Inhibition of Platelet Phospholipase A2 Activity by Catuaba Extract Suggests Antiinflammatory Properties
Overview
Affiliations
In the inflammation process, phospholipase A2 (PLA2) catalyses the cleavage of the sn-2 ester-linked fatty acids from phospholipids, being the enzyme responsible for arachidonic acid (AA) release by cells for the biosynthesis of the prostaglandins and thromboxanes via the cyclooxygenase system, and the leukotrienes and eicosatetraenoids via the lipoxygenase pathway. AA mobilization by PLA2 and subsequent prostaglandins synthesis is considered to be a pivotal event in inflammation. Therefore, drugs that inhibit PLA2, thus blocking the COX and LOX pathways in the AA cascade, may be effective in the treatment of inflammatory processes. New strategies for the treatment of inflammatory processes could be detected by a search for active principles of vegetal origin that control the lipid mediator production by inhibition of PLA2. The present data are part of a wide explorative investigation on the effects of Trichilia catigua (catuaba), which found that PLA2 activity was totally inhibited by catuaba at a concentration of 120 microg/mL, suggesting that this natural substance may have antiinflammatory properties.
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