Human 15-lipoxygenase-1 (LO) possesses mainly 15-lipoxygenase activity whereas the animal ortholog 12/15-LO possesses mainly 12-lipoxygenase activity. These findings have raised the question if studies on animals can predict the function of 15-LO-1 in human. In this study we have characterized the arachidonic acid metabolites formed by porcine 12/15-LO. Mini pigs were infected with a parasite to increase the number of blood eosinophils, which highly express 12/15-LO. Isolated porcine polymorphonuclear leukocytes (PMNL) were incubated with arachidonic acid and the produced metabolites were analysed with HPLC and mass spectrometry (MS). The cells were found to produce 15-hydroxyeicosatetraenoic acid (HETE) and 12-HETE at a ratio of 1:5. Furthermore 8,15-dihydroxyeicosatetraenoic acids (DiHETEs) and 14,15-DiHETE were formed. Based on HPLC, UV-spectroscopy and MS analysis it was found that porcine PMNL also produced eoxin (EX) C4. These results demonstrate that although porcine 12/15-LO possesses primarily 12-lipoxygenase activity, the enzyme can catalyse the formation of EXC(4).
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.plefa.2012.07.003 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Biosynthesis of eoxin C4 by porcine leukocytes.
Prostaglandins Leukot Essent Fatty Acids
February 2013
Department of Medicine, Karolinska University Hospital and Karolinska Institutet, Solna, SE-171 76 Stockholm, Sweden.
Human 15-lipoxygenase-1 (LO) possesses mainly 15-lipoxygenase activity whereas the animal ortholog 12/15-LO possesses mainly 12-lipoxygenase activity. These findings have raised the question if studies on animals can predict the function of 15-LO-1 in human. In this study we have characterized the arachidonic acid metabolites formed by porcine 12/15-LO.
View Article and Find Full Text PDFCloning, purification and characterization of non-human primate 12/15-lipoxygenases.
Prostaglandins Leukot Essent Fatty Acids
May 2010
Orexo AB, P.O. Box 303, 751 05 Uppsala, Stockholm, Sweden.
The enzyme 15-lipoxygenase-1 (15-LO-1) possesses mainly 15-LO activity and has so far only been described in human cells and rabbit reticulocytes. The animal ortholog, except rabbit reticulocytes, is an enzyme with predominantly a 12-lipoxygenase activity, commonly referred to as 12/15-LO. We describe herein the characterization of the 12/15-LOs in Macaca mulatta (rhesus monkey) and in Pongo pygmaeus (orang-utan).
View Article and Find Full Text PDF12/15-Lipoxygenase gene disruption attenuates atherogenesis in LDL receptor-deficient mice.
Circulation
October 2001
Institute of Lipid and Atherosclerosis Research, Sheba Medical Center, Tel-Hashomer, Sackler Faculty of Medicine, Tel-Aviv University, Israel.
Background: Human 15-lipoxygenase (LO) and its murine analogue 12/15-LO are capable of directly oxidizing esterified fatty acids in lipoproteins and phospholipids. Because these oxidized products possess atherogenic properties, it was suggested that LOs may be involved in enhancing atherogenesis. Previous in vivo tests of the role of LOs in atherogenesis animal models, however, have yielded conflicting results.
View Article and Find Full Text PDFCo-regulated expression of glomerular 12/15-lipoxygenase and interleukin-4 mRNAs in rat nephrotoxic nephritis.
Kidney Int
August 1994
Department of Medicine, Emory University, Atlanta, Georgia.
Arachidonate 12- and 15-lipoxygenase (LO) products are generated in experimental glomerulonephritis. 15-S-HETE (a 15-LO product) and lipoxins (interaction products between 5-LO and either 12-LO or 15-LO) counteract the proinflammatory actions of leukotrienes. IL-4 has been shown to up-regulate 15-LO gene expression in human leukocytes.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!