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sperm; apoptosis? GPX5 Unknown GPX6 GPX1 homologue? Thioredoxin reductase (TRs) Multiple roles including dithiol-disulphide oxoreductase Detoxifies peroxides, reduces thioredoxin (control of cell growth); maintains redox state of transcription factors
Center for Health Disparities and Molecular Medicine, School of Medicine, Loma Linda University, Loma Linda, California, USA
Division of Biochemistry, Department of Basic Sciences, School of Medicine, Loma Linda University, Loma Linda, California, USA
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Center for Health Disparities and Molecular Medicine, School of Medicine, Loma Linda University, Loma Linda, California, USA
Division of Biochemistry, Department of Basic Sciences, School of Medicine, Loma Linda University, Loma Linda, California, USA
Department of Medicine, School of Medicine, Loma Linda University, Loma Linda, California, USA
Department of Orthopedics, School of Medicine, Loma Linda University, Loma Linda, California, USA
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mechanism by which the TRs mediate the effects of TH is by acting as nuclear receptors, ligand-inducible transcription factors which regulate the expression of target genes. However, recent studies have determined that TH can exert nongenomic effects in
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). Peroxisome proliferator-activated receptors (PPARs) are ligand-activated transcription factors that regulate the expression of target genes involved in lipid homeostasis and in antioxidant and anti-inflammatory processes ( Wahli & Michalik 2012 ). Endogenous
Pharmacology Research 4, Novo Nordisk A/S, Novo Nordisk Park F6.2.13, DK 2760 Måløv, Denmark
Steno Diabetes Center, Niels Steensensvej 2, DK 2820 Gentofte, Denmark
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Pharmacology Research 4, Novo Nordisk A/S, Novo Nordisk Park F6.2.13, DK 2760 Måløv, Denmark
Steno Diabetes Center, Niels Steensensvej 2, DK 2820 Gentofte, Denmark
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Pharmacology Research 4, Novo Nordisk A/S, Novo Nordisk Park F6.2.13, DK 2760 Måløv, Denmark
Steno Diabetes Center, Niels Steensensvej 2, DK 2820 Gentofte, Denmark
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Pharmacology Research 4, Novo Nordisk A/S, Novo Nordisk Park F6.2.13, DK 2760 Måløv, Denmark
Steno Diabetes Center, Niels Steensensvej 2, DK 2820 Gentofte, Denmark
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Pharmacology Research 4, Novo Nordisk A/S, Novo Nordisk Park F6.2.13, DK 2760 Måløv, Denmark
Steno Diabetes Center, Niels Steensensvej 2, DK 2820 Gentofte, Denmark
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hGH and cytokines on the induction of SOCS-3 mRNA expression after extended exposure. Effects of hGH and cytokines on activation of the transcription factors NFκB, STAT1 and STAT5 To determine whether activation of
London Regional Cancer Program, Biochemistry, 790 Commissioners Road, Room A4-921, London, Ontario, N6A 4L6 Canada Departments of
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London Regional Cancer Program, Biochemistry, 790 Commissioners Road, Room A4-921, London, Ontario, N6A 4L6 Canada Departments of
London Regional Cancer Program, Biochemistry, 790 Commissioners Road, Room A4-921, London, Ontario, N6A 4L6 Canada Departments of
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100 kb of the STC2 gene ( Lin et al . 2007 ). Therefore, it seems likely that for E 2 regulation of the STC2 gene, other transcription factors may be mediating the effect as has been documented for the Sp1, AP-1 and nuclear factor-κB ( Chambliss
Departments of Medicine,
Physiology and Pharmacology,
Paediatrics, University of Western Ontario, London, Ontario, Canada N6A 4V2
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Departments of Medicine,
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Paediatrics, University of Western Ontario, London, Ontario, Canada N6A 4V2
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Departments of Medicine,
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Paediatrics, University of Western Ontario, London, Ontario, Canada N6A 4V2
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Departments of Medicine,
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Paediatrics, University of Western Ontario, London, Ontario, Canada N6A 4V2
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was performed using Taqman probe technologies in an ABI PRISM 7900HT Sequence Detection System (Applied Biosystems, Foster City, CA, USA) to determine the relative abundance of the transcription factor Pdx-1 (Mn00435565_m1) and nestin (Rn00564394_m1
Biology, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong, China
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Biology, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong, China
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Biology, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong, China
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Biology, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong, China
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.aist.go.jp/research/db/TFSEARCH.html ) revealed a number of putative transcription factor-binding sites on the 5′-flanking region of the seabream ghrelin gene (Fig. 5 ). Functional mapping of the seabream ghrelin promoter The promoter activity of the 5
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confirmed by increased creatine kinase (CK) activity and morphological differentiation, which was indicated by myotube formation. We have also examined the effect of PD98059 not only on the expression levels of myogenic transcriptional factor mRNAs (myogenin
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The p100 coactivator, first identified as a coactivator of the Epstein-Barr virus-encoded transcription factor, EBNA-2, in cultured cells, interacts with a number of transcription factors. However, the role of p100 in animals is unclear. We found that the abundance of p100 is closely associated with the lactating state in mammary tissue of mice and cows. Using two antibodies against independent parts of the protein, p100 immunoreactivity was localised to mammary epithelial cells, and was enriched in both nuclei and endoplasmic reticulum/organelle fractions. Stimulation of beta-casein expression in cultured mammary epithelial cells was associated with an increase in abundance of the p100 protein. The relative abundance of p100 mRNA was not altered in mammary tissue throughout the gestation-lactation cycle, indicating that the abundance of p100 is altered by a post-transcriptional mechanism. Further work is required to clarify the function of p100 in mammary epithelial cells.
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Expression of transcription factors binding to the activating protein-1 (AP-1) site is induced by estrogens in association with epithelial proliferation in the uterus, but, in the oviduct, the relationship between cell proliferation and differentiation and AP-1 transcription factors is not well understood. In the developing rat oviduct, we found that proliferation and differentiation of epithelial cells were region-dependently regulated by 17beta-estradiol (E2). To determine the role of AP-1 transcription factors in the development of rat oviduct, we performed immunohistochemistry for epithelial c-jun and c-fos proteins in E2-untreated and -treated newborn rats. E2 increased the expression of c-jun and c-fos during proliferation of undifferentiated epithelial cells, but diminished both proteins during accelerated differentiation of ciliated epithelial cells. A pure estrogen receptor (ER) antagonist, ICI 182,780, inhibited changes in their expression during both cell proliferation and differentiation. Importantly, no reduction of c-jun was noted in the epithelial cells of the foxj1-deficient oviduct, which lacks cilia development. This study shows that c-jun and c-fos are regulated during epithelial cell proliferation and differentiation in a region-specific manner. This provides critical information for understanding the molecular and cellular mechanisms of the development of the neonatal oviduct.