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Jan Christiansen, Astrid M Kolte, Thomas v O Hansen and Finn C Nielsen

- and microfilament-based RNA localization . Genes and Development 12 1593 – 1598 . Herder C Rathmann W Strassburger K Finner H Grallert H Huth C Meisinger C Gieger C Martin S Giani G 2008 Variants of the PPARG, IGF2BP2

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Lucia Kořínková, Martina Holubová, Barbora Neprašová, Lucie Hrubá, Veronika Pražienková, Michal Bencze, Martin Haluzík, Jaroslav Kuneš, Lenka Maletínská and Blanka Železná

to WT saline, but no treatment affected their expression ( Fig. 4D and E ). A similar pattern was observed for peroxisome proliferator-activated receptors Ppara and Pparg , which are other regulators of fatty acid oxidation ( Fig. 4F and G

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Stephen Fitter, Kate Vandyke, Stan Gronthos and Andrew C W Zannettino

5′-gtcatagtccgcctagaagcat-3′; CCAAT/enhancer binding protein, alpha ( CEBPA ), 5′-gggcaaggccaagaagtc-3′ and 5′-ttgtcactggtcagctccag-3′; peroxisome proliferator-activated receptor gamma 2 ( PPARG ), 5′-ctcctattgacccagaaagc-3′ and 5

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Stefania Carobbio, Barry Rosen and Antonio Vidal-Puig

population by serial passage in serum and FGF followed by expression of adipogenic transcription factors via inducible (Tet system) lentiviral constructs to induce adipocyte terminal differentiation. Expression of PPARg2 alone results in very efficient

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Alexander Kot, Zhendong A Zhong, Hongliang Zhang, Yu-An Evan Lay, Nancy E Lane and Wei Yao

to osteoclasts including: osteoclast differentiation, NF-kappa B signaling and TNF signaling ( Table 4 ). In the osteoclast differentiation pathway, three genes were upregulated in male PRcKO osteoprogenitors: Csf1, Pparg and Tnfrsf11b . Many

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Huixia Li, Zhuanmin Zhang, Dongxu Feng, Lin Xu, Fang Li, Jiali Liu, Xinxin Jin, Zhuang Qian, Xiaomin Kang and Hongzhi Sun

observed no significant changes in Adipoq , Ap2 , and Pparg mRNA expression in AT between PGRN-treated mice and controls ( Fig. 3B ), several cytokines including TNF-α, IL-1β, and IL-6 were elevated in plasma or AT from PGRN-treated mice ( Fig. 3B and

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H Roger Lijnen and Ilse Scroyen

comparable for DC101 and 1C8 treatment (13±0.42 vs 13±0.55 mg/g tissue). In SC or GON adipose tissues, no significant differences were observed in the expression of Ppar γ ( Pparg ), adiponectin, or Glut4 between treatment with DC101 or 1C8 ( Fig. 3A, B

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Abby F Fleisch, Robert O Wright and Andrea A Baccarelli

intake during early pregnancy and later childhood adiposity. RXRA may be involved in insulin sensitivity, adipogenesis, and fat metabolism based on its interaction with PPARG when serving as a transcription factor ( Godfrey et al . 2011 ). These rodent

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Loes P M Duivenvoorde, Evert M van Schothorst, Annelies Bunschoten and Jaap Keijer

are rate limiting enzymes in cholesterol synthesis, while Elovl6 controls the first, rate limiting condensation step of fatty acid elongation ( Leonard et al . 2004 ). The transcription of Ppara and Pparg , two other key regulators of lipid

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He Jiang, Xiao-Ping Ye, Zhong-Yin Yang, Ming Zhan, Hai-Ning Wang, Huang-Min Cao, Hui-Jun Xie, Chun-Ming Pan, Huai-Dong Song and Shuang-Xia Zhao

TNF α , MCP1 ( CCL2 ), and IL6 and decreases the mRNA and protein levels of adiponectin and PPARγ (PPARG). These data suggest that an unfavorable adipokine profile may be created by hyperaldosteronism. However, the molecular and cellular mechanisms