ISSN: 2041-6792

Clinical Investigation

Cyclooxygenase:

  Cyclooxygenase (COX) enzymes catalyze arachidonic acid's double dioxygenation into prostaglandin endoperoxides, the direct precursors of prostaglandins, and thromboxane. Such lipid mediators work via multiple receptors coupling with G-protein to cause a wide variety of physiological and pathophysiological responses. Non-steroidal anti-inflammatory drugs (NSAIDs) suppress their biosynthesis, and prevent the attachment of arachidonic acid to the COX enzymes. NSAIDs – e.g., aspirin, ibuprofen, naproxen, celecoxib – are among the world's most commonly used medications which relieve plenty of human misery. The isoenzymes Cyclooxygenase, COX-1 and COX-2, catalyze the formation of prostaglandins, thromboxane and levuloglandins. The prostaglandins are autocoid mediators that cause virtually any established physiological and pathological process via their reversible association with membrane receptors coupled with G-protein. Levuloglandins are a newer class of products which seem to be working by permanent, covalent binding to various proteins. COX enzymes are clinically essential, as aspirin and various other non-steroidal anti-inflammatory medications block them. This COX inhibition provides relief of inflammatory, pyretic, thrombotic, neurodegenerative, and oncological diseases. Around a hundred years have passed after Hoffman developed and synthesized acetylsalicylic (aspirin) as an agent intended to minimize salicylates' gastrointestinal discomfort while preserving their efficacy. Systematic improvements in our knowledge of the structure, control and function of COX isoenzymes over the past forty years have allowed COX-2 selective inhibitors to be engineered and synthesized as agents intended to reduce gastrointestinal inflammation of aspirin and non-selective NSAIDs.  

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