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The COX-2 enzyme was discovered in 1988 by Daniel Simmons, a Brigham Young University researcher. [30] The mouse COX-2 gene was cloned by UCLA scientist Harvey Herschman, a finding published in 1991. [31] The basic research leading to the discovery of COX-2 inhibitors has been the subject of at least two lawsuits.
Cyclooxygenase-2 (COX-2), also known as prostaglandin-endoperoxide synthase 2 (HUGO PTGS2), is an enzyme that in humans is encoded by the PTGS2 gene. [5] In humans it is one of three cyclooxygenases. It is involved in the conversion of arachidonic acid to prostaglandin H 2, an important precursor of prostacyclin, which is expressed in inflammation.
COX is a common target for anti-inflammatory drugs. The most significant difference between the isoenzymes, which allows for selective inhibition, is the substitution of isoleucine at position 523 in COX-1 with valine in COX-2. The smaller Val 523 residue in COX-2 allows access to a hydrophobic side-pocket in the enzyme (which Ile 523 ...
Once the COX-2 enzyme was identified, Dup-697 became the building-block for synthesis of COX-2 inhibitors. Celecoxib and rofecoxib, the first COX-2 inhibitors to reach market, were based on DuP-697. [ 5 ] [ 6 ] It took less than eight years to develop and market the first COX-2 inhibitor, with Celebrex ( celecoxib ) launched in December 1998 ...
17709 Ensembl ENSG00000198712 ENSMUSG00000064354 UniProt P00403 P00405 RefSeq (mRNA) n/a n/a RefSeq (protein) n/a NP_904331 Location (UCSC) Chr M: 0.01 – 0.01 Mb Chr M: 0.01 – 0.01 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Location of the MT-CO2 gene in the human mitochondrial genome. MT-CO2 is one of the three cytochrome c oxidase subunit mitochondrial genes (orange boxes ...
The underlying mechanism for the deleterious effect proposes that endothelial cells lining the microvasculature in the body express COX-2, whose selective inhibition results in levels of prostaglandin I2 (PGI2, prostacyclin) down-regulated relative to thromboxane (since COX-1 in platelets is unaffected).
The location of HRE sites on the genome varies among cancer cell types, however hypoxia based signaling has been found to activate VM related genes including VE-cadherin, COX-2, Twist, Nodal, EphA2, VEGF-A, and VEGR-1. [7]
The conversion from arachidonic acid to prostaglandin H 2 is a two-step process. First, COX-1 catalyzes the addition of two free oxygens to form the 1,2-dioxane bridge and a peroxide functional group to form prostaglandin G 2 (PGG 2). [3] Second, COX-2 reduces the peroxide functional group to a secondary alcohol, forming prostaglandin H 2.