A prostaglandin J2 metabolite binds peroxisome proliferator-activated receptor γ and promotes adipocyte differentiation

Kliewer, Steven A.; Lenhard, James M.; Willson, Timothy M.; Patel, Indravadan R.; Morris, Dan; Lehmann, Jürgen

doi:10.1016/0092-8674(95)90194-9

Cited by 1,919 publications

(1,295 citation statements)

References 29 publications

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“…24,25,27 Figure 3. Photomicrograph of mineralized nodules after 14 days of exposure to polyunsaturated fatty acids.…”

Section: Oil Red O Staining Versus Alkaline Phosphatase Activity As Mmentioning

confidence: 99%

“…23 These receptors are activated by free fatty acids and their oxidation products as well as by some prostaglandins derived from fatty acids that induce the differentiation of preadipocytes into adipocytic cells. [24][25][26][27] AA, which is a precursor for prostaglandins of the -2-family, has specifically been implicated in adipocyte differentiation. 23 With ageing there is a decrease in osteoprogenitor cells with an accompanying increase in adipocytes in bone marrow.…”

Section: Introductionmentioning

confidence: 99%

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Effects of arachidonic acid and docosahexaenoic acid on differentiation and mineralization of MC3T3‐E1 osteoblast‐like cells

Coetzee

Haag

Kruger

2008

Cell Biochemistry & Function

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Osteoblasts in culture can differentiate into mature mineralizing osteoblasts when stimulated with osteogenic agents. Clinical trials and in vivo animal studies suggest that specific polyunsaturated fatty acids (PUFAs) may benefit bone health. The aim of this study was to investigate whether arachidonic acid (AA) and docosahexaenoic acid (DHA) affect osteogenesis in osteoblasts and the transdifferentiation into adipocytes. Results from this study show that long-term exposure to AA inhibited alkaline phosphatase (ALP) activity in these cells, which might be prostaglandin E 2 (PGE 2 )-mediated. DHA exposure also inhibited ALP activity which was evident after both short-and long-term exposures. The mechanism whereby DHA inhibits ALP activity is not clear and needs to be investigated. Although long-term exposure to PUFAs inhibited ALP activity, the mineralizing properties of these cells were not compromised. Furthermore, PUFA exposure did not induce adipocyte-like features in these cells as evidenced by the lack of cytoplasmic triacylglycerol accummulation. More research is required to elucidate the cellular mechanisms of action of PUFAs on bone.

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“…24,25,27 Figure 3. Photomicrograph of mineralized nodules after 14 days of exposure to polyunsaturated fatty acids.…”

Section: Oil Red O Staining Versus Alkaline Phosphatase Activity As Mmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Effects of arachidonic acid and docosahexaenoic acid on differentiation and mineralization of MC3T3‐E1 osteoblast‐like cells

Coetzee

Haag

Kruger

2008

Cell Biochemistry & Function

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“…These include modified fatty acids, members of the prostanoid family, in particular 15-deoxy-D 12,14 -prostaglandin J 2 (15d-PGJ 2 ) and linoleic acid derivatives [12,13], and insulin-sensitizing thiazolidinedione compounds such as BRL-49653 (rosiglitazone), pioglitazone, and troglitazone [14][15][16].…”

Section: Introductionmentioning

confidence: 99%

IL‐13 induces expression of CD36 in human monocytes through PPARγ activation

et al. 2007

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The class B scavenger receptor CD36 is a component of the pattern recognition receptors on monocytes that recognizes a variety of molecules. CD36 expression in monocytes depends on exposure to soluble mediators. We demonstrate here that CD36 expression is induced in human monocytes following exposure to IL-13, a Th2 cytokine, via the peroxisome proliferator-activated receptor (PPAR)c pathway. Induction of CD36 protein was paralleled by an increase in CD36 mRNA. The PPARc pathway was demonstrated using transfection of a PPARc expression plasmid into the murine macrophage cell line RAW264.7, expressing very low levels of PPARc, and in peritoneal macrophages from PPARc-conditional null mice. We also show that CD36 induction by IL-13 via PPARc is dependent on phospholipase A2 activation and that IL-13 induces the production of endogenous 15-deoxy-D 12,14 -prostaglandin J 2 , an endogenous PPARc ligand, and its nuclear localization in human monocytes. Finally, we demonstrate that CD36 and PPARc are involved in IL-13-mediated phagocytosis of Plasmodium falciparum-parasitized erythrocytes. These results reveal a novel role for PPARc in the alternative activation of monocytes by IL-13, suggesting that endogenous PPARc ligands, produced by phospholipase A2 activation, could contribute to the biochemical and cellular functions of CD36.Leukocyte signaling * These 2 authors contributed equally to this work. IntroductionThe innate immune system protects the host in the early phase of infection. Circulating monocytes and tissue macrophages (Mu) mediate much of this innate immune response [1]. The strategy of recognition in the innate response is mediated by the coordinated action of pathogen-associated molecular patterns and pattern recognition receptors. Scavenger receptors and mannose receptor are important pattern recognition receptors in monocytes/Mu [2,3]. The modulation of the expression of these receptors may be critical in the role of these cells in antigen processing, scavenging, and host defence against pathogens. Several members of the scavenger receptor family, including Mu class A scavenger receptors and CD36, have been identified as receptors for modified lipoproteins on Mu, and their relevance to lipid uptake has been demonstrated in vitro and in vivo [4]. The scavenger receptor CD36, an 88-kDa integral membrane protein, is a class B scavenger receptor expressed on a wide variety of cells, in particular on monocytes and monocytederived Mu [5,6]. CD36 is known as a receptor for the uptake of oxidatively modified low-density lipoprotein (LDL) [7] and is also able to bind anionic phospholipid phosphatidylserine [8]. This scavenger receptor is implicated in the clearance of apoptotic cells [9]. Recently, McGilvray and colleagues [10] described a CD36-dependent nonopsonic phagocytosis of erythrocytes containing P. falciparum, by monocytes and culture-derived Mu, and a decrease in the parasiteinduced TNF secretion by monocytes/Mu. These processes were accentuated by CD36 up-regulation by peroxisome proliferator-acti...

