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Thomas, Douglas D.

Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

12 Issues per year


IMPACT FACTOR 2016: 3.273

CiteScore 2016: 3.01

SCImago Journal Rank (SJR) 2015: 1.607
Source Normalized Impact per Paper (SNIP) 2015: 0.751

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1437-4315
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In This Section
Volume 383, Issue 3-4 (Apr 2002)

Issues

15-Lipoxygenase-1: A Prooxidant Enzyme

T. Schewe
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.2002.041

Abstract

Human and rabbit reticulocyte 15-lipoxygenase (15-lipoxygenase-1) and the leukocytetype 12-lipoxygenases (12/15-lipoxygenases) of pig, beef, mouse and rat constitute a particular subfamily of mammalian lipoxygenases (reticulocytetype lipoxygenases) with unique properties and functions. They catalyze enzymatic lipid peroxidation in complex biological structures via direct dioxygenation of phospholipids and cholesterol esters of biomembranes and plasma lipoproteins. Moreover, they are a source of free radicals initiating nonenzymatic lipid peroxidation and other oxidative processes. Expression and activity of reticulocytetype lipoxygenases are highly regulated. Moreover, the susceptibility of intracellular membranes toward these lipoxygenases is controlled and may be increased together with lipoxygenase activity under conditions of oxidative stress. Thus, oxidative stress may favor a concerted package of lipoxygenase mediated enzymatic and nonenzymatic lipid peroxidation and cooxidative processes. Reaction of reticulocytetype lipoxygenases with lowdensity lipoprotein renders the latter atherogenic and appears to be involved in the formation of atherosclerotic lesions.

About the article

Published Online: 2005-06-01

Published in Print: 2002-04-12



Citation Information: Biological Chemistry, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2002.041. Export Citation

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