EicosanoidsPub Date : 1997-01-01DOI: 10.1007/978-1-4615-5325-0
D. Kritchevsky, J. Olcese, R. Dantzer, Emmanuele Wollman, D. Crabb, P. Kolodziejczyk, A. L. Munguía
{"title":"Eicosanoids and Other Bioactive Lipids in Cancer, Inflammation, and Radiation Injury 2","authors":"D. Kritchevsky, J. Olcese, R. Dantzer, Emmanuele Wollman, D. Crabb, P. Kolodziejczyk, A. L. Munguía","doi":"10.1007/978-1-4615-5325-0","DOIUrl":"https://doi.org/10.1007/978-1-4615-5325-0","url":null,"abstract":"","PeriodicalId":11520,"journal":{"name":"Eicosanoids","volume":"189 1","pages":"S1-29"},"PeriodicalIF":0.0,"publicationDate":"1997-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"75775309","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Physiology and Pathophysiology of Eicosanoids. Proceedings of a Symposium. Kloster Knechtsteden, January 20-23, 1992.","authors":"","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":11520,"journal":{"name":"Eicosanoids","volume":"5 Suppl ","pages":"S1-65"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12532914","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"A Calluna vulgaris extract 5-lipoxygenase inhibitor shows potent antiproliferative effects on human leukemia HL-60 cells.","authors":"A Najid, A Simon, C Delage, A J Chulia, M Rigaud","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>A water-Calluna vulgaris extract (water-CVE) was found to be a relatively specific arachidonate 5-lipoxygenase inhibitor and showed potent anti-proliferative effects on human leukemic HL60 cells. Water-CVE completely inhibited potato 5-lipoxygenase activity at 250 micrograms/ml, partially inhibited soybean 15-lipoxygenase at pH 7.4 and had no effect either on this 15-lipoxygenase at its optimal activity pH (pH 9) or on Lupinus albus 5-, 8-, 15-lipoxygenase. In culture, the proliferation and DNA synthesis of HL60 cells were decreased by water-CVE in a dose-dependent manner with an IC50 of 200 micrograms/ml at day 4. This effect of water-CVE is related to the starting density of HL60 cells. These results suggest that arachidonate 5-lipoxygenase metabolites and/or leukotrienes could play an essential role in cellular functions of leukemic cells and may explain the success of the use of Calluna vulgaris as tea and baths in folk medicine.</p>","PeriodicalId":11520,"journal":{"name":"Eicosanoids","volume":"5 1","pages":"45-51"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12590460","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Functionally diverse purinergic P2Y-receptors mediate prostanoid synthesis in cultured rat astrocytes: the role of ATP-induced phosphatidyl-inositol breakdown.","authors":"A Seregi, S Doll, A Schobert, G Hertting","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Cultured rat astrocytes possess purinergic P2Y-receptors. Stimulation of these receptors with ATP (10(-3) M) results in increased phosphatidylinositol biphosphate (PIP2)-breakdown and prostanoid formation. We have investigated the relevance of the PIP2-pathway in prostanoid synthesis. The intracellular Ca(2+)-mobilizing agent thapsigargin (TG) (10(-6) M) and the diacylglycerol (DAG)-mimetic tetradecaoylphorbol acetate (TPA) (10(-8)-10(-6) M) both stimulate prostaglandin D2 production. ATP-induced prostanoid formation can be mimicked by combined addition of TG and TPA, suggesting the importance of the second messengers IP3 and DAG, generated during P2Y-receptor mediated PIP2-breakdown. Inhibition of ATP-induced PIP2-hydrolysis by TPA (IC50 about 5 x 10(-8) M) or by 10(-4) M neomycine, however, does not affect astroglial prostanoid synthesis, showing that P2Y-receptor mediated prostanoid formation may occur also in the absence of PIP2-hydrolysis. These findings suggest that additional postreceptor mechanisms exist in the signal transduction chain of ATP-induced astroglial prostanoid synthesis. A possible involvement of phospholipase A2 and/or of Ca(2+)-channels, directly coupled to P2Y-receptors is proposed.</p>","PeriodicalId":11520,"journal":{"name":"Eicosanoids","volume":"5 Suppl ","pages":"S19-22"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12507505","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The role of the epidermal 12-hydroxyeicosatetraenoic acid receptor in the skin.","authors":"T Ruzicka","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The epidermal layer of the skin is the site of active arachidonic acid metabolism. The main product of epidermal keratinocytes is the 12-lipoxygenase derivative 12(S)-hydroxy-eicosatetraenoic acid (12(S)-HETE). Its biological effects in skin are mediated via specific, high affinity binding sites present on both keratinocytes and epidermal antigen presenting Langerhans cells. The main biological effect is chemotaxis of keratinocytes suggesting a physiological role of 12-HETE in cutaneous wound healing. Analysis of 12-HETE receptors in various cutaneous disease states revealed a dramatic defect in lesional and uninvolved psoriatic skin which may represent a central molecular defect in the pathophysiology of the disease.</p>","PeriodicalId":11520,"journal":{"name":"Eicosanoids","volume":"5 Suppl ","pages":"S63-5"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12507508","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
H Kühn, J Belkner, R Wiesner, T Schewe, V Z Lankin, A K Tikhaze
{"title":"Structure elucidation of oxygenated lipids in human atherosclerotic lesions.","authors":"H Kühn, J Belkner, R Wiesner, T Schewe, V Z Lankin, A K Tikhaze","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Oxidative modification of low density lipoproteins and tissue lipids has been proposed to be involved in the pathogenesis of atherosclerosis. We examined human atherosclerotic lesions of various stages from fifteen victims of acute heart failure and detected substantial amounts of oxygenated fatty acids in the tissue ester lipids. The degree of lipid oxygenation correlated with the stage of advancement of the lesion. More than 85% of the oxygenated fatty acids were localized in the cholesterol esters, whereas phospholipids contained only small amounts. Structure elucidation of the oxygenation products indicated a nonspecific product pattern of various isomers of keto- and hydroxy-octadecadienoic acid. The data presented suggest an involvement of lipid peroxidation in the pathogenesis of atherosclerosis and indicate that the majority of the oxygenation products are formed via nonspecific, non-enzymatic reactions possibly initiated by the action of a 15-lipoxygenase.</p>","PeriodicalId":11520,"journal":{"name":"Eicosanoids","volume":"5 1","pages":"17-22"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12589782","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Thromboxane synthase inhibition in allergen challenged sheep lung: effect on eicosanoid synthesis.","authors":"R Dworski, G A FitzGerald, J R Sheller","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>We determined the effect of a novel inhibitor of thromboxane synthase, DP1904, on the baseline and allergen stimulated release of eicosanoids into the bronchoalveolar lavage fluid of sheep. DP1904 was effective in reducing the baseline and allergen stimulated production of TXB2. Inhibition of thromboxane synthase was associated with an increase in other prostaglandin endoperoxide metabolites, PGE2 and PGD2. Diversion of endoperoxide metabolism occurs in sheep lung tissue in vivo.</p>","PeriodicalId":11520,"journal":{"name":"Eicosanoids","volume":"5 1","pages":"35-7"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12589785","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
A Jörres, C Chiabrando, O Kordonouri, A Schiessler, S Hess, S Farke, G M Gahl, C Müller, L Rivoltella, R Djurup
{"title":"Thromboxane B2 urinary metabolites in patients undergoing cardiopulmonary bypass.","authors":"A Jörres, C Chiabrando, O Kordonouri, A Schiessler, S Hess, S Farke, G M Gahl, C Müller, L Rivoltella, R Djurup","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The urinary excretion of selected markers for renal injury and thromboxane metabolites was studied in 16 patients undergoing cardiopulmonary bypass (CPB). Excretion of both tubular and glomerular markers sharply increased on day 1 after CPB and remained elevated throughout the observation period (five days). Immunoreactive thromboxane B2 (i-TXB2, mainly reflecting 2,3-dinor-TXB2) and immunoreactive 11-keto-thromboxane B2 (i-11-keto-TXB2) were measured by direct enzyme immunoassays. TXB2, 2,3-dinor-TXB2 and 11-keto-TXB2 were also measured in selected samples by GC-MS. Urinary excretion rates of both i-TXB2 and i-11-keto-TXB2 markedly increased on day 1 after surgery and decreased thereafter. Following CPB, excretion rates of 2,3-dinor-TXB2 and TXB2 displayed parallel changes, suggesting that in these patients most urinary TXB2 derives from blood platelets rather than the kidney. Taken together, our observations do not support the hypothesis that acute renal injury observed after CPB is caused by exaggerated thromboxane biosynthesis in the kidney.</p>","PeriodicalId":11520,"journal":{"name":"Eicosanoids","volume":"5 3-4","pages":"147-51"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12467464","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Loss of cytosolic 15-lipoxygenase activity in A23187-stimulated human leukocytes: involvement of a translocation process?","authors":"M Bongrazio, A Roscher, P Ludwig, S Nigam","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>We focused our study on the subcellular redistribution of 15-lipoxygenase in human leukocytes challenged with A23187 and arachidonic acid (AA). We found that in cytosolic fractions of stimulated cells the 15-lipoxygenase (15-LO) activity, measured as 15-HETE, was 65% less than in controls. However, no activity was found in cell membranes. This effect was complete within 2 min of incubation and was correlated in a dose dependent manner to exogenously added AA. No significant difference in cytosolic distribution of 15-LO activity was observed when cells were stimulated in presence of various concentrations of Ca++. Immunoblot analysis showed that the loss of cytosolic 15-LO activity registered after challenging with A23187 was associated with a concomitant loss of the enzyme content in the cytosol, suggesting the possibility of a translocation process. Neither the 15-LO activity nor the enzyme was, however, found in the cell membrane under our present experimental conditions. But, addition of protease inhibitors showed a slight increase of 15-LO activity in the membrane fraction. Despite the small effect, this may indicate a translocation of 15-LO following challenge of human leukocytes with A23187.</p>","PeriodicalId":11520,"journal":{"name":"Eicosanoids","volume":"5 3-4","pages":"191-5"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12467467","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
J Van Wauwe, M C Coene, G Van Nyen, W Cools, L Le Jeune, W Lauwers
{"title":"Suggested mechanism for the formation of 15-hydroxyeicosatrienoic acid by rat epidermal microsomes.","authors":"J Van Wauwe, M C Coene, G Van Nyen, W Cools, L Le Jeune, W Lauwers","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>We have previously demonstrated that rat epidermal microsomes NADPH-dependently convert 15(S)-hydroperoxy-5,8,11,13-eicosatetraenoic acid (15-HPETE) into 15-hydroxy-5,8,11-eicosatrienoic acid (15-HETrE). The present study examines the mechanism of this reductive conversion. Rat epidermal microsomes were incubated with [1-14C]15-HPETE in the presence and absence of NADPH. Major reaction products were purified by high performance liquid chromatography (HPLC) and analyzed by gas chromatography-mass spectrometry (GC-MS), UV spectroscopy and/or cochromatography with standard products. In the presence of NADPH, 15-HPETE was transformed to 13-hydroxy-14,15-epoxy-5,8,11-eicosatrienoic acid (13-HEpETrE), 15(S)-hydroxy-5,8,11,13-eicosatetraenoic acid (15-HETE), 15-keto-5,8,11-eicosatrienoic acid (15-KETrE) and 15-hydroxy-5,8,11-eicosatrienoic acid (15-HETrE). In the absence of NADPH, the microsomes reacted with 15-HPETE to form 13-HEpETrE, 15-keto-5,8,11,13-eicosatetraenoic acid (15-KETE) and 15-HETE. Furthermore, when supplemented with NADPH, epidermal microsomes converted 15-KETE to 15-KETrE, which was subsequently reduced to 15-HETrE. These data suggest that rat epidermal microsomes are capable of metabolizing 15-HPETE to 15-HETrE via the following reaction steps: conversion of HPETE to KETE, NADPH-dependent double bond saturation in KETE to KETrE and keto-reduction of the latter compound to HETrE.</p>","PeriodicalId":11520,"journal":{"name":"Eicosanoids","volume":"5 3-4","pages":"141-6"},"PeriodicalIF":0.0,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12466827","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}