| First Author | Ueno N | Year | 2005 |
| Journal | Biochem Biophys Res Commun | Volume | 338 |
| Issue | 1 | Pages | 70-6 |
| PubMed ID | 16140261 | Mgi Jnum | J:102582 |
| Mgi Id | MGI:3607804 | Doi | 10.1016/j.bbrc.2005.08.152 |
| Citation | Ueno N, et al. (2005) Coupling between cyclooxygenases and terminal prostanoid synthases. Biochem Biophys Res Commun 338(1):70-6 |
| abstractText | Biosynthesis of prostanoids is regulated by three sequential enzymatic steps, namely phospholipase A2, cyclooxygenase (COX), and terminal prostanoid synthase. Recent evidence suggests that lineage-specific terminal prostanoid synthases, including prostaglandin (PG) E2, PGD2, PGF2alpha, PGI2, and thromboxane synthases, show distinct functional coupling with upstream COX isozymes, COX-1 and COX-2. This can account, at least in part, for segregated utilization of the two COX isozymes in distinct phases of PG-biosynthetic responses. In terms of their localization and COX preference, terminal prostanoid synthases are classified into three categories: (i) the perinuclear enzymes that prefer COX-2, (ii) the cytosolic enzyme that prefers COX-1, and (iii) the translocating enzyme that utilizes both COXs depending on the stimulus. Additionally, altered supply of arachidonic acid by phospholipase A2s significantly affects the efficiency of COX-terminal prostanoid synthase coupling. In this review, we summarize our recent understanding of the coupling profiles between the two COXs and various terminal prostanoid synthases. |
