cyclin d1 Search Results


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  • 94
    Millipore cdk4 cyclind1
    Effect of 7,3′,4′-THIF on the kinase activities of the <t>cyclin</t> <t>D1-CDK4</t> and cyclin E-CDK2 complexes and direct binding to CDK4 and CDK2. A , 7,3′,4′-THIF suppresses the activity of the cyclin D1-CDK4 and cyclin E-CDK2 complexes.
    Cdk4 Cyclind1, supplied by Millipore, used in various techniques. Bioz Stars score: 94/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Cell Signaling Technology Inc cyclin d1 2978
    Repeated low-dose NaAsO 2 exposure induced phosphorylated protein expression of GSK-3β/cyclinD1, p21 and p27 was regulated by AKT. Protein expression was detected by the Western blot analysis. (A) Images are the representative results of three separate experiments. Quantitative graphs ( n = 3) showed the relative intensity of the target proteins compare with β-actin, including p -AKT (B) , p -GSK-3β (C) , total <t>cyclin</t> D1 (D) , p -cyclin D1 (E) , p -p21 (F) , p -p27 (G) , total p21 (H) and total p27 (I) . NaAsO 2 exposure induced increased expression of p -AKT, p -GSK-3β, total cyclin D1, p -p21, and p -p27, but decreased expression of p -cyclin D1, total p21, and total p27. Treatment of MK2206 significantly reversed the expression of all of the above proteins. Significant difference was defined as p less than 0.05. a, vs. the corresponding 0 μM group; b, vs. the corresponding 0.05 μM group; c, vs. the MK2206(-) group of the same NaAsO 2 concentration.
    Cyclin D1 2978, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 37 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Cell Signaling Technology Inc cyclin d1
    Tbx2 regulated expression of endogenous Ccnd1 . Knockdown of Tbx2 led to down‐regulation of Ccnd1 expression (a, b). (a) Relative fold change in mRNA levels of candidate proliferation‐related genes in melan‐a cell transfected with si‐Tbx2‐1 or si‐Tbx2‐2 compared to mock cells. Down‐regulation of Tbx2 caused reduction of several proliferation‐related genes, including Ccnd1 , Bcl9l , Cdca7 , Mphosph9, and Dna2 . (b) Western blot analysis of TBX2 and <t>Cyclin</t> D1 expression in melan‐a cell transfected with si‐C, si‐Tbx2‐1 or si‐Tbx2‐2. Note that knockdown of Tbx2 lead to reduction in levels of Cyclin D1, consistent with reduction in Tbx2 mRNA seen in (a). Intensity of bands was measured using ImageJ software and fold‐change compared to level seen in mock cells is indicated. (c) Immunolabelling for TBX2, Cyclin D1, and MITF in melan‐a cells showed that TBX2 and Cyclin D1 colocalized in nuclei of melan‐a cells. Bar = 20 μm. (d, e) Overexpression of TBX2 up‐regulated expression of Ccnd1 . Melan‐a cells were infected with the GFP or GFP‐TBX2 lentivirus, respectively, and cells were continually cultured for at least a week. (d) Relative fold‐change in mRNA levels of candidate proliferation‐related genes in melan‐a cells overexpressing TBX2. Results show that overexpression of TBX2 lead to up‐regulation of Ccnd1 . (e) Western blot analysis of TBX2 and Cyclin D1 expression in TBX2‐overexpressing melan‐a cells. Note that expression of Cyclin D1 increased after overexpression of Tbx2 . Intensity of bands was measured using ImageJ software and fold‐change was compared to expression in mock cells. Data for (a) and (d) are from triplicate experiments and are represented as mean ± SD. * P
    Cyclin D1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 9522 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Abcam cyclind1
    MiR-374b increases GIST-T1 cell cycle entry (A) Results of GIST cell apoptosis in each group by flow cytometry. (B) Expressions of P53 and <t>cyclinD1</t> by RT-qPCR. (C) Protein levels of P53 and cyclinD1 by Western blotting; p
    Cyclind1, supplied by Abcam, used in various techniques. Bioz Stars score: 94/100, based on 574 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Roche cyclin d1
    Vitamin D 3 -dependent VDR signaling reduces β-catenin transcriptional activity A. Western analysis demonstrating a dose-dependent reduction in active β-catenin (ABC) levels in R7 cells treated with the designated concentrations of 1,25D 3 for 48 hours, but no change in total β-catenin. B. qRT-PCR analysis of β-catenin target genes <t>cyclin</t> D1, TCF-7, VEGF, and MMP7 in R7 cells treated with the designated concentrations of 1,25D 3 for 72 hours. Data represent mean values from three independent experiments ± SE. C. Dual luciferase assays in R7 cells co-transfected with Topflash and pRLTX (expressing Renilla ) plasmids for 48 hours, then treated with the designated concentrations of 1,25D 3 for 24 hours. Luciferase activities were normalized for transfection efficiency to Renilla activity. Data represent mean values from three independent experiments ± SE. D. Crystal violet staining of R7 cells transfected with a stabilized form of β-catenin (ΔN) or empty vector and treated with 100 nM 1,25D 3 or vehicle control (EtOH). Data represent mean values from four independent experiments ± SE. * P
