Peroxisome proliferator-activated receptor gamma regulates expression of signal transducer and activator of transcription 5A

Olsen, Hanne; Haldosén, Lars-Arne

doi:10.1016/j.yexcr.2005.12.023

Cited by 13 publications

(10 citation statements)

References 47 publications

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“…STAT5A promoter was recently shown to contain numerous PPAR-responsive elements that mediate PPARγ regulatory activity on Stat5a gene expression in rat mammary cells (55). Some of these PPAR-responsive elements are conserved in human STAT5A and STAT5B genes and may similarly mediate PPAR regulatory activities in CD34 + hematopoietic progenitors.…”

Section: Discussionmentioning

confidence: 99%

Human and simian immunodeficiency viruses deregulate early hematopoiesis through a Nef/PPARγ/STAT5 signaling pathway in macaques

Prost¹,

Dantec²,

Augé³

et al. 2008

J. Clin. Invest.

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Section: Discussionmentioning

confidence: 99%

Human and simian immunodeficiency viruses deregulate early hematopoiesis through a Nef/PPARγ/STAT5 signaling pathway in macaques

Prost¹,

Dantec²,

Augé³

et al. 2008

J. Clin. Invest.

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“…2C9_wt_I to IV, EMSA oligonucleotides containing the wild-type form at ERE half-site I to IV; 2C9_mut_I to IV, EMSA oligonucleotides carrying disruptive mutations at ERE half-site I to IV. ERE cons, oligonucleotide comprising a representative ERE consensus sequence shown to bind ER␣ (Olsen and Haldosén, 2006 moter were generated by annealing sense and antisense oligonucleotides (Table 1). Double-stranded oligonucleotides were 32 P-labeled (GE Healthcare, Chalfont St. Giles, Buckinghamshire, UK) using the T4 DNA polynucleotide kinase system (Invitrogen) in a final reaction volume of 25 l.…”

Section: Methodsmentioning

confidence: 99%

“…The migration of this band was identical to the migration of the complex produced by the oligo containing the functional ERE half-site of the CYP2C19 promoter (Mwinyi et al, 2010b) (supplemental figure). Competition experiments were performed with the respective nonlabeled wild-type oligonucleotide (lanes 3 and 4) and an oligonucleotide comprising a representative ERE consensus sequence (Olsen and Haldosén, 2006) (lanes 5 and 6). ER␣ antibody caused a supershift indicated by the black arrow at lane 1.These antibodies also competed away the above indicated CYP2C19 complex (supplemental figure).…”

Section: Er␣ Bindsmentioning

confidence: 99%

The Ligands of Estrogen Receptor α Regulate Cytochrome P4502C9 (CYP2C9) Expression

Mwinyi¹,

Cavaco²,

Yurdakok³

et al. 2011

J Pharmacol Exp Ther

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Cytochrome P4502C9 (CYP2C9) is an important drug-metabolizing enzyme responsible for the metabolism of approximately 16% of all clinically relevant drugs. It was shown previously that the activity of CYP2C9 in vivo is inhibited by oral contraceptives. The mechanisms of this effect have not been elucidated. We hypothesize that this may occur because of the sex steroid-dependent activation of estrogen receptor ␣ (ER␣) with further transactivation of the CYP2C9 gene. Here, we show that the CYP2C9 promoter indeed contains a functionally relevant estrogen responsive element (ERE) half-site at position Ϫ149/Ϫ145. Its ER␣ binding activity was tested by the luciferase gene reporter assay. Promoter constructs bearing this site were cotransfected with ER␣ into Huh7 hepatoma cells and treated with various ER␣ ligands including 4-hydroxytamoxifen (4-OHT), raloxifene (R), 17␤-estradiol (EE), and 17␣-ethinylestradiol (ETE). The luciferase activity driven by the wild-type CYP2C9 promoter construct was up-regulated by 4-OHT and R and significantly or marginally suppressed by ETE and EE, respectively. An identical effect was observed in primary hepatocytes treated with these compounds. Mutations introduced into the ERE half-site abolished the observed effects in the Huh7 cells. Electrophoretic mobility-shift assay revealed sequencespecific binding of a nuclear protein to the oligonucleotide containing the ERE half-site, which was identified as ER␣ by antibody supershift analysis. In addition, the association of ER␣ with CYP2C9 promoter was strongly supported by chromatin immunoprecipitation data. Taken together, these results indicate that ER␣ and its ligands play an important role in the regulation of CYP2C9 expression.

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“…Because onset of cardiovascular disease is associated with obesity/type 2 diabetes, the feedback of CT-1 on PPAR expression in adipocytes may constitute a link between these two diseases [36]. On the contrary, STAT5a appears to be proadipogenic via up-regulation of PPAR and C/EBP , whereas PPAR upregulates STAT5a expression in a positive cross-talk [37].…”

Section: Signal Transducer and Activator Of Transcriptionmentioning

confidence: 99%

Transcriptional regulation of peroxisome proliferator-activated receptors and liver X receptors

Villacorta

Garcia-Barrio²,

Chen

2007

Curr Atheroscler Rep

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Peroxisome proliferator-activated receptors (PPAR) and liver X receptors (LXR) regulate a plethora of biologic processes and key metabolic and physiologic events. Deregulation of their transcription and activity is commonly associated with dyslipidemic disorders, diabetes, cancer, and cardiovascular disease. This review addresses recent advances in our understanding of the molecular mechanisms regulating transcription of these nuclear receptors. The heterogeneity of factors regulating their transcription and activity suggests intricate regulatory networks that determine their tissue expression pattern and their responses to pharmacologic agents. Understanding such mechanisms will facilitate unraveling their protective effects in disease as well as the design of effective targeted therapies.

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Peroxisome proliferator-activated receptor gamma regulates expression of signal transducer and activator of transcription 5A

Cited by 13 publications

References 47 publications

Human and simian immunodeficiency viruses deregulate early hematopoiesis through a Nef/PPARγ/STAT5 signaling pathway in macaques

Human and simian immunodeficiency viruses deregulate early hematopoiesis through a Nef/PPARγ/STAT5 signaling pathway in macaques

The Ligands of Estrogen Receptor α Regulate Cytochrome P4502C9 (CYP2C9) Expression

Transcriptional regulation of peroxisome proliferator-activated receptors and liver X receptors

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