PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 30477664-9 2018 CONCLUSIONS: Based on these findings, we emphasize that RCs and PGs have a similar expression of inflammatory mediators (COX-2 and TNF-alpha) although the secretion of TNF-alpha by macrophages and of COX-2 by several cells was higher in PGs, indicating a greater inflammatory response in these lesions. Phosphatidylglycerols 64-67 prostaglandin-endoperoxide synthase 2 Homo sapiens 121-126 30477664-9 2018 CONCLUSIONS: Based on these findings, we emphasize that RCs and PGs have a similar expression of inflammatory mediators (COX-2 and TNF-alpha) although the secretion of TNF-alpha by macrophages and of COX-2 by several cells was higher in PGs, indicating a greater inflammatory response in these lesions. Phosphatidylglycerols 64-67 prostaglandin-endoperoxide synthase 2 Homo sapiens 200-205 27028995-4 2016 Knocking down COX-2 inhibited the production of prostaglandin E2 (PGE2), the phosphorylation of p38 or JNKs in SUV-irradiated cells, which indicated that COX-2 is not only the key enzyme for PGs synthesis, but also an upstream regulator of p38 or JNKs after SUV irradiation. Phosphatidylglycerols 191-194 prostaglandin-endoperoxide synthase 2 Homo sapiens 14-19 27028995-4 2016 Knocking down COX-2 inhibited the production of prostaglandin E2 (PGE2), the phosphorylation of p38 or JNKs in SUV-irradiated cells, which indicated that COX-2 is not only the key enzyme for PGs synthesis, but also an upstream regulator of p38 or JNKs after SUV irradiation. Phosphatidylglycerols 191-194 prostaglandin-endoperoxide synthase 2 Homo sapiens 154-159 26498686-8 2015 We demonstrated that in this pathway mPGES1 is induced by COX2 overexpression, via autocrine PGs release, likely PGF2alpha, through an EGR1-dependent mechanism. Phosphatidylglycerols 93-96 prostaglandin-endoperoxide synthase 2 Homo sapiens 58-62 23943857-8 2013 Together, our data demonstrate a proapoptotic mechanism of celecoxib involving initial upregulation of COX-2 and PPARgamma and a subsequent nuclear translocation of PPARgamma by COX-2-dependent PGs. Phosphatidylglycerols 194-197 prostaglandin-endoperoxide synthase 2 Homo sapiens 178-183 23479225-3 2013 Under proinflammatory conditions, the expression of cyclooxygenase-2 leads to the release of large amounts of PGs, such as PGE2, that exert their effects through EP receptors and other intracellular targets. Phosphatidylglycerols 110-113 prostaglandin-endoperoxide synthase 2 Homo sapiens 52-68 19015962-10 2009 CONCLUSION: This study demonstrates COX-2 induction and synthesis of L-PGDS-derived, PPARgamma-activating PGs as a possible mechanism of apoptosis by MA. Phosphatidylglycerols 106-109 prostaglandin-endoperoxide synthase 2 Homo sapiens 36-41 18071320-9 2008 Collectively, this study suggests COX-2 induction and synthesis of L-PGDS-derived, PPARgamma-activating PGs as a decisive target by which several chemotherapeutics induce apoptosis. Phosphatidylglycerols 104-107 prostaglandin-endoperoxide synthase 2 Homo sapiens 34-39 17307169-2 2007 Although the spectrum of the downstream products of COX2 action in testis, namely PGs, and their effects are not known, our results show that Prostaglandin D2 (PGD2) likely plays a role. Phosphatidylglycerols 82-85 prostaglandin-endoperoxide synthase 2 Homo sapiens 52-56 17229571-4 2007 Calcitriol inhibits the prostaglandin (PG) pathway by three actions: (i) the inhibition of the expression of cyclooxygenase-2 (COX-2), the enzyme that synthesizes PGs, (ii) the induction of the expression of 15-prostaglandin dehydrogenase (15-PGDH), the enzyme that inactivates PGs and (iii) decreasing the expression of EP and FP PG receptors that are essential for PG signaling. Phosphatidylglycerols 163-166 prostaglandin-endoperoxide synthase 2 Homo sapiens 109-125 17229571-4 2007 Calcitriol inhibits the prostaglandin (PG) pathway by three actions: (i) the inhibition of the expression of cyclooxygenase-2 (COX-2), the enzyme that synthesizes PGs, (ii) the induction of the expression of 15-prostaglandin dehydrogenase (15-PGDH), the enzyme that inactivates PGs and (iii) decreasing the expression of EP and FP PG receptors that are essential for PG signaling. Phosphatidylglycerols 163-166 prostaglandin-endoperoxide synthase 2 Homo sapiens 127-132 17229571-4 2007 Calcitriol inhibits the prostaglandin (PG) pathway by three actions: (i) the inhibition of the expression of cyclooxygenase-2 (COX-2), the enzyme that synthesizes PGs, (ii) the induction of the expression of 15-prostaglandin dehydrogenase (15-PGDH), the enzyme that inactivates PGs and (iii) decreasing the expression of EP and FP PG receptors that are essential for PG signaling. Phosphatidylglycerols 278-281 prostaglandin-endoperoxide synthase 2 Homo sapiens 127-132 15975667-2 2005 Cyclooxygenase-2 (COX) is the key enzyme that catalyzes the two sequential steps in the biosynthesis of PGs from arachidonic acid. Phosphatidylglycerols 104-107 prostaglandin-endoperoxide synthase 2 Homo sapiens 0-16 15975667-2 2005 Cyclooxygenase-2 (COX) is the key enzyme that catalyzes the two sequential steps in the biosynthesis of PGs from arachidonic acid. Phosphatidylglycerols 104-107 prostaglandin-endoperoxide synthase 2 Homo sapiens 18-21 16124396-1 2005 Cyclooxygenase-2 (COX-2) is an enzyme induced by inflammatory and mitogenic stimuli and results in enhanced synthesis of PGs in inflamed and neoplastic tissues. Phosphatidylglycerols 121-124 prostaglandin-endoperoxide synthase 2 Homo sapiens 0-16 16124396-1 2005 Cyclooxygenase-2 (COX-2) is an enzyme induced by inflammatory and mitogenic stimuli and results in enhanced synthesis of PGs in inflamed and neoplastic tissues. Phosphatidylglycerols 121-124 prostaglandin-endoperoxide synthase 2 Homo sapiens 18-23 12939602-2 2003 However, the biologic role and molecular mechanism of COX-2-mediated PGs in the control of liver cancer growth have not been established. Phosphatidylglycerols 69-72 prostaglandin-endoperoxide synthase 2 Homo sapiens 54-59 12021245-8 2002 They also link adiponectin to the COX-2-dependent PGs that are critical in this process. Phosphatidylglycerols 50-53 prostaglandin-endoperoxide synthase 2 Homo sapiens 34-39 10874015-11 2000 Stimulating GK production of PGs by AN extract could be due to induction of cyclooxygenase-2 (COX-2) mRNA expression and protein production. Phosphatidylglycerols 29-32 prostaglandin-endoperoxide synthase 2 Homo sapiens 76-92 10965822-9 2000 These findings suggest that PGs produced by COX-2-expressing macrophages induce VEGF production by macrophages, but not by cancer cells, in an autocrine fashion. Phosphatidylglycerols 28-31 prostaglandin-endoperoxide synthase 2 Homo sapiens 44-49 10027847-2 1999 However, the relative contribution of phospholipase A2 to the release of PGs in cells expressing cyclooxygenase-2 is not clear. Phosphatidylglycerols 73-76 prostaglandin-endoperoxide synthase 2 Homo sapiens 97-113 9575890-1 1998 The inflammatory cytokine interleukin-1 beta (IL-1 beta) induces both cyclooxygenase-2 (Cox-2) and the inducible nitric oxide synthase (iNOS) with concomitant release of PGs and nitric oxide (NO) by glomerular mesangial cells. Phosphatidylglycerols 170-173 prostaglandin-endoperoxide synthase 2 Homo sapiens 70-86 9575890-1 1998 The inflammatory cytokine interleukin-1 beta (IL-1 beta) induces both cyclooxygenase-2 (Cox-2) and the inducible nitric oxide synthase (iNOS) with concomitant release of PGs and nitric oxide (NO) by glomerular mesangial cells. Phosphatidylglycerols 170-173 prostaglandin-endoperoxide synthase 2 Homo sapiens 88-93