Pub. Date : 1997 Jan
PMID : 9016346
11 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
1 | Altered sensitivity of aspirin-acetylated prostaglandin G/H synthase-2 to inhibition by nonsteroidal anti-inflammatory drugs. | Aspirin | prostaglandin-endoperoxide synthase 2 | Homo sapiens |
2 | Aspirin (ASA) acetylates Ser516 of prostaglandin G/H synthase-2 (PGHS-2) resulting in a modified enzyme that converts arachidonic acid to 15(R)-hydroxy-eicosatetraeroic acid [15(R)-HETE]. | Aspirin | prostaglandin-endoperoxide synthase 2 | Homo sapiens |
3 | Aspirin (ASA) acetylates Ser516 of prostaglandin G/H synthase-2 (PGHS-2) resulting in a modified enzyme that converts arachidonic acid to 15(R)-hydroxy-eicosatetraeroic acid [15(R)-HETE]. | Aspirin | prostaglandin-endoperoxide synthase 2 | Homo sapiens |
4 | Aspirin (ASA) acetylates Ser516 of prostaglandin G/H synthase-2 (PGHS-2) resulting in a modified enzyme that converts arachidonic acid to 15(R)-hydroxy-eicosatetraeroic acid [15(R)-HETE]. | Aspirin | prostaglandin-endoperoxide synthase 2 | Homo sapiens |
5 | Aspirin (ASA) acetylates Ser516 of prostaglandin G/H synthase-2 (PGHS-2) resulting in a modified enzyme that converts arachidonic acid to 15(R)-hydroxy-eicosatetraeroic acid [15(R)-HETE]. | Aspirin | prostaglandin-endoperoxide synthase 2 | Homo sapiens |
6 | ASA has pharmacological benefits that may not all be limited to inhibition of prostaglandin synthesis, and this study was initiated to further investigate the properties of ASA-acetylated PGHS-2 and of the mutation of Ser516 to methionine, which mimics ASA acetylation. | Aspirin | prostaglandin-endoperoxide synthase 2 | Homo sapiens |
7 | ASA has pharmacological benefits that may not all be limited to inhibition of prostaglandin synthesis, and this study was initiated to further investigate the properties of ASA-acetylated PGHS-2 and of the mutation of Ser516 to methionine, which mimics ASA acetylation. | Aspirin | prostaglandin-endoperoxide synthase 2 | Homo sapiens |
8 | Both the S516M mutant and ASA-acetylated form of PGHS-2 (ASA-PGHS-2) synthesize 15(R)-HETE and have apparent K(m) values for arachidonic acid within 10-fold of the apparent K(m) value for untreated PGHS-2. | Aspirin | prostaglandin-endoperoxide synthase 2 | Homo sapiens |
9 | Both the S516M mutant and ASA-acetylated form of PGHS-2 (ASA-PGHS-2) synthesize 15(R)-HETE and have apparent K(m) values for arachidonic acid within 10-fold of the apparent K(m) value for untreated PGHS-2. | Aspirin | prostaglandin-endoperoxide synthase 2 | Homo sapiens |
10 | Both the S516M mutant and ASA-acetylated form of PGHS-2 (ASA-PGHS-2) synthesize 15(R)-HETE and have apparent K(m) values for arachidonic acid within 10-fold of the apparent K(m) value for untreated PGHS-2. | Aspirin | prostaglandin-endoperoxide synthase 2 | Homo sapiens |
11 | These results demonstrate that the sensitivity to inhibition by NSAIDs of the 15-HETE production by ASA-treated PGHS-2 is different than that of prostaglandin production by PGHS-2 and that Ser516 plays an important role in the interaction with fenamate inhibitors. | Aspirin | prostaglandin-endoperoxide synthase 2 | Homo sapiens |