Anti-cyclooxygenase effects of lipid extracts from the New Zealand green-lipped mussel, Perna canaliculus
| Autor: | Theodore A. Macrides, Nicolette Kalafatis, Paul Wynne, Sarah McPhee, D.W. Harney, Lynn D. Hodges, Paul F.A. Wright |
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| Rok vydání: | 2006 |
| Předmět: |
Perna
Time Factors Physiology medicine.medical_treatment Indomethacin Anti-Inflammatory Agents Prostaglandin Biochemistry Gas Chromatography-Mass Spectrometry chemistry.chemical_compound Fish Oils medicine Animals Molecular Biology Perna canaliculus chemistry.chemical_classification Protease Arachidonic Acid biology Fatty acid Mussel Fish oil biology.organism_classification Lipids Enzyme chemistry Prostaglandin-Endoperoxide Synthases Arachidonic acid New Zealand |
| Zdroj: | Comparative biochemistry and physiology. Part B, Biochemistrymolecular biology. 146(3) |
| ISSN: | 1096-4959 |
| Popis: | Total lipid extracts of P. canaliculus (a bivalve marine mollusc native to New Zealand, commonly called the green-lipped mussel) and Mytilus edulis (commonly called the common blue mussel) moderately inhibited ovine COX-1 and COX-2 pure enzymes in vitro. The inhibition was increased after the mussel extracts were saponified by KOH hydrolysis. Protease- and protease-lipase-hydrolysed lipid extracts of P. canaliculus exhibited similarly strong COX inhibition as the KOH-hydrolysed extract. Lyprinol(R) (a commercial extract from P. canaliculus) also exhibited strong inhibition of both COX isoforms, an effect that was increased 10-fold upon subsequent hydrolysis. In contrast, fish oil was not as anti-COX active as Lyprinol. The Lyprinol free fatty acid fraction, and to a lesser extent the Lyprinol triglyceride fraction, were the only lipid classes of Lyprinol to exhibit strong inhibition of the COX isoforms. The purified PUFA extracts were all bioactive, potently inhibiting COX-1 and COX-2. Incubation of Lyprinol in the absence of exogenous arachidonic acid (AA) showed the appearance of alternate prostaglandin metabolites, confirming Lyprinol PUFA as a competitive substrate inhibitor of AA metabolism. |
| Databáze: | OpenAIRE |
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