Pub. Date : 1997 Feb 18
PMID : 9048568
11 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
1 | Treatment of PGHS-2 with aspirin (acetyl salicylic acid, ASA) was previously shown to result in acetylation of a specific serine residue, cyclooxygenase inhibition, and increased lipoxygenase activity. | Aspirin | prostaglandin-endoperoxide synthase 2 | Homo sapiens |
2 | Treatment of PGHS-2 with aspirin (acetyl salicylic acid, ASA) was previously shown to result in acetylation of a specific serine residue, cyclooxygenase inhibition, and increased lipoxygenase activity. | Aspirin | prostaglandin-endoperoxide synthase 2 | Homo sapiens |
3 | Treatment of PGHS-2 with aspirin (acetyl salicylic acid, ASA) was previously shown to result in acetylation of a specific serine residue, cyclooxygenase inhibition, and increased lipoxygenase activity. | Aspirin | prostaglandin-endoperoxide synthase 2 | Homo sapiens |
4 | We now have found the ASA-treated PGHS-2 radical to be indistinguishable from that in control PGHS-2. | Aspirin | prostaglandin-endoperoxide synthase 2 | Homo sapiens |
5 | Addition of nimesulide to ASA-treated PGHS-2 inhibited the lipoxygenase and resulted in a narrow radical EPR like that seen in PGHS-2 treated with TNM or nimesulide alone. | Aspirin | prostaglandin-endoperoxide synthase 2 | Homo sapiens |
6 | Addition of nimesulide to ASA-treated PGHS-2 inhibited the lipoxygenase and resulted in a narrow radical EPR like that seen in PGHS-2 treated with TNM or nimesulide alone. | Aspirin | prostaglandin-endoperoxide synthase 2 | Homo sapiens |
7 | Both native and ASA-treated PGHS-2 produced only the R stereoisomer of 11- and 15-HETE, demonstrating that the lipoxygenase stereochemistry was not changed by ASA. | Aspirin | prostaglandin-endoperoxide synthase 2 | Homo sapiens |
8 | Native and ASA-treated PGHS-2 had lipoxygenase K(m) values considerably higher than that of the control PGHS-2 cyclooxygenase. | Aspirin | prostaglandin-endoperoxide synthase 2 | Homo sapiens |
9 | Native and ASA-treated PGHS-2 had lipoxygenase K(m) values considerably higher than that of the control PGHS-2 cyclooxygenase. | Aspirin | prostaglandin-endoperoxide synthase 2 | Homo sapiens |
10 | Taken together, these results suggest that the same PGHS-2 tyrosyl radical serves as the oxidant for both cyclooxygenase and lipoxygenase catalysis and that acetylation of PGHS-2 by ASA favors arachidonate binding in an altered conformation which results in abstraction of the pro-R hydrogen from C13 and formation of 11(R)- and 15(R)-HETE. | Aspirin | prostaglandin-endoperoxide synthase 2 | Homo sapiens |
11 | Taken together, these results suggest that the same PGHS-2 tyrosyl radical serves as the oxidant for both cyclooxygenase and lipoxygenase catalysis and that acetylation of PGHS-2 by ASA favors arachidonate binding in an altered conformation which results in abstraction of the pro-R hydrogen from C13 and formation of 11(R)- and 15(R)-HETE. | Aspirin | prostaglandin-endoperoxide synthase 2 | Homo sapiens |