    Cyclin D1, supplied by Roche, used in various techniques. Bioz Stars score: 92/100, based on 217 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Becton Dickinson cyclin d1
    Canonical miR-34a growth control targets are poorly expressed in LCLs relative to HCT-116 cells. (a) Relative mRNA levels as determined by qRT-PCR of <t>cyclin</t> D1, D2, and E2; cdk4; cdk6; and c-Met in LCLs and HCT-116 cells. The asterisk indicates a value below the threshold for detection. (b) Western analysis of miR-34a targets in HCT-116 cells and EF3D LCLs expressing pcDNA3 vector (−) or pCDNA3-miR-34a (+). Quantitation of protein expression is noted below each band.
    Cyclin D1, supplied by Becton Dickinson, used in various techniques. Bioz Stars score: 92/100, based on 565 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Santa Cruz Biotechnology cyclin d1
    SNHG20 knockdown regulated several genes related to proliferation and metastasis ( A , B ) The mRNA level of P21, <t>Cyclin</t> D1, Vimentin, and E-cadherin was detected by qRT-PCR in A2780 and CAOV-3 cells transfecting with si-SNHG20-1 or -2 (* P
    Cyclin D1, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 94/100, based on 10420 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Agilent technologies cyclin d1
    <t>Cyclin</t> D1 strong positive expression in invasive ductal carcinoma of no special type (× 100)
    Cyclin D1, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 93/100, based on 582 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    R&D Systems cyclin d1
    <t>Cyclin</t> D1 strong positive expression in invasive ductal carcinoma of no special type (× 100)
    Cyclin D1, supplied by R&D Systems, used in various techniques. Bioz Stars score: 90/100, based on 20 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Proteintech cyclin d1
    Pim-1 depletion altered the RUNX3, <t>Cyclin</t> D1 and CDK4 levels. A . Western blot analysis showed the expression of RUNX3 protein in SACC cells after Pim-1 siRNA transfection. The expression of GAPDH was used as a loading control. B . Western blot analysis showed the expression Cyclin D1 and CDK4 protein in SACC cells after Pim-1 siRNA transfection. The expression of β-actin was used as a loading control.
    Cyclin D1, supplied by Proteintech, used in various techniques. Bioz Stars score: 92/100, based on 600 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Addgene inc cyclin d1
    GCN5 directly binds to the <t>cyclin</t> E1, cyclin D1, and E2F1 promoters, increasing histone H3 and H4 acetylation levels within these regions. A, cyclin E1, cyclin D1, and E2F1 luciferase reporter assay performed in HEK293T cells. Empty control vector and
    Cyclin D1, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 86 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Merck KGaA cyclin d1
    Effects of PKF 115–584 on <t>Cyclin</t> D1 expression. A, B : Cyclin D1 mRNA expression in non-treated endometrial epithelial (A) and stromal (B) cells of patients with and without endometriosis. Endo (+) (M: n = 6, P: n = 20, ES: n = 7, MS: n = 15, LS: n = 6). Endo (–) (M: n = 4, P: n = 11; ES: n = 8, MS: n = 8; LS: n = 4). C, D : Cyclin D1 mRNA expression in PKF 115–584–treated endometrial epithelial (C) and stromal (D) cells of patients with and without endometriosis. Endo (+):(M: n = 6, P: n = 20, ES: n = 7, MS: n = 15, LS: n = 6). Endo (–):(M: n = 4, P: n = 11, ES: n = 8, MS: n = 8, LS: n = 4). E : Cyclin D1 protein expression in non-treated and PKF 115–584–treated endometrial epithelial cells from the mid-secretory and menstrual phases. Endo (+):(M: n = 4, MS: n = 5). Endo (–):(M: n = 4, MS: n = 5). F : Representative photomicrographs of western blot analysis in non-treated and PKF 115–584–treated endometrial epithelial from the mid-secretory phase. Numerical values are presented as the mean+SEM. Expression levels of Cyclin D1 mRNA are given relative to the expression levels of the reference gene, GAPDH. Relative density is density of Cyclin D1 relative to that of Actin. M: menstrual phase, P: proliferative phase, ES: early secretory phase, MS: mid- secretory phase, LS: late secretory phase. a: p
    Cyclin D1, supplied by Merck KGaA, used in various techniques. Bioz Stars score: 92/100, based on 37 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Leica Microsystems cyclin d1
    Effects of PKF 115–584 on <t>Cyclin</t> D1 expression. A, B : Cyclin D1 mRNA expression in non-treated endometrial epithelial (A) and stromal (B) cells of patients with and without endometriosis. Endo (+) (M: n = 6, P: n = 20, ES: n = 7, MS: n = 15, LS: n = 6). Endo (–) (M: n = 4, P: n = 11; ES: n = 8, MS: n = 8; LS: n = 4). C, D : Cyclin D1 mRNA expression in PKF 115–584–treated endometrial epithelial (C) and stromal (D) cells of patients with and without endometriosis. Endo (+):(M: n = 6, P: n = 20, ES: n = 7, MS: n = 15, LS: n = 6). Endo (–):(M: n = 4, P: n = 11, ES: n = 8, MS: n = 8, LS: n = 4). E : Cyclin D1 protein expression in non-treated and PKF 115–584–treated endometrial epithelial cells from the mid-secretory and menstrual phases. Endo (+):(M: n = 4, MS: n = 5). Endo (–):(M: n = 4, MS: n = 5). F : Representative photomicrographs of western blot analysis in non-treated and PKF 115–584–treated endometrial epithelial from the mid-secretory phase. Numerical values are presented as the mean+SEM. Expression levels of Cyclin D1 mRNA are given relative to the expression levels of the reference gene, GAPDH. Relative density is density of Cyclin D1 relative to that of Actin. M: menstrual phase, P: proliferative phase, ES: early secretory phase, MS: mid- secretory phase, LS: late secretory phase. a: p
