Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1975314 | Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology | 2014 | 8 Pages |
Abstract
Prostaglandins (PG) have been shown to play important physiological roles in insects and marine invertebrates, yet the knowledge of their biosynthetic pathways is often lacking. Recently, we described cyclooxygenases in two amphipod crustaceans, Gammarus sp. and Caprella sp. In the present study, we report the cloning and characterization of prostaglandin E synthases (PGES) from the same organisms. The amphipod membrane-bound PGES-2-type enzymes share about 40% of the amino acid sequence identity with human mPGES-2, contain a conserved Cys110-x-x-Cys113 motif and have very low heme-binding affinity. The recombinant enzymes purified in the absence of dithiothreitol specifically catalyze the isomerization of PGH2 into PGE2. The PGES activity is increased in the presence of reduced glutathione and inhibited with a sulfhydryl group inhibitor. We assume that the amphipod mPGES-2, unlike in their mammalian counterparts, is responsible for PGE2 synthesis, not only in vitro but also in vivo.
Keywords
COXNi-NTAPHMBcPGESPGESHHTmPGESMDAGSTGSHCytosolic prostaglandin E synthasep-hydroxymercuribenzoatecyclooxygenaseArachidonic acidArthropodrapid amplification of cDNA endsCrustaceanmalondialdehydeRaceUTR یا untranslated regions untranslated regionNickel Nitrilotriacetic acidprostaglandin E synthaseprostaglandinhigh performance liquid chromatographyHPLCGlutathioneglutathione S-transferase
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Authors
Kristella Hansen, Külliki Varvas, Ivar Järving, Nigulas Samel,