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Arachidonic acid metabolic enzymes represent a group of catalytic proteins, including phospholipase A2 (PLA2), cyclooxygenases (COX-1 and COX-2), and lipoxygenases (e.g., 5-LOX), that govern the production of bioactive lipid mediators known as eicosanoids [4]. These enzymes are central to the inflammatory response, as they convert membrane-derived arachidonic acid into prostaglandins, thromboxanes, and leukotrienes, which mediate pain, fever, and vascular changes [1, 4]. PLA2 initiates the process by releasing free arachidonic acid from phospholipids, which is then channeled into the COX pathway for prostaglandin synthesis or the LOX pathway for leukotriene production [2, 3]. Pharmacological suppression of these enzymes is a primary therapeutic strategy for managing conditions such as rheumatoid arthritis, osteoarthritis, and asthma [1, 5]. Common drugs like nonsteroidal anti-inflammatory drugs (NSAIDs) inhibit COX enzymes, while agents like zileuton target 5-LOX to reduce airway inflammation [1, 3]. However, because these enzymes also play vital roles in maintaining the gastric mucosa and renal function, their systemic inhibition can lead to significant safety concerns, including gastrointestinal bleeding and cardiovascular risks [3, 4].
Inhibition of cyclooxygenase (COX-1/COX-2), lipoxygenase (5-LOX), or phospholipase A2 (PLA2) activity to reduce the synthesis of pro-inflammatory eicosanoids [1, 2].
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