    Cyclin D1, supplied by Leica Microsystems, used in various techniques. Bioz Stars score: 92/100, based on 17 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Thermo Fisher cyclin d1
    Effect of lovastatin and docetaxel on expression of genes involved in the initiation and progression of mitosis, cytokinesis, and MAP kinases signalling pathway. HGT-1 cells were treated with 12.5 μ lovastatin (L12.5) or with 5 or 10 n docetaxel (D5 or D10) alone or in combination for 48 h. <t>Cyclin</t> D1, cyclin B1, aurora kinase A ( A ), aurora kinase B and survivin ( B ) mRNA levels were analysed by real-time RT–PCR. Relative mRNA levels were normalised to P0 mRNA levels. Values are means±s.d. ( n =4). * Compared with control, #compared with docetaxel treatment, † compared with lovastatin treatment. One symbol: P
    Cyclin D1, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 93/100, based on 2539 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Epitomics cyclin d1
    LMP1 increased the binding ability of transcription factors EGFR and STAT3 to <t>cyclin</t> D1 promoter in vitro . (A) STAT3 binding activities within the cyclin D1 promoter were examined by EMSA. A biotin-labeled wild-type STAT3 oligonucleotide probe was incubated with nuclear extracts of CNE1 and CNE1-LMP1 cells in the presence of a 200-fold excess of unlabeled wild-type STAT3 (lane 4), unlabeled mutant STAT3 oligonucleotides (lane 5), or noncompetitive unlabeled NF-κB oligonucleotide (NS, lane 6). Biotin-labeled mutant STAT3 oligonucleotide probe was incubated with nuclear extracts of the indicated NPC cell lines (lanes 8–9). (B) Ten micrograms of nuclear extracts were pre-incubated with biotin-labeled STAT3 oligonucleotide probe in the presence of inhibitors directed against different phosphorylation sites of STAT3 (indicated above each lane). (C) The biotin-labeled wild-type EGFR oligonucleotide probe was incubated with nuclear extracts of CNE1 and CNE1-LMP1 cells in the presence of a 200-fold excess of unlabeled wild-type EGFR (lane 4), unlabeled mutant EGFR oligonucleotides (lane 6) or noncompetitive unlabeled NFκB oligonucleotide (NS, lane 7), and then EGFR DNA binding activities were examined by EMSA. (D-E) The nuclear extracts of CNE1 and CNE1-LMP1 cells were pre-incubated with biotin-labeled EGFR oligonucleotide probe in the presence of inhibitors AG1478, directed against phosphorylation of EGFR, or DNAzyme 1 (DZ1), targeting LMP1. RD: relative density.
    Cyclin D1, supplied by Epitomics, used in various techniques. Bioz Stars score: 92/100, based on 622 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Sangon Biotech cyclin d1
    Protein expression of <t>Cyclin</t> D1, p-Akt and Akt increased in miR-17 mimic-transfected rat glioma C6 cells. Protein expression of Cyclin D1, p-Akt and Akt in glioma C6 cells was detected by Western Blot. After glioma C6 cells were transfected with inhibitor of miR-17 (200 nM) for 72 h, the protein expression of Cyclin D1, Akt and p-Akt increased compared to Lipofectamine and negative control groups. * indicates that p
    Cyclin D1, supplied by Sangon Biotech, used in various techniques. Bioz Stars score: 92/100, based on 127 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    Cell Signaling Technology Inc anti cyclin d1
    miR-614 suppresses PPP2R2A expression by directly targeting the PPP2R2A 3′-UTR and altered levels of proteins associated with cell proliferation and cell apoptosis in A2780 cells. (A) Predicted miR-614c target sequence in the 3′-UTR of PPP2R2A (PPP2R2A-3′-UTR) and positions of three mutated nucleotides (red) in the 3′-UTR of miR-614 (miR-614-mut). (B) Expression of PPP2R2A in A2780 cells transfected with miR-614 or the miR-614-in were detected by western blotting analysis. α-tubulin served as the loading control. (C) Luciferase reporter assay of A2780 cells transfected with the pGL3-PPP2R2A-3′-UTR reporter and miR-614 or miR-614-in or miR-614-mut oligonucleotides. (D) Reverse transcription-quantitative polymerase chain reaction analysis of expression of BAD and <t>Cyclin</t> D1 in A2780 cells. (E) Western blot analysis of protein expression of Cyclin D1, BAD, p-Rb and Rb in A2780 cells. α-tubulin served as the loading control. *P
    Anti Cyclin D1, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 94/100, based on 2096 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Effect of 7,3′,4′-THIF on the kinase activities of the cyclin D1-CDK4 and cyclin E-CDK2 complexes and direct binding to CDK4 and CDK2. A , 7,3′,4′-THIF suppresses the activity of the cyclin D1-CDK4 and cyclin E-CDK2 complexes.

    Journal: The Journal of Biological Chemistry

    Article Title: 7,3?,4?-Trihydroxyisoflavone Inhibits Epidermal Growth Factor-induced Proliferation and Transformation of JB6 P+ Mouse Epidermal Cells by Suppressing Cyclin-dependent Kinases and Phosphatidylinositol 3-Kinase *

    doi: 10.1074/jbc.M109.094797

    Figure Lengend Snippet: Effect of 7,3′,4′-THIF on the kinase activities of the cyclin D1-CDK4 and cyclin E-CDK2 complexes and direct binding to CDK4 and CDK2. A , 7,3′,4′-THIF suppresses the activity of the cyclin D1-CDK4 and cyclin E-CDK2 complexes.

    Article Snippet: Assays of cyclin D1-CDK4 and cyclin E-CDK2 kinase activity were performed in accordance with instructions provided by Millipore Corp.

    Techniques: Binding Assay, Activity Assay

    Effect of 7,3′,4′-THIF on G 1 phase-related proteins in EGF-stimulated JB6 P+ cells. A , 7,3′,4′-THIF inhibits EGF-induced expression of cyclin D1, CDK4, cyclin E, and CDK2 in JB6 P+ cells. B , 7,3′,4′-THIF

    Journal: The Journal of Biological Chemistry

    Article Title: 7,3?,4?-Trihydroxyisoflavone Inhibits Epidermal Growth Factor-induced Proliferation and Transformation of JB6 P+ Mouse Epidermal Cells by Suppressing Cyclin-dependent Kinases and Phosphatidylinositol 3-Kinase *

    doi: 10.1074/jbc.M109.094797

    Figure Lengend Snippet: Effect of 7,3′,4′-THIF on G 1 phase-related proteins in EGF-stimulated JB6 P+ cells. A , 7,3′,4′-THIF inhibits EGF-induced expression of cyclin D1, CDK4, cyclin E, and CDK2 in JB6 P+ cells. B , 7,3′,4′-THIF

    Article Snippet: Assays of cyclin D1-CDK4 and cyclin E-CDK2 kinase activity were performed in accordance with instructions provided by Millipore Corp.

    Techniques: Expressing

    Repeated low-dose NaAsO 2 exposure induced phosphorylated protein expression of GSK-3β/cyclinD1, p21 and p27 was regulated by AKT. Protein expression was detected by the Western blot analysis. (A) