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The transcription factor Pax8 plays an important role in the expression of the differentiated phenotype of thyroid follicular cells. It has recently been shown that Pax8 is necessary for thyroglobulin (Tg) gene expression in the fully differentiated rat thyroid cell line PC. We have used the PC model system to investigate the role of Pax8 as a mediator of TSH regulation of Tg gene expression. We have demonstrated that Pax8 expression, as well as Tg expression, is severely reduced in cells grown in the absence of hormones and serum. The re-addition of TSH or forskolin to the culture medium is able to restore to wild-type levels the expression of both Pax8 and Tg. We have determined that the action of TSH/forskolin on Pax8 is at the transcriptional level. However, the re-expression of Pax8 can be observed several hours before that of Tg, suggesting that either another factor is needed or that Pax8 itself must be post-translationally modified by a newly synthesized protein to become active. To distinguish between these two possibilities we have stably transfected into PC cells an exogenous Pax8 that is expressed independently of TSH. Our results indicate that in these cells the Tg promoter is still dependent on TSH despite the constitutive presence of Pax8. Furthermore, we also show that in this condition Tg gene transcription requires de novo protein synthesis. In conclusion, TSH regulates the expression of Pax8 at a transcriptional level and also regulates the activity of Pax8 by controlling the expression of one or more as yet unknown factors.
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Growth factors are essential for cellular growth and differentiation in both normal and malignant human breast epithelial cells. In the present study we investigated the effect of epidermal growth factor (EGF), transforming growth factor alpha (TGFalpha) and phorbol myristate acetate (PMA) on chicken ovalbumin upstream promoter-transcription factor (COUP-TF) expression in human breast cancer cells. The orphan receptors COUP-TFI and COUP-TFII are members of the nuclear receptor superfamily. The high degree of evolutionary conservation of these proteins strongly argues for an important biological function. COUP-TF expression was highest in SK-BR3 cells (approximately 130 amol/ micro g total RNA), while the lowest COUP-TF expression was observed in MCF-7 cells (3.5 amol/ micro g total RNA). While treatment of EGF, TGFalpha and PMA induced expression of COUP-TFII, COUP-TFI did not respond to these agents. Oncostatin M (OSM) is known to exert an antiproliferative effect in breast cancer cells. Treatment of MCF-7 cells with OSM resulted in an approximately 90% reduction of COUP-TFII mRNA expression. In SK-BR3 cells, treatment with the MEK inhibitor UO126 resulted in a profound suppression of endogenous COUP-TFII expression. Furthermore, cotreatment with UO126 prevented induction of COUP-TFII expression by EGF in MCF-7 cells. In conclusion, our data provide evidence, for the first time, that mitogenic substances which activate the MAP kinase pathway, can induce COUP-TFII expression. Our results strongly suggest that an active MAP kinase pathway is essential for COUP-TFII expression in human breast cancer cells.
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Core-binding factor A1 (Cbfa1), also called Pebp2 alpha A/AML3, is a transcription factor that belongs to the runt-domain gene family. Cbfa1-deficient mice are completely incapable of both endochondral and intramembranous bone formation, indicating that Cbfa1 is indispensable for osteogenesis. Maturation of chondrocytes in these mice is also disorganized, suggesting that Cbfa1 may also play a role in chondrogenesis. The aim of this study was to examine the expression and regulation of Pebp2 alpha A/AML3/Cbfa1 expression in the chondrocyte-like cell line, TC6. Northern blot analysis indicated that Cbfa1 mRNA was constitutively expressed as a 6.3 kb message in TC6 cells and the level of Cbfa1 expression was enhanced by treatment with bone morphogenetic protein-2 (BMP2) in a time- and dose-dependent manner. This effect was blocked by an RNA polymerase inhibitor, 5,6-dichloro-1-beta-d-ribofuranosylbenzimidazole, but not by a protein synthesis inhibitor, cycloheximide. Western blot analysis of the cell lysates using polyclonal antibody raised against Cbfa1 indicated that BMP2 treatment increased the Cbfa1 protein level in TC6 cells. In TC6 cells, BMP2 treatment enhanced expression of alkaline phosphatase and type I collagen mRNAs but suppressed that of type II collagen mRNA. In addition to TC6 cells, Cbfa1 mRNA was also expressed in primary cultures of chondrocytes and BMP2 treatment enhanced Cbfa1 mRNA expression in these cells similarly to its effect on TC6 cells. These data indicate that the Pebp2 alpha A/AML3/Cbfa1 gene is expressed in a chondrocyte-like cell line, TC6, and its expression is enhanced by treatment with BMP.
