Acta Chimica and Pharmaceutica Indica
ISSN: 2277-288X

Cyclooxygenase

 Cyclooxygenase (COX), authoritatively known as prostaglandin-endoperoxide synthase (PTGS), is a protein (explicitly, a group of isozymes, EC 1.14.99.1) that is answerable for arrangement of prostanoids, including thromboxane and prostaglandins, for example, prostacyclin, from arachidonic corrosive. An individual from the creature type heme peroxidase family, it is otherwise called prostaglandin G/H synthase. The particular response catalyzed is the change from arachidonic corrosive to Prostaglandin H2, by means of a short-living Prostaglandin G2 intermediate. Cyclooxygenase (COX) is a rate-constraining chemical engaged with the transformation of arachidonic corrosive to prostaglandin H2, which is the forerunner of a few atoms, including prostaglandins, prostacyclin, and thromboxanes. Selectivity for COX-2 is the primary element of celecoxib, etoricoxib, and different individuals from this medication class. Since COX-2 is typically explicit to aroused tissue, there is considerably less gastric aggravation related with COX-2 inhibitors, with a diminished danger of peptic ulceration. The selectivity of COX-2 doesn't appear to discredit opposite reactions of NSAIDs, most eminently an expanded danger of kidney disappointment, and there is proof that shows an expansion in the danger of cardiovascular failure, apoplexy, and stroke through an expansion of thromboxane lopsided by prostacyclin (which is diminished by COX-2 inhibition).[citation needed] Rofecoxib (brand name Vioxx) was pulled back in 2004 as a result of such concerns. Some other COX-2 specific NSAIDs.

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