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“…7 Natural polyunsaturated fatty acids can activate PPAR-γ , and 15-deoxy-᭝ 12,14 -prostaglandin J 2 (15d-PGJ 2 ), a metabolite of PGD 2 , is the most specific natural agonist for PPAR-γ . 8,9 Adhesion of white blood cells to vascular endothelial cells is an important event in the early stage of immunological and inflammatory responses; 10,11 and proinflammatory cytokines are known to stimulate the endothelium to express adhesion molecules such as vascular adhesion molecule-1 (VCAM-1), intercellular adhesion molecule-1 (ICAM-1) and E-selectin. 12 CX3CL1/fractalkine is a chemokine with the N-terminal chemokine domain containing a unique CX3C motif.…”

Section: Introductionmentioning

confidence: 99%

15‐Deoxy‐Δ^12,14‐prostaglandin J₂ inhibitsCX3CL1/fractalkine expression in human endothelial cells

Imaizumi¹,

Matsumiya

Tamo³

et al. 2002

Immunol Cell Biol

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Summary Peroxisome proliferator-activated receptor-γ (PPAR-γ ) is a member of nuclear hormone receptor superfamily, and is known to play a role in various biological processes including inflammatory responses and adipocyte differentiation. CX3CL1/fractalkine is a potent agonist for chemotaxis and adhesion of monocytes and lymphocytes. Endothelial cells produce fractalkine when stimulated with cytokines such as interleukin-1 (IL-1), tumour necrosis factor-α and interferon-γ (IFN-γ ). We herein report that 15-deoxy-᭝ 12,14 -prostaglandin J 2 (15d-PGJ 2 ), a PPAR-γ agonist, inhibits the expression of fractalkine induced by IFN-γ or IL-1 β in human endothelial cells. Agonist for PPAR-α (WY14643) or PPAR-γ (ciglitazone) did not inhibit the cytokine-induced fractalkine expression, and the effect of 15d-PGJ 2 may be independent of PPAR. 15-Deoxy-⌬ 12,14 prostaglandin J 2 also inhibited the adhesion of blood mononuclear cells to endothelial monolayers treated with IFN-γ or IL-1 β . The data suggest that 15d-PGJ 2 regulates inflammatory reactions, at least in part, through the inhibition of fractalkine expression and leucocyte traffic through the endothelium.

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A prostaglandin J2 metabolite binds peroxisome proliferator-activated receptor γ and promotes adipocyte differentiation

Cited by 1,919 publications

References 29 publications

Effects of arachidonic acid and docosahexaenoic acid on differentiation and mineralization of MC3T3‐E1 osteoblast‐like cells

Effects of arachidonic acid and docosahexaenoic acid on differentiation and mineralization of MC3T3‐E1 osteoblast‐like cells

IL‐13 induces expression of CD36 in human monocytes through PPARγ activation

15‐Deoxy‐Δ^12,14‐prostaglandin J₂ inhibitsCX3CL1/fractalkine expression in human endothelial cells

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A prostaglandin J2 metabolite binds peroxisome proliferator-activated receptor γ and promotes adipocyte differentiation

Cited by 1,919 publications

References 29 publications

Effects of arachidonic acid and docosahexaenoic acid on differentiation and mineralization of MC3T3‐E1 osteoblast‐like cells

Effects of arachidonic acid and docosahexaenoic acid on differentiation and mineralization of MC3T3‐E1 osteoblast‐like cells

IL‐13 induces expression of CD36 in human monocytes through PPARγ activation

15‐Deoxy‐Δ12,14‐prostaglandin J2 inhibitsCX3CL1/fractalkine expression in human endothelial cells

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15‐Deoxy‐Δ^12,14‐prostaglandin J₂ inhibitsCX3CL1/fractalkine expression in human endothelial cells