Lee Gil Ya Cancer and Diabetes Institute, Department of Endocrinology and Metabolism, Howard Hughes Medical Institute, Gachon Medical Research Institute, Department of Rehabilitation Medicine, College of Pharmacy, Gachon University, 7-45 Songdo‐dong, Yeonsu‐ku, Incheon, Korea
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Lee Gil Ya Cancer and Diabetes Institute, Department of Endocrinology and Metabolism, Howard Hughes Medical Institute, Gachon Medical Research Institute, Department of Rehabilitation Medicine, College of Pharmacy, Gachon University, 7-45 Songdo‐dong, Yeonsu‐ku, Incheon, Korea
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known as the unfolded protein response, which involves double-stranded RNA-activated protein kinase RNA-like kinase (PERK), activating transcription factor 6 (ATF6), and inositol requiring enzyme 1 (IRE1) pathways ( Wu & Kaufman 2006 , Lai et al . 2007
Department of Biochemistry, Faculty of Medicine, University of Hong Kong, Pokfulam, Hong Kong SAR, China
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Department of Biochemistry, Faculty of Medicine, University of Hong Kong, Pokfulam, Hong Kong SAR, China
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Department of Biochemistry, Faculty of Medicine, University of Hong Kong, Pokfulam, Hong Kong SAR, China
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Department of Biochemistry, Faculty of Medicine, University of Hong Kong, Pokfulam, Hong Kong SAR, China
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Department of Biochemistry, Faculty of Medicine, University of Hong Kong, Pokfulam, Hong Kong SAR, China
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complexes through interactions with a large repertoire of transcription factors and components of basal transcription machinery ( Chan & La Thangue 2001 , Vo & Goodman 2001 ). The intrinsic acetyltransferase activity of p300 augments the activation of gene
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specific transcription factors, co-factors, and adaptor proteins. The activity of GR is modulated by post-transcriptional modifications, similar to C/EBPs, and the GR is involved in complex cross-talk with other signaling pathways, for instance nuclear
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this disease every year ( Ferlay et al. 2015 ). Approximately 70% of breast tumors are estrogen receptor α (ERα) positive, and tumor cell proliferation is thought to be dependent on the activity of this hormone-mediated transcription factor ( Hayashi
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Introduction The transcriptional networks driving mammalian cell development and function are only beginning to be elucidated. In many tissues transcription factors critical to normal development and function have been identified but, in general
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Cell and Developmental Biology, Departments of
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target genes required for proper islet cell function. MafA and MafB were only recently linked to Insulin and Glucagon expression and represent the principal members of the large Maf transcription factor family expressed in the pancreas ( Olbrot et al
Department of Physiology and Biophysics, Interdisciplinary Biomedical Sciences Program, Arkansas Children's Nutrition Center, Buck Institute for Age Research, University of Arkansas for Medical Sciences, 4301 W. Markham Street, Little Rock, Arkansas 72202, USA
Department of Physiology and Biophysics, Interdisciplinary Biomedical Sciences Program, Arkansas Children's Nutrition Center, Buck Institute for Age Research, University of Arkansas for Medical Sciences, 4301 W. Markham Street, Little Rock, Arkansas 72202, USA
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Department of Physiology and Biophysics, Interdisciplinary Biomedical Sciences Program, Arkansas Children's Nutrition Center, Buck Institute for Age Research, University of Arkansas for Medical Sciences, 4301 W. Markham Street, Little Rock, Arkansas 72202, USA
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Department of Physiology and Biophysics, Interdisciplinary Biomedical Sciences Program, Arkansas Children's Nutrition Center, Buck Institute for Age Research, University of Arkansas for Medical Sciences, 4301 W. Markham Street, Little Rock, Arkansas 72202, USA
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in the pathobiology of uterine endometrial and breast cancers. Figure 1 Cladogram of the human Sp and KLF transcription factors. The 110-aa domain containing the buttonhead box (BTD)/zinc finger motifs was used for the multiple alignment with ClustalW
