Rat PPARδ Contains a CGG Triplet Repeat and Is Prominently Expressed in the Thalamic Nuclei

Xing, Guoqiang; Zhang, Lixin; Zhang, Lei; Heynen, Terri; Yoshikawa, Takeo; Smith, Mark A.; Weiss, Susan R.B.; Detera-Wadleigh, S D

doi:10.1006/bbrc.1995.2871

Cited by 80 publications

(50 citation statements)

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“…Since expression of PPAR␤ mRNA is reported to be high in the developing neural tubes of embryos and fetuses as well as the adult rodent brain (8,9,11,51), brains from PPAR␤-null mice were examined. The diameters of the brains of PPAR␤-null mice were significantly smaller than those of wild-type mice, which is likely due to the relatively smaller size of the PPAR␤-null mice (data not shown).…”

Section: Ppar␤-null Mice Are Smaller With Reduced Adipose Storesmentioning

confidence: 99%

“…No target genes that are controlled only by PPAR␤ have been identified, but activators for PPAR␤ including fatty acids (27), bezafibrate (28), and a furan-conjugated linoleic acid metabolite (39) are reported to activate reporter gene constructs containing PPREs through PPAR␤. Despite the lack of a specific PPAR␤ ligand to induce activation, there are several reports suggesting roles for PPAR␤ in adipocyte differentiation (5), brain function (51), epidermal differentiation (37), uterine implantation (33), and colon cancer (20). In large part, these studies are correlative associations; definitive proof for PPAR␤ function requires the use of a null mouse model.…”

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confidence: 99%

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Growth, Adipose, Brain, and Skin Alterations Resulting from Targeted Disruption of the Mouse Peroxisome Proliferator-Activated Receptor β(δ)

Peters

Lee

Wen

et al. 2000

Molecular and Cellular Biology

614

451

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To determine the physiological roles of peroxisome proliferator-activated receptor ␤ (PPAR␤), null mice were constructed by targeted disruption of the ligand binding domain of the murine PPAR␤ gene. Homozygous PPAR␤-null term fetuses were smaller than controls, and this phenotype persisted postnatally. Gonadal adipose stores were smaller, and constitutive mRNA levels of CD36 were higher, in PPAR␤-null mice than in controls. In the brain, myelination of the corpus callosum was altered in PPAR␤-null mice. PPAR␤ was not required for induction of mRNAs involved in epidermal differentiation induced by O-tetradecanoylphorbol-13-acetate (TPA). The hyperplastic response observed in the epidermis after TPA application was significantly greater in the PPAR␤-null mice than in controls. Inflammation induced by TPA in the skin was lower in wild-type mice fed sulindac than in similarly treated PPAR␤-null mice. These results are the first to provide in vivo evidence of significant roles for PPAR␤ in development, myelination of the corpus callosum, lipid metabolism, and epidermal cell proliferation.

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Section: Ppar␤-null Mice Are Smaller With Reduced Adipose Storesmentioning

confidence: 99%

mentioning

confidence: 99%

Growth, Adipose, Brain, and Skin Alterations Resulting from Targeted Disruption of the Mouse Peroxisome Proliferator-Activated Receptor β(δ)

Peters

Lee

Wen

et al. 2000

Molecular and Cellular Biology

614

451

View full text Add to dashboard Cite

show abstract

“…To date, three subtypes of PPAR have been cloned in amphibians, rodents and humans: PPAR ␣ ( 10 , 11 ), PPAR ␦ (also called PPAR ␤ , NUC-1, or FAAR) ( 12 ), and PPAR ␥ ( 13 ). Various types of fatty acids, some eicosanoids, and some hypolipidemic and antidiabetic drugs have been shown to activate PPARs by acting as their ligands (14)(15)(16).…”

mentioning

confidence: 99%

Possible Role of Fatty Acids in Milk as the Regulator of the Expression of Cytosolic Binding Proteins for Fatty Acids and Vitamin A through PPAR.ALPHA. in Developing Rats

Mochizuki

Kawai

et al. 2007

J Nutr Sci Vitaminol

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Summary Fatty acids in milk are thought to play an important role in intestinal maturation and gene expression in the postnatal small intestine. In this study, we determined the jejunal mRNA levels, in rats, of peroxisome proliferator-activated receptor ␣ (PPAR ␣ ) and PPAR ␦ which are nuclear receptors for fatty acids. We also measured expression of their target genes during the postnatal period, namely liver type fatty acid-binding protein (L-FABP) and cellular retinol-binding protein, type II (CRBPII). The mRNA levels of PPAR ␣ , L-FABP and CRBPII, but not PPAR ␦ , gradually increased during the suckling period and then sharply declined to a low level at the end of the weaning period. Rat pups at 17 d of age, weaned to a high-fat diet, showed significantly greater mRNA levels of PPAR ␣ , L-FABP and CRBPII than those weaned to a low-fat diet. Oral administration of PPAR ␣ ligand, WY14,643 during four consecutive days of the weanling period caused a parallel increase in the mRNA levels of PPAR ␣ , L-FABP and CRBPII genes. Furthermore, caprylic acid and oleic acid, which are major components of fatty acids in milk, induced jejunal PPAR ␣ , L-FABP and CRBPII gene expression. Our results suggest that fatty acids in milk may play a pivotal role in maintaining an enhanced level of expression of L-FABP and CRBPII genes in the small intestine, presumably by acting as inducers of PPAR ␣ gene expression.

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“…Drugs that serve as hypolipidemic agents in humans, including numerous fibrates and WY-14653, are PPAR␣ ligands and agonists (17)(18)(19)(20). PPAR␦ is widely expressed in a variety of tissues, including the brain (21,22). While it has been shown that it may play a role in regulating cholesterol metabolism in an animal model of insulin resistance (M. Recently, several laboratories have examined the effects of PPAR␥ activation on the inflammatory responses of monocytes and macrophages (23,24).…”

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confidence: 99%

Activation of Peroxisome Proliferator-Activated Receptor γ Does Not Inhibit IL-6 or TNF-α Responses of Macrophages to Lipopolysaccharide In Vitro or In Vivo

Thieringer¹,

Fenyk-Melody²,

Grand³

et al. 2000

The Journal of Immunology

184

115

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We have investigated the potential use of peroxisome proliferator-activated receptor γ (PPARγ) agonists as anti-inflammatory agents in cell-based assays and in a mouse model of endotoxemia. Human peripheral blood monocytes were treated with LPS or PMA and a variety of PPARγ agonists. Although 15-deoxy-Δ12,14-prostaglandin J2 (15d-PGJ2) at micromolar concentrations significantly inhibited the production of TNF-α and IL-6, four other high affinity PPARγ ligands failed to affect cytokine production. Similar results were obtained when the monocytes were allowed to differentiate in culture into macrophages that expressed significantly higher levels of PPARγ or when the murine macrophage cell line RAW 264.7 was used. Furthermore, saturating concentrations of a potent PPARγ ligand not only failed to block cytokine production, but also were unable to block the inhibitory activity of 15d-PGJ2. Thus, activation of PPARγ does not appear to inhibit the production of cytokines by either monocytes or macrophages, and the inhibitory effect observed with 15d-PGJ2 is most likely mediated by a PPARγ-independent mechanism. To examine the anti-inflammatory activity of PPARγ agonists in vivo, db/db mice were treated with a potent thiazolidinedione that lowered their elevated blood glucose and triglyceride levels as expected. When thiazolidinedione-treated mice were challenged with LPS, they displayed no suppression of cytokine production. Rather, their blood levels of TNF-α and IL-6 were elevated beyond the levels observed in control db/db mice challenged with LPS. Comparable results were obtained with the corresponding lean mice. Our data suggest that compounds capable of activating PPARγ in leukocytes will not be useful for the treatment of acute inflammation.

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Rat PPARδ Contains a CGG Triplet Repeat and Is Prominently Expressed in the Thalamic Nuclei

Cited by 80 publications

References 0 publications

Growth, Adipose, Brain, and Skin Alterations Resulting from Targeted Disruption of the Mouse Peroxisome Proliferator-Activated Receptor β(δ)

Growth, Adipose, Brain, and Skin Alterations Resulting from Targeted Disruption of the Mouse Peroxisome Proliferator-Activated Receptor β(δ)

Possible Role of Fatty Acids in Milk as the Regulator of the Expression of Cytosolic Binding Proteins for Fatty Acids and Vitamin A through PPAR.ALPHA. in Developing Rats

Activation of Peroxisome Proliferator-Activated Receptor γ Does Not Inhibit IL-6 or TNF-α Responses of Macrophages to Lipopolysaccharide In Vitro or In Vivo

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