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Cyclooxygenase 1 enzyme is a constitutively expressed enzyme encoded by the PTGS1 gene and is best known for catalyzing the initial step in the biosynthesis of prostaglandins and thromboxane from arachidonic acid[1][3][7]. COX-1 is present in most tissues, where it plays a key role in maintaining physiological functions such as gastric mucosal protection, platelet aggregation, and renal blood flow[1][5][7]. It is the molecular target of numerous nonsteroidal anti-inflammatory drugs (NSAIDs) including aspirin, which exert antiinflammatory, analgesic, antipyretic, and antithrombotic effects by inhibiting COX-1 activity[1][4][8]. Inhibition of COX-1 is associated with classic NSAID toxicities like gastrointestinal ulceration and bleeding[7]. While traditionally seen as a "housekeeping" enzyme, recent data imply more complex roles for COX-1 and highlight the consequences of its inhibition in various clinical scenarios[4][5].
Nonselective and selective inhibition (by NSAIDs) blocking enzymatic conversion of arachidonic acid to prostaglandins/thromboxane, thus reducing inflammation, pain, fever, and platelet aggregation[1][3][4][8].
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