Upon induction of metamorphosis, larvae of the marine hydroid Hydractinia echinata release [C-14]-arachidonic acid from previously labeled endogenous sources. The lipoxygenase inhibitors nordihydroguaiaretic acid and 5,8,11,14-eicosatetraynoic acid inhibited metamorphosis induced by Cs+ and 1,2-sn-dioctanoylglycerol, whereas the inhibitors of cyclooxygenase, indomethacin, and acetylsalicylic acid were ineffective, suggesting a role for lipoxygenase metabolites of arachidonic acid in induction of metamorphosis. Lipoxygenase products in Hydractinia echinata were isolated and identified by gas chromatography/mass spectrometry. 8- and 18-HETE were the most abundant metabolites. In cytosolic fractions from larvae activity of an arachidonic acid metabolizing enzyme, presumably a lipoxygenase, was found. The metabolic product was identified by H-1-NMR and chiral phase HPLC as 8(R)-HETE. Its production was strongly inhibited by NDGA, but not by indomethacin.

Possible involvement of arachidonic acid and eicosanoids in metamorphic events in Hydractinia echinata (Coelenterata; Hydrozoa).

De Petrocellis L;Di Marzo V
1994

Abstract

Upon induction of metamorphosis, larvae of the marine hydroid Hydractinia echinata release [C-14]-arachidonic acid from previously labeled endogenous sources. The lipoxygenase inhibitors nordihydroguaiaretic acid and 5,8,11,14-eicosatetraynoic acid inhibited metamorphosis induced by Cs+ and 1,2-sn-dioctanoylglycerol, whereas the inhibitors of cyclooxygenase, indomethacin, and acetylsalicylic acid were ineffective, suggesting a role for lipoxygenase metabolites of arachidonic acid in induction of metamorphosis. Lipoxygenase products in Hydractinia echinata were isolated and identified by gas chromatography/mass spectrometry. 8- and 18-HETE were the most abundant metabolites. In cytosolic fractions from larvae activity of an arachidonic acid metabolizing enzyme, presumably a lipoxygenase, was found. The metabolic product was identified by H-1-NMR and chiral phase HPLC as 8(R)-HETE. Its production was strongly inhibited by NDGA, but not by indomethacin.
1994
Istituto di Chimica Biomolecolare - ICB - Sede Pozzuoli
Istituto di Scienze Applicate e Sistemi Intelligenti "Eduardo Caianiello" - ISASI
PROTEIN-KINASE-C
HYDROXYEICOSATETRAENOIC ACIDS
HYDRA-VULGARIS
2ND MESSENGERS
PHOSPHOLIPASE-A2
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/20.500.14243/225509
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