Genomic structure and analysis of transcriptional regulation of the mouse zinc-fingers and homeoboxes 1 (ZHX1) gene

Shou, Zhangfei; Yamada, Kazuya; Inazu, Tetsuya; Kawata, Hiroko; Hirano, Shogo; Mizutani, Tetsuya; Yazawa, Takashi; Sekiguchi, Toshio; Yoshino, Miki; Kajitani, Takashi; Okada, Kenichiro; Miyamoto, Kaoru

doi:10.1016/s0378-1119(02)01093-4

Cited by 21 publications

(17 citation statements)

References 37 publications

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“…For the inhibition assay, a 200-fold excess of unlabeled competitor oligonucleotide was added in the reaction. Competitor oligonucleotides were synthesized according to the sequences reported previously: Oct, YY and NF-Y (19), Myb (20), Sox (21) and NF-κB (22). For the supershift assay, 2 μg of rabbit polyclonal IgG Ab (Ab) against c-Myc (A-14) (Santa Cruz Biotechnology) was preincubated with the nuclear extracts for 30 min at room temperature and the mixture was subjected to EMSA.…”

Section: Methodsmentioning

confidence: 99%

Regulation of Id2 expression by CCAAT/enhancer binding protein

Karaya

Mori²,

Kimoto³

et al. 2005

Nucleic Acids Research

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Mice deficient for Id2, a negative regulator of basic helix–loop–helix (bHLH) transcription factors, exhibit a defect in lactation due to impaired lobuloalveolar development during pregnancy, similar to the mice lacking the CCAAT enhancer binding protein (C/EBP) β. Here, we show that Id2 is a direct target of C/EBPβ. Translocation of C/EBPβ into the nucleus, which was achieved by using a system utilizing the fusion protein between C/EBPβ and the ligand-binding domain of the human estrogen receptor (C/EBPβ-ERT), demonstrated the rapid induction of endogenous Id2 expression. In reporter assays, transactivation of the Id2 promoter by C/EBPβ was observed and, among three potential C/EBPβ binding sites found in the 2.3 kb Id2 promoter region, the most proximal element was responsible for the transactivation. Electrophoretic mobility shift assay (EMSA) identified this element as a core sequence to which C/EBPβ binds. Chromatin immunoprecipitation (ChIP) furthermore confirmed the presence of C/EBPβ in the Id2 promoter region. Northern blotting showed that Id2 expression in C/EBPβ-deficient mammary glands was reduced at 10 days post coitus (d.p.c.), compared with that in wild-type mammary glands. Thus, our data demonstrate that Id2 is a direct target of C/EBPβ and provide insight into molecular mechanisms underlying mammary gland development during pregnancy.

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Section: Methodsmentioning

confidence: 99%

Regulation of Id2 expression by CCAAT/enhancer binding protein

Karaya

Mori²,

Kimoto³

et al. 2005

Nucleic Acids Research

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“…A 1.1-kb EcoRI/MluI fragment of the pF3, a 1.3-kb EcoRI fragment of the pGK5, a 1.9-kb PstI/ DraI fragment of the pLPK57, a 1.8-kb EcoRI fragment of the pUC119-FAS, and a 1.2-kb PstI fragment of the pUC18-PEPCK were used as the probes for SHARP-2, glucokinase (GK), LPK, FAS, and phosphoenolpyruvate carboxykinase (PEPCK), respectively (23)(24)(25). For cDNA cloning mouse 36B4, a ribosomal protein, reverse transcription-polymerase chain reaction was carried out using oligonucleotides, 5Ј-ATGCCCAG-GGAAGACAGGGCGACC-3Ј and 5Ј-TTAGTCGAAGAGACCGAATCC-CATA-3Ј as primers and mouse liver cDNA as a template (26). The product was subcloned into the pGEM-T Easy to give pGEM-T Easy 36B4.…”

Section: Methodsmentioning

confidence: 99%

Insulin Induces the Expression of the SHARP-2/Stra13/DEC1 Gene via a Phosphoinositide 3-Kinase Pathway

Yamada

Kawata

Shou

et al. 2003

Journal of Biological Chemistry

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Transcription of the rat fatty acid synthase (FAS) gene in the rat liver can be regulated by feeding a high carbohydrate diet. A carbohydrate response element (ChoRE) located on the rat FAS gene promoter has been identified. Using multiple copies of the ChoRE as the bait in a yeast one-hybrid system, a rat liver cDNA library was screened, and the cDNA of ChoRE-binding proteins was cloned. A positive clone that encodes a basic helix-loop-helix protein, enhancer of split-and hairy-related protein-2 (SHARP-2), was obtained. Northern blot analysis revealed that the levels of SHARP-2 mRNA increase when a high carbohydrate diet is fed to normal rats or when insulin is administered to diabetic rats. In primary cultured rat hepatocytes, insulin rapidly induced an accumulation of SHARP-2 mRNA even in the absence of glucose. A time course for the increase in SHARP-2 mRNA levels indicated that it followed by those of FAS and L-type pyruvate kinase mRNAs and that the initial time course of SHARP-2 mRNA was similar to changes in the levels of glucokinase mRNA and phosphoenolpyruvate carboxykinase mRNA. Although wortmannin, LY294002, and actinomycin D blocked the increase in SHARP-2 mRNA levels by insulin, rapamycin, staurosporine, PD98059, okadaic acid, and 8-bromocyclic AMP had no effect. In addition, nuclear run-on assay revealed that transcription of the rat SHARP-2 gene was induced by insulin. Thus, we conclude that insulin induces the transcription of the rat SHARP-2 gene via a phosphoinositide 3-kinase pathway.

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“…Reverse transcription and polymerase chain reaction (RT-PCR) was performed as described previously [14]. Primers used were 5Ј-CACGG ACGCA GGTTC ACCGT GG-3Ј and 5Ј-CCGGT CTAGA TTAGT CTTTG GTTTC TAAGT TTAAA GG-3Ј oligonucleotides for SHARP-2 and 5Ј-GAACG GGAAG CTCAC TGGCA-3Ј and 5Ј-TCCAC CACCC TGTTG CTGTA-3Ј oligonucleotides for glyceraldehyde 3-phosphate dehydrogenase (GAPDH).…”

Section: Reverse Transcription Polymerase Chain Reaction Analysismentioning

confidence: 99%

Gene Expression of Basic Helix-Loop-Helix Transcription Factor, SHARP-2, Is Regulated by Gonadotropins in the Rat Ovary and MA-10 Cells1

Yamada

Kawata

Mizutani

et al. 2004

Biology of Reproduction

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Basic helix-loop-helix (bHLH) proteins regulate transcription from the E box sequence (5'-CANNTG-3') located in the regulatory region of most gene promoters. The rat enhancer of split- and hairy-related protein 2 (SHARP-2) is a member of the bHLH protein family. To analyze the possible role of SHARP-2 in the rat ovary, the regulation of the expression of the SHARP-2 gene was examined, and the SHARP-2 protein was characterized. Northern blot analysis revealed that the level of SHARP-2 mRNA abruptly and temporarily increases as the result of the action of LH, i.e., eCG or hCG treatment alone or hCG after eCG treatment, in the rat ovary, as indicated by the treatment of primary cultured rat granulosa cells with hCG after FSH treatment or of mouse Leydig MA-10 cells with hCG or 8-bromoadenosine 3',5'-cyclic monophosphate. An in situ hybridization analysis showed that eCG treatment increases the level of the SHARP-2 transcript in theca interna cells and that hCG treatment, after the administration of eCG, increases the level of the SHARP-2 transcript in granulosa cells. Furthermore, transfection experiments with green fluorescence protein (GFP) expression vectors into primary cultured granulosa cells and MA-10 cells revealed that the entire coding sequence of SHARP-2 fused to the GFP is localized in the nucleus. The transcriptional activity of SHARP-2 also was examined using transient DNA transfection experiments. When an expression vector encoding the full length of SHARP-2 was cotransfected with thymidine kinase promoter-luciferase reporter plasmids, with or without E box sequences, into MA-10 cells, the luciferase activity was decreased in an E box-dependent manner. We conclude that the level of SHARP-2 mRNA is regulated by gonadotropins and that SHARP-2 functions as a transcriptional repressor localized in the nucleus.

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Genomic structure and analysis of transcriptional regulation of the mouse zinc-fingers and homeoboxes 1 (ZHX1) gene

Cited by 21 publications

References 37 publications

Regulation of Id2 expression by CCAAT/enhancer binding protein

Regulation of Id2 expression by CCAAT/enhancer binding protein

Insulin Induces the Expression of the SHARP-2/Stra13/DEC1 Gene via a Phosphoinositide 3-Kinase Pathway

Gene Expression of Basic Helix-Loop-Helix Transcription Factor, SHARP-2, Is Regulated by Gonadotropins in the Rat Ovary and MA-10 Cells1

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