Lipoxygenase catalyzed oxygenation of hydroxy fatty acids to lipoxins

Adv Exp Med Biol. 1988:229:39-49. doi: 10.1007/978-1-4757-0937-7_4.

Abstract

The pure lipoxygenases from rabbit reticulocytes and soybeans convert a variety of substrates (arachidonic acid, 15-HPETE, 15-HETE, 5-HETE, various DiHETE isomers) to trihydroxy eicosanoids containing a conjugated tetraene system (lipoxins). In general, the methyl esters are better substrates for lipoxin formation than are the free acids. Lipoxygenase inhibitors (5,8,11,14-eicosatetraynoic acid, nordihydroguaiaretic acid) strongly inhibit the lipoxin formation. The complete stereochemistry of the lipoxin B formed from 15S-HETE methyl ester has been established by co-chromatography with authentic standards on various types of HPLC columns, by GC/MS analysis, by gas liquid chromatography of the ozonolysis fragments of the menthoxy carbonyl derivatives and 1H-NMR studies. The molar absorption coefficient of the conjugated tetraenes was measured as epsilon 301 = 53,000. The lipoxins formed from 15-HETE and various DiHETE isomers are formed exclusively via the oxygenation pathway as shown by experiments under an 17O2 atmosphere and/or by anaerobic incubations. Our results indicate that lipoxins can be synthesized via lipoxygenase-catalyzed sequential oxygenation of polyenoic fatty acids and their hydro(pero)xy derivatives.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Esters / metabolism
  • Glycine max / enzymology
  • Hydroxy Acids / metabolism*
  • Hydroxyeicosatetraenoic Acids / biosynthesis*
  • Hydroxyeicosatetraenoic Acids / metabolism
  • Lipoxins*
  • Lipoxygenase / metabolism*
  • Oxidation-Reduction
  • Rabbits
  • Reticulocytes / enzymology
  • Spectrophotometry, Ultraviolet
  • Substrate Specificity

Substances

  • Esters
  • Hydroxy Acids
  • Hydroxyeicosatetraenoic Acids
  • Lipoxins
  • 15-hydroxy-5,8,11,13 eicosatetraenoic acid methyl ester
  • 15-hydroxy-5,8,11,13-eicosatetraenoic acid
  • lipoxin B4
  • Lipoxygenase