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Y Takazawa
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K Tsuji
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A Nifuji
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H Kurosawa
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Y Ito
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M Noda
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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.

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Yoon Sin Oh 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
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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Youn-Jung Lee 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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Yup Kang 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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Jaeseok Han 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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Oh-Kyung Lim 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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Hee-Sook Jun 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
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

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Jee H Lee Laboratory of Molecular Endocrinology and Diabetes Unit, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts, USA
Department of Biochemistry, Faculty of Medicine, University of Hong Kong, Pokfulam, Hong Kong SAR, China

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Jamie L Volinic Laboratory of Molecular Endocrinology and Diabetes Unit, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts, USA
Department of Biochemistry, Faculty of Medicine, University of Hong Kong, Pokfulam, Hong Kong SAR, China

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Constanze Banz Laboratory of Molecular Endocrinology and Diabetes Unit, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts, USA
Department of Biochemistry, Faculty of Medicine, University of Hong Kong, Pokfulam, Hong Kong SAR, China

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Kwok-Ming Yao Laboratory of Molecular Endocrinology and Diabetes Unit, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts, USA
Department of Biochemistry, Faculty of Medicine, University of Hong Kong, Pokfulam, Hong Kong SAR, China

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Melissa K Thomas Laboratory of Molecular Endocrinology and Diabetes Unit, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts, USA
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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Abraham B Roos Respiratory Medicine Unit, Lung Research Laboratory L4:01, Department of Medicine, Karolinska Institutet, Karolinska University Hospital – Solna, 171 76 Stockholm, Sweden

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Magnus Nord Respiratory Medicine Unit, Lung Research Laboratory L4:01, Department of Medicine, Karolinska Institutet, Karolinska University Hospital – Solna, 171 76 Stockholm, Sweden

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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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Koen D Flach Division of Molecular Pathology, The Netherlands Cancer Institute, Amsterdam, The Netherlands

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Wilbert Zwart Division of Molecular Pathology, The Netherlands Cancer Institute, Amsterdam, The Netherlands

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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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Brad G Hoffman
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Steven J M Jones Department of Cancer Endocrinology, Micheal Smith Genome Sciences Centre, BC Cancer Research Center, 675 West 10th Avenue, Vancouver, BC, Canada V5Z 1L3

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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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Isabella Artner Cell and Developmental Biology, Departments of

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Yan Hang Cell and Developmental Biology, Departments of

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Min Guo Cell and Developmental Biology, Departments of

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Guoqiang Gu Cell and Developmental Biology, Departments of

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Roland Stein Cell and Developmental Biology, Departments of
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

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R C M Simmen 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
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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J M P Pabona 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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M C Velarde 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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C Simmons 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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O Rahal 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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F A Simmen 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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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

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Masaya Takeda Department of Medicine and Clinical Science, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, 2-5-1 Shikata-cho, Okayama City 700-8558, Japan

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Fumio Otsuka Department of Medicine and Clinical Science, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, 2-5-1 Shikata-cho, Okayama City 700-8558, Japan

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Hiroyuki Otani Department of Medicine and Clinical Science, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, 2-5-1 Shikata-cho, Okayama City 700-8558, Japan

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Kenichi Inagaki Department of Medicine and Clinical Science, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, 2-5-1 Shikata-cho, Okayama City 700-8558, Japan

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Tomoko Miyoshi Department of Medicine and Clinical Science, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, 2-5-1 Shikata-cho, Okayama City 700-8558, Japan

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Jiro Suzuki Department of Medicine and Clinical Science, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, 2-5-1 Shikata-cho, Okayama City 700-8558, Japan

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Yukari Mimura Department of Medicine and Clinical Science, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, 2-5-1 Shikata-cho, Okayama City 700-8558, Japan

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Toshio Ogura Department of Medicine and Clinical Science, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, 2-5-1 Shikata-cho, Okayama City 700-8558, Japan

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Hirofumi Makino Department of Medicine and Clinical Science, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, 2-5-1 Shikata-cho, Okayama City 700-8558, Japan

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implicated it in processes of inflammation, atherosclerosis, cell cycle control, apoptosis, and carcinogenesis ( Auwerx 1999 ). PPARs act as a transcription factor when heterodimerized with the retinoid X receptor and bound to the proper ligands, including

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Gary B Silberstein Department of Molecular, Cell and Developmental Biology, Sinsheimer Laboratories, University of California, Santa Cruz, California 95064, USA

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Katharine Van Horn Department of Molecular, Cell and Developmental Biology, Sinsheimer Laboratories, University of California, Santa Cruz, California 95064, USA

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Eva Hrabeta-Robinson Department of Molecular, Cell and Developmental Biology, Sinsheimer Laboratories, University of California, Santa Cruz, California 95064, USA

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Jennifer Compton Department of Molecular, Cell and Developmental Biology, Sinsheimer Laboratories, University of California, Santa Cruz, California 95064, USA

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RANKL. RANKL is the ligand for receptor activator of nuclear factor-kappaB (RANK) and is induced by progesterone ( Fata et al. 2000 , Brisken et al. 2002 ). Pax-2 is a proto-oncogene transcription factor characterized by a paired domain and

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