prostaglandin-d2 has been researched along with 13-hydroxy-9-11-octadecadienoic-acid* in 6 studies
1 review(s) available for prostaglandin-d2 and 13-hydroxy-9-11-octadecadienoic-acid
Article | Year |
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[Activation mechanism of PPARgamma by its endogenous ligands].
Topics: Adipocytes; Cell Differentiation; Humans; Insulin Resistance; Ligands; Linoleic Acids; Linoleic Acids, Conjugated; Macrophage Activation; PPAR gamma; Prostaglandin D2 | 2007 |
5 other study(ies) available for prostaglandin-d2 and 13-hydroxy-9-11-octadecadienoic-acid
Article | Year |
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Differential Effects of Estrogen Receptor Alpha and Beta on Endogenous Ligands of Peroxisome Proliferator-Activated Receptor Gamma in Papillary Thyroid Cancer.
The inhibition of estrogen receptor alpha (ERα) or the activation of ERβ can inhibit papillary thyroid cancer (PTC), but the precise mechanism is not known. We aimed to explore the role of ERα and ERβ on the production of endogenous peroxisome proliferator-activated receptor gamma (PPARγ) ligands in PTC.. 2 PTC cell lines, 32 pairs of PTC tissues and matched normal thyroid tissues were used in this study. The levels of endogenous PPARγ ligands 15(S)-hydroxyeicosatetraenoic acid (15(S)-HETE), 13-S-hydroxyoctadecadienoic acid (13(S)-HODE), and15-deoxy-Δ12,14-prostaglandin J2 (PGJ2) were measured by ELISA.. The levels of PGJ2 and 15(S)-HETE were significantly reduced in PTC, but 13(S)-HODE was not changed. Activation of ERα or inhibition of ERβ significantly downregulated the production of PGJ2, 15(S)-HETE and 13(S)-HODE, whereas inhibition of ERα or activation of ERβ markedly upregulated the production of these three ligands. Application of endogenous PPARγ ligands inhibited growth, induced apoptosis of cancer cells, and promoted the efficacy of chemotherapy.. The levels of endogenous PPARγ ligands PGJ2 and 15(S)-HETE are significantly decreased in PTC. The inhibition of ERα or activation of ERβ can inhibit PTC by stimulating the production of endogenous PPARγ ligands to induce apoptosis in cancer cells. Topics: Adult; Apoptosis; Cell Movement; Cell Proliferation; Estrogen Receptor beta; Female; Humans; Hydroxyeicosatetraenoic Acids; Ligands; Linoleic Acids; Male; Middle Aged; PPAR gamma; Prognosis; Prostaglandin D2; Thyroid Cancer, Papillary; Thyroid Neoplasms; Tumor Cells, Cultured | 2021 |
Effects of mPGES-1 deletion on eicosanoid and fatty acid profiles in mice.
mPGES-1 is considered an alternative target for anti-inflammatory treatment with improved selectivity and safety compared to NSAIDs. mPGES-1 depletion not only suppresses inflammation via absence of inducible PGE2 but might also cause an activation of anti-inflammatory pathways. We studied effects of mPGES-1 deletion on the eicosanoid and fatty acid (FA) profiles in mice. In LPS-induced peritoneal macrophages from mPGES-1 knock-out (mPGES-1-/-, KO) mice PGE2 production was markedly attenuated, whereas levels of PGD2 metabolites (15-deoxy-Δ(12,14) PGJ2 and 15-deoxy-Δ(12,14) PGD2) were increased compared to wild type mice. The levels of oxidized fatty acid 13-HODE were also significantly up-regulated in KO macrophages. Significant differences in the total lipid FA composition (decrease in monounsaturated FA and increase in eicosadienoic acid) were detected in spleen of KO and WT mice. These effects of mPGES-1 deletion on eicosanoid and fatty acid metabolism have important implications for future mPGES-1 inhibitors and deserve further investigation. Topics: Animals; Brain; Cells, Cultured; Eicosanoids; Fatty Acids; Fatty Acids, Monounsaturated; Intramolecular Oxidoreductases; Linoleic Acids; Lipopolysaccharides; Macrophages, Peritoneal; Mice; Mice, Inbred DBA; Mice, Knockout; Prostaglandin D2; Prostaglandin-E Synthases; Spleen; Up-Regulation | 2013 |
15-Deoxy-delta(12,14)-prostaglandin J(2) inhibits IL-10 and IL-12 production by macrophages.
15-Deoxy-Delta(12,14)-prostaglandin J(2) (dPGJ(2)) is a metabolite of prostaglandin D(2), that binds to peroxisome proliferator-activated receptor gamma (PPARgamma). PPARgamma and prostaglandin D(2) synthase, which is required for dPGJ(2) synthesis, are predominantly expressed in macrophages. In contrast, IL-10 and IL-12 produced by macrophages stimulate Th1 and Th2 immune response, respectively. This study investigated the effect of dPGJ(2) on IL-10 and IL-12 production by macrophages in response to lipopolysaccharide (LPS). Our data clearly demonstrated that dPGJ(2) inhibits LPS-induced IL-10 and IL-12 production by macrophages. A different agonist of PPARgamma, 13-hydroxyoctadecadienoic acid, similarly inhibited the production of IL-10 and IL-12 in response to LPS. Further, dPGJ(2) did not appear to act through the PGD(2) receptor. These results suggest that dPGJ(2) may inhibit LPS-induced IL-10 and IL-12 production by macrophages through PPARgamma. Topics: Animals; In Vitro Techniques; Interleukin-10; Interleukin-12; Linoleic Acids; Lipopolysaccharides; Macrophages, Peritoneal; Male; Prostaglandin D2; Rats; Rats, Wistar; Receptors, Cytoplasmic and Nuclear; Receptors, Immunologic; Receptors, Prostaglandin; Transcription Factors | 2001 |
Regulation of ferritin light chain gene expression by oxidized low-density lipoproteins in human monocytic THP-1 cells.
Genes induced or suppressed by oxidized low-density lipoproteins (oxLDL) in human monocytic THP-1 cells were searched using differential display reverse transcriptase polymerase chain reactions (DDRT-PCR). Among the many differentially expressed cDNA fragments, one was dramatically stimulated by the oxLDL in a steady state level, which was later found to contain sequences corresponding to ferritin light chain (L-ferritin) in a sequence homology search. The stimulatory effect of the oxLDL on the level of L-ferritin mRNA in the THP-1 cells was both time- and dose-dependent. When the cells were allowed to differentiate in the presence of phorbol 12-myristate 13-acetate (PMA), the differentiated cells were generally less responsive to the oxLDL than the undifferentiated ones. An increase of L-ferritin mRNA was observed when the cells were treated with the lipid components in the oxLDL such as 9-HODE, 13-HODE, and 25-hydroxycholesterol. In addition, a stimulation of the L-ferritin gene expression was also observed when the cells were treated with an endogenous peroxisome proliferator-activated receptor gamma (PPARgamma) ligand, 15d-PGJ2, in a time- and dose-dependent manner. These results suggest that oxLDL or its constituents are related to the stimulation of L-ferritin expression via PPARgamma. Topics: Apoferritins; Base Sequence; Cell Differentiation; Cell Line; DNA Primers; Ferritins; Gene Expression Regulation; Humans; Hydroxycholesterols; Ligands; Linoleic Acids; Linoleic Acids, Conjugated; Lipoproteins, LDL; Monocytes; Prostaglandin D2; Receptors, Cytoplasmic and Nuclear; Reverse Transcriptase Polymerase Chain Reaction; RNA, Messenger; Signal Transduction; Tetradecanoylphorbol Acetate; Transcription Factors | 1999 |
Oxidized LDL regulates macrophage gene expression through ligand activation of PPARgamma.
Macrophage uptake of oxidized low-density lipoprotein (oxLDL) is thought to play a central role in foam cell formation and the pathogenesis of atherosclerosis. We demonstrate here that oxLDL activates PPARgamma-dependent transcription through a novel signaling pathway involving scavenger receptor-mediated particle uptake. Moreover, we identify two of the major oxidized lipid components of oxLDL, 9-HODE and 13-HODE, as endogenous activators and ligands of PPARgamma. Our data suggest that the biologic effects of oxLDL are coordinated by two sets of receptors, one on the cell surface, which binds and internalizes the particle, and one in the nucleus, which is transcriptionally activated by its component lipids. These results suggest that PPARgamma may be a key regulator of foam cell gene expression. Topics: Animals; CD36 Antigens; Cell Differentiation; Cells, Cultured; Dimerization; Fatty Acids, Unsaturated; Humans; Ligands; Linoleic Acids; Linoleic Acids, Conjugated; Lipopolysaccharide Receptors; Lipoproteins, LDL; Macrophages; Membrane Proteins; Monocytes; Oxidation-Reduction; Prostaglandin D2; Receptors, Cytoplasmic and Nuclear; Receptors, Immunologic; Receptors, Lipoprotein; Receptors, Retinoic Acid; Receptors, Scavenger; Recombinant Fusion Proteins; Retinoid X Receptors; Scavenger Receptors, Class B; Signal Transduction; Transcription Factors; Transcriptional Activation | 1998 |