Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Chemical Compound Review:

AC1NQXKH (5S,6E,8Z,11Z,14Z)-5- hydroperoxyicosa-6,8...

Synonyms: CHEMBL1743204, BSPBio_001445, CHEBI:15632, HMDB01193, BML1-C04, ...

Schwarz, K. et al., Walstra, P. et al., Zhang, L.Y. et al., MacMillan, D.K. et al., Proudfoot, A.E. et al., et al.

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High impact information on LMFA03060012

In the presence of subthreshold inhibitory concentrations of SNO-Glu, the LOOH, 5-hydroperoxy-6,8,11,14-eicosatetraenoic acid, increased platelet aggregation, an effect reversed by GSH-Px [1].
The mechanism of action of 15-lipoxygenase acting as an LTA4 synthase is proposed to involve removing the pro-R hydrogen atom at carbon-10 of 5(S)-HPETE, which is antarafacial to the hydroperoxy group to yield LTA4 [2].
The wild-type 5-lipoxygenase converts 5S-HpETE almost exclusively to leukotriene A(4) as indicated by the dominant formation of leukotriene A(4) hydrolysis products [3].
Synthesis and 5-lipoxygenase inhibitory activity of 5-hydroperoxy-6,8,11,14-eicosatetraenoic acid analogues [4].
Thus, incubation at pH 6.7 led to the formation of 5(S)-HPETE and 15(S)-HPETE in a ratio of 52:48, and incubation at pH 9.8 strongly suppressed production of 5(S)-HPETE and led to formation of 5(S)-HPETE and 15(S)-HPETE in a ratio of 3:97 [5].

Anatomical context of LMFA03060012

Comparison of biological activity with known basophil and eosinophil-activating hydroxyeicosanoids demonstrated similar activity with 5(S)-hydroperoxy-6E,8Z,11Z,14Z-eicosatetraenoic acid (5(S)-HPETE) [6].

Gene context of LMFA03060012

In contrast to bovine platelet 12-lipoxygenase and other 12-lipoxygenases, this enzyme is unable to convert 5(S)-HETE (5(S)-hydroxy,6-trans-8,11,14-cis-eicosatetraenoic acid) or 5(S)-HPETE (5(S)-hydroperoxy,6-trans-8,11,14-cis-eicosatetraenoic acid) into 5(S),12(S)-dihydroxy-6,10-trans,8,14-cis-eicosatetraenoic acid [7].
5(S)-HPETE occasionally increased the K conductance, but failed to occlude the somatostatin response [8].

Analytical, diagnostic and therapeutic context of LMFA03060012

In this study we altered the positional specificity of the human 5-lipoxygenase by multiple site-directed mutagenesis and assayed the leukotriene A(4) synthase activity of the mutant enzyme species with (5S,6E,8Z,11Z,14Z)-5-hydroperoxy-6,8,11,14-eicos atetraenoic acid (5S-HpETE) as substrate [3].

References

Glutathione peroxidase potentiates the inhibition of platelet function by S-nitrosothiols. Freedman, J.E., Frei, B., Welch, G.N., Loscalzo, J. J. Clin. Invest. (1995) [Pubmed]
Eosinophil 15-lipoxygenase is a leukotriene A4 synthase. MacMillan, D.K., Hill, E., Sala, A., Sigal, E., Shuman, T., Henson, P.M., Murphy, R.C. J. Biol. Chem. (1994) [Pubmed]
Alterations in leukotriene synthase activity of the human 5-lipoxygenase by site-directed mutagenesis affecting its positional specificity. Schwarz, K., Gerth, C., Anton, M., Kuhn, H. Biochemistry (2000) [Pubmed]
Synthesis and 5-lipoxygenase inhibitory activity of 5-hydroperoxy-6,8,11,14-eicosatetraenoic acid analogues. Kerdesky, F.A., Schmidt, S.P., Holms, J.H., Dyer, R.D., Carter, G.W., Brooks, D.W. J. Med. Chem. (1987) [Pubmed]
Specificity of two lipoxygenases from rice: unusual regiospecificity of a lipoxygenase isoenzyme. Zhang, L.Y., Hamberg, M. Lipids (1996) [Pubmed]
Isolation of a lipid-soluble histamine release factor from human platelets. Proudfoot, A.E., Gatto, R., Wells, T.N., Bacon, K.B. Biochem. Biophys. Res. Commun. (1994) [Pubmed]
12-Lipoxygenase from bovine polymorphonuclear leukocytes, an enzyme with leukotriene A4-synthase activity. Walstra, P., Verhagen, J., Veldink, G.A., Vliegenthart, J.F. Biochem. Biophys. Res. Commun. (1987) [Pubmed]
The role of arachidonic acid metabolism in somatostatin and substance P effects on inward rectifier K conductance in rat brain neurons. Koyano, K., Grigg, J.J., Velimirovic, B.M., Nakajima, S., Nakajima, Y. Neurosci. Res. (1994) [Pubmed]

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