Compounds > 15-hydroxy-11-alpha-9-alpha-(epoxymethano)prosta-5-13-dienoic-acid

15-hydroxy-11-alpha-9-alpha-(epoxymethano)prosta-5-13-dienoic-acid and 15-hydroxy-5-8-11-13-eicosatetraenoic-acid

15-hydroxy-11-alpha-9-alpha-(epoxymethano)prosta-5-13-dienoic-acid has been researched along with 15-hydroxy-5-8-11-13-eicosatetraenoic-acid* in 2 studies

Other Studies

2 other study(ies) available for 15-hydroxy-11-alpha-9-alpha-(epoxymethano)prosta-5-13-dienoic-acid and 15-hydroxy-5-8-11-13-eicosatetraenoic-acid

Article	Year
Residual cyclooxygenase activity of aspirin-acetylated COX-2 forms 15 R-prostaglandins that inhibit platelet aggregation. FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2019, Volume: 33, Issue:1 Aspirin (acetylsalicylic acid) inhibits prostaglandin (PG) synthesis by transfer of its acetyl group to a serine residue in the cyclooxygenase (COX) active site. Acetylation of Ser530 inhibits catalysis by preventing access of arachidonic acid substrate in the COX-1 isoenzyme. Acetylated COX-2, in contrast, gains a new catalytic activity and forms 15 R hydroxy-eicosatetraenoic acid (15 R-HETE) as alternate product. Here we show that acetylated COX-2 also retains COX activity, forming predominantly 15 R-configuration PGs (70 or 62% 15 R, respectively, determined using radiolabeled substrate or LC-MS analysis). Although the K Topics: 15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5,13-dienoic Acid; Acetylation; Aspirin; Cells, Cultured; Chromatography, Liquid; Cyclooxygenase 2; Dinoprostone; Humans; Hydroxyeicosatetraenoic Acids; Kinetics; Leukocytes; Mass Spectrometry; Platelet Aggregation	2019
IL-1 beta regulates the expression of the Gi2 alpha gene via lipid mediators in guinea pig tracheal muscle. Biochemical and biophysical research communications, 1994, Sep-30, Volume: 203, Issue:3 When isolated guinea pig muscle preparations were incubated with human recombinant IL-1 beta, mRNA level of Gi2 alpha but not of Gs alpha increased in a time and dose dependent manner. The increase was partially blocked by inhibitors of lipoxygenase (NDGA) and cyclooxygenase (indomethacin) and PAF antagonist (SC47014A), while U46619 (thromboxane A2 mimetic), LTD4, 15-HETE and PAF partially mimicked it. The IL-1 beta induced Gi2 alpha expression was almost completely inhibited by anti-phospholipase A2 antiserum, whereas preimmune serum had no apparent effects. From these observations, we suggest that IL-1 beta first induces the synthesis and release of Type II inflammatory phospholipase A2, which in turn stimulates the expression of Gi2 alpha gene via production of various lipid mediators. Topics: 15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5,13-dienoic Acid; Animals; Gene Expression Regulation; GTP-Binding Proteins; Guinea Pigs; Humans; Hydroxyeicosatetraenoic Acids; Indomethacin; Interleukin-1; Leukotriene D4; Lipids; Lipoxygenase Inhibitors; Masoprocol; Muscle, Smooth; Platelet Activating Factor; Prostaglandin Endoperoxides, Synthetic; Recombinant Proteins; Thromboxane A2; Trachea; Vasoconstrictor Agents	1994

Article

Year

Residual cyclooxygenase activity of aspirin-acetylated COX-2 forms 15 R-prostaglandins that inhibit platelet aggregation.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2019, Volume: 33, Issue:1

Aspirin (acetylsalicylic acid) inhibits prostaglandin (PG) synthesis by transfer of its acetyl group to a serine residue in the cyclooxygenase (COX) active site. Acetylation of Ser530 inhibits catalysis by preventing access of arachidonic acid substrate in the COX-1 isoenzyme. Acetylated COX-2, in contrast, gains a new catalytic activity and forms 15 R hydroxy-eicosatetraenoic acid (15 R-HETE) as alternate product. Here we show that acetylated COX-2 also retains COX activity, forming predominantly 15 R-configuration PGs (70 or 62% 15 R, respectively, determined using radiolabeled substrate or LC-MS analysis). Although the K

Topics: 15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5,13-dienoic Acid; Acetylation; Aspirin; Cells, Cultured; Chromatography, Liquid; Cyclooxygenase 2; Dinoprostone; Humans; Hydroxyeicosatetraenoic Acids; Kinetics; Leukocytes; Mass Spectrometry; Platelet Aggregation

2019

IL-1 beta regulates the expression of the Gi2 alpha gene via lipid mediators in guinea pig tracheal muscle.

Biochemical and biophysical research communications, 1994, Sep-30, Volume: 203, Issue:3

When isolated guinea pig muscle preparations were incubated with human recombinant IL-1 beta, mRNA level of Gi2 alpha but not of Gs alpha increased in a time and dose dependent manner. The increase was partially blocked by inhibitors of lipoxygenase (NDGA) and cyclooxygenase (indomethacin) and PAF antagonist (SC47014A), while U46619 (thromboxane A2 mimetic), LTD4, 15-HETE and PAF partially mimicked it. The IL-1 beta induced Gi2 alpha expression was almost completely inhibited by anti-phospholipase A2 antiserum, whereas preimmune serum had no apparent effects. From these observations, we suggest that IL-1 beta first induces the synthesis and release of Type II inflammatory phospholipase A2, which in turn stimulates the expression of Gi2 alpha gene via production of various lipid mediators.

Topics: 15-Hydroxy-11 alpha,9 alpha-(epoxymethano)prosta-5,13-dienoic Acid; Animals; Gene Expression Regulation; GTP-Binding Proteins; Guinea Pigs; Humans; Hydroxyeicosatetraenoic Acids; Indomethacin; Interleukin-1; Leukotriene D4; Lipids; Lipoxygenase Inhibitors; Masoprocol; Muscle, Smooth; Platelet Activating Factor; Prostaglandin Endoperoxides, Synthetic; Recombinant Proteins; Thromboxane A2; Trachea; Vasoconstrictor Agents

1994