachidonate 5-Lipoxygenase
2001Leukotrienes are lipid messenger molecules that are secreted by leukocytes to orchestrate a rapid and prolonged immune response. The enzyme 5-lipoxygenase catalyzes the rate-limiting first two steps in the synthesis of leukotrienes from arachidonic acid.
T G, Brock, A M, Healy
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