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Cyclooxygenases are key enzymes that catalyze the conversion of arachidonic acid to prostaglandins and thromboxanes—lipid mediators central to the processes of inflammation and pain. There are two main isoforms relevant to human disease: cyclooxygenase‑1 (COX‑1), which is constitutively expressed in most tissues and involved in physiological functions such as gastric mucosal protection; and cyclooxygenase‑2 (COX‑2), which is inducible at sites of inflammation. Nonsteroidal anti-inflammatory drugs (NSAIDs) exert their effects primarily by inhibiting these enzymes, thereby reducing prostaglandin production. Selective inhibition of COX‑2 provides anti-inflammatory and analgesic benefits while minimizing gastrointestinal side effects associated with COX‑1 inhibition. However, both non-selective NSAIDs and selective COX‑2 inhibitors carry risks including gastrointestinal toxicity, renal impairment, and increased cardiovascular events[8][1][5]. Note: The original target name "Enzymes involved in inflammation and pain" is not a precise molecular entity but rather a functional group encompassing several enzymes—most notably cyclooxygenases—which are established therapeutic targets for inflammatory diseases[5]. For structured data purposes it is recommended to use specific canonical names such as "Cyclooxygenase‑1 enzyme" or "Cyclooxygenase‑2 enzyme".
Inhibition of prostaglandin synthesis via reversible or irreversible inhibition of cyclooxygenases[8][2]
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