Gene interactions and pathways from curated databases and text-mining
Mol Pharmacol 2002, PMID: 11854442

Regulation of cyclooxygenase-2 expression by phospholipase D in human amnion-derived WISH cells.

Park, Dae-Won; Bae, Yoe-Sik; Nam, Ju-Ock; Kim, Jong-Ho; Lee, Young-Gi; Park, Yoon-Ki; Ryu, Sung Ho; Baek, Suk-Hwan

Prostaglandins (PGs) are known to play a key role in the initiation of labor, but the mechanisms regulating their synthesis in amnion are largely unknown. In this study, the regulatory mechanisms for PGE(2) production during phospholipase D (PLD) and p38-dependent activation of WISH cells were investigated. We found that the stimulation of WISH cells with interleukin (IL)-1 beta elicited dose-dependent synthesis of cyclooxygenase-2 (COX-2) mRNA, protein, and their products, PGE(2). Moreover, the treatment of [(3)H]myristate-labeled cells in the presence of 1-butanol caused the dose-dependent formation of [(3)H]phosphatidylbutanol (PBt), a product specific to PLD activity. Pretreating the cells with 1-butanol and Ro 31-8220 inhibited the IL-1 beta-induced COX-2 expression, but 3-butanol did not affect this response. In addition, evidence that PLD was involved in the stimulation of COX-2 expression was provided by the observations that COX-2 expression was stimulated by the dioctanoyl phosphatidic acid (PA) and that the prevention of PA dephosphorylation by 1-propranolol potentiated COX-2 expression by IL-1 beta. Moreover, IL-1 beta stimulation of the cells caused the phosphorylation of p38 and extracellular signal-regulated kinase (ERK), and IL-1 beta-induced COX-2 expression was inhibited by the pretreatment of WISH cells with a p38 inhibitor, in contrast ERK upstream inhibitor had no effect. Furthermore, Ro 31-8220 inhibited IL-1 beta-induced p38 phosphorylation but not ERK phosphorylation. The results of this study indicate that in human amnion cells, IL-1 beta might activate PLD through an upstream protein kinase C to elicit p38 and finally induce COX-2 expression.

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Text Mining Data

cyclooxygenase-2 — phospholipase D: " Regulation of cyclooxygenase-2 expression by phospholipase D in human amnion derived WISH cells "

phospholipase D ( PLD ) → p38: " In this study, the regulatory mechanisms for PGE ( 2 ) production during phospholipase D ( PLD ) and p38 dependent activation of WISH cells were investigated "

COX-2 → IL-1 beta: " Pretreating the cells with 1-butanol and Ro 31-8220 inhibited the IL-1 beta induced COX-2 expression, but 3-butanol did not affect this response "

COX-2 → PLD: " In addition, evidence that PLD was involved in the stimulation of COX-2 expression was provided by the observations that COX-2 expression was stimulated by the dioctanoyl phosphatidic acid ( PA ) and that the prevention of PA dephosphorylation by 1-propranolol potentiated COX-2 expression by IL-1 beta "

p38 ⊣ COX-2: " Moreover, IL-1 beta stimulation of the cells caused the phosphorylation of p38 and extracellular signal regulated kinase ( ERK ), and IL-1 beta induced COX-2 expression was inhibited by the pretreatment of WISH cells with a p38 inhibitor, in contrast ERK upstream inhibitor had no effect "

COX-2 ⊣ IL-1: " Moreover, IL-1 beta stimulation of the cells caused the phosphorylation of p38 and extracellular signal regulated kinase ( ERK ), and IL-1 beta induced COX-2 expression was inhibited by the pretreatment of WISH cells with a p38 inhibitor, in contrast ERK upstream inhibitor had no effect "

COX-2 ⊣ IL-1 beta: " Moreover, IL-1 beta stimulation of the cells caused the phosphorylation of p38 and extracellular signal regulated kinase ( ERK ), and IL-1 beta induced COX-2 expression was inhibited by the pretreatment of WISH cells with a p38 inhibitor, in contrast ERK upstream inhibitor had no effect "

p38 → IL-1: " Moreover, IL-1 beta stimulation of the cells caused the phosphorylation of p38 and extracellular signal regulated kinase ( ERK ), and IL-1 beta induced COX-2 expression was inhibited by the pretreatment of WISH cells with a p38 inhibitor, in contrast ERK upstream inhibitor had no effect "

p38 → IL-1 beta: " Moreover, IL-1 beta stimulation of the cells caused the phosphorylation of p38 and extracellular signal regulated kinase ( ERK ), and IL-1 beta induced COX-2 expression was inhibited by the pretreatment of WISH cells with a p38 inhibitor, in contrast ERK upstream inhibitor had no effect "

p38 → IL-1 beta: " Furthermore, Ro 31-8220 inhibited IL-1 beta induced p38 phosphorylation but not ERK phosphorylation "

ERK → IL-1 beta: " Furthermore, Ro 31-8220 inhibited IL-1 beta induced p38 phosphorylation but not ERK phosphorylation "

PLD → IL-1: " The results of this study indicate that in human amnion cells, IL-1 beta might activate PLD through an upstream protein kinase C to elicit p38 and finally induce COX-2 expression "

PLD → IL-1 beta: " The results of this study indicate that in human amnion cells, IL-1 beta might activate PLD through an upstream protein kinase C to elicit p38 and finally induce COX-2 expression "

PLD → COX-2: " The results of this study indicate that in human amnion cells, IL-1 beta might activate PLD through an upstream protein kinase C to elicit p38 and finally induce COX-2 expression "

IL-1 → COX-2: " The results of this study indicate that in human amnion cells, IL-1 beta might activate PLD through an upstream protein kinase C to elicit p38 and finally induce COX-2 expression "

IL-1 beta → COX-2: " The results of this study indicate that in human amnion cells, IL-1 beta might activate PLD through an upstream protein kinase C to elicit p38 and finally induce COX-2 expression "

Manually curated Databases

No curated data.