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Inhibition of platelet phospholipase A 2 activity by catuaba extract suggests antiinflammatory properties
Author(s) -
Barbosa Nádia R.,
Fischmann Lygia,
Talib Leda L.,
Gattaz Wagner F.
Publication year - 2004
Publication title -
phytotherapy research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.019
H-Index - 129
eISSN - 1099-1573
pISSN - 0951-418X
DOI - 10.1002/ptr.1579
Subject(s) - pharmacognosy , traditional medicine , pharmacology , biological activity , platelet , phospholipase a2 , chemistry , medicine , biology , biochemistry , in vitro , enzyme
In the inammation process, phospholipase A 2 (PLA 2 ) 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 PLA 2 and subsequent prostaglandins synthesis is considered to be a pivotal event in inammation. Therefore, drugs that inhibit PLA 2 , thus blocking the COX and LOX pathways in the AA cascade, may be effective in the treatment of inammatory processes. New strategies for the treatment of inammatory processes could be detected by a search for active principles of vegetal origin that control the lipid mediator production by inhibition of PLA 2 . The present data are part of a wide explorative investigation on the effects of Trichilia catigua (catuaba), which found that PLA 2 activity was totally inhibited by catuaba at a concentration of 120 µg/mL, suggesting that this natural substance may have antiinammatory properties. Copyright © 2004 John Wiley & Sons, Ltd.