Lipoxygenase in trout gill tissue acting on arachidonic, eicosapentaenoic and docosahexaenoic acids

J. Bruce German, Geza G. Bruckner, John E. Kinsella

Research output: Contribution to journalArticle

Abstract

Lipoxygenase activity was characterized in the gill tissue of fresh-water trout. Incubation of arachidonic acid with gill preparations yielded 12-hydroxyeicosatetraenoic acid as the major product, suggesting a 12-lipoxygenase. Eicosapentaenoic acid was similarly converted to the 12-hydroxyeicosapentaenoic acid. Both arachidonic acid and docosahexaenoic acid were converted with equal apparent velocities and affinities into single monohydroxy derivatives. Analyses of the hydroxy product of docosahexaenoic acid were consistent with 14-hydroxydocosahexaenoic acid. This enzyme activity was localized to the cytosolic fraction and displayed a broad pH optimum around pH 7. The enzyme was insensitive to the cyclooxygenase inhibitors indomethacin and aspirin but activity was strongly inhibited in the presence of the lipoxygenase inhibitors, SnCl2(5 mM), esculetin (10 μM) and eicosatetraynoic acid (100 μM).

Original languageEnglish (US)
Pages (from-to)12-20
Number of pages9
JournalBiochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
Volume875
Issue number1
DOIs
StatePublished - Jan 3 1986
Externally publishedYes

Fingerprint

Eicosapentaenoic Acid
Lipoxygenase
Docosahexaenoic Acids
Trout
Arachidonic Acid
Arachidonate 12-Lipoxygenase
Tissue
Hydroxyeicosatetraenoic Acids
Lipoxygenase Inhibitors
Cyclooxygenase Inhibitors
Enzyme activity
Enzymes
Fresh Water
Indomethacin
Aspirin
Derivatives
Acids
Water
esculetin
14-hydroxydocosahexaenoic acid

Keywords

  • (Trout gill)
  • Eicosanoid metabolism
  • Lipoxygenase
  • Polyunsaturated fatty acid

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Endocrinology

Cite this

Lipoxygenase in trout gill tissue acting on arachidonic, eicosapentaenoic and docosahexaenoic acids. / Bruce German, J.; Bruckner, Geza G.; Kinsella, John E.

In: Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism, Vol. 875, No. 1, 03.01.1986, p. 12-20.

Research output: Contribution to journalArticle

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AU - Kinsella, John E.

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N2 - Lipoxygenase activity was characterized in the gill tissue of fresh-water trout. Incubation of arachidonic acid with gill preparations yielded 12-hydroxyeicosatetraenoic acid as the major product, suggesting a 12-lipoxygenase. Eicosapentaenoic acid was similarly converted to the 12-hydroxyeicosapentaenoic acid. Both arachidonic acid and docosahexaenoic acid were converted with equal apparent velocities and affinities into single monohydroxy derivatives. Analyses of the hydroxy product of docosahexaenoic acid were consistent with 14-hydroxydocosahexaenoic acid. This enzyme activity was localized to the cytosolic fraction and displayed a broad pH optimum around pH 7. The enzyme was insensitive to the cyclooxygenase inhibitors indomethacin and aspirin but activity was strongly inhibited in the presence of the lipoxygenase inhibitors, SnCl2(5 mM), esculetin (10 μM) and eicosatetraynoic acid (100 μM).

AB - Lipoxygenase activity was characterized in the gill tissue of fresh-water trout. Incubation of arachidonic acid with gill preparations yielded 12-hydroxyeicosatetraenoic acid as the major product, suggesting a 12-lipoxygenase. Eicosapentaenoic acid was similarly converted to the 12-hydroxyeicosapentaenoic acid. Both arachidonic acid and docosahexaenoic acid were converted with equal apparent velocities and affinities into single monohydroxy derivatives. Analyses of the hydroxy product of docosahexaenoic acid were consistent with 14-hydroxydocosahexaenoic acid. This enzyme activity was localized to the cytosolic fraction and displayed a broad pH optimum around pH 7. The enzyme was insensitive to the cyclooxygenase inhibitors indomethacin and aspirin but activity was strongly inhibited in the presence of the lipoxygenase inhibitors, SnCl2(5 mM), esculetin (10 μM) and eicosatetraynoic acid (100 μM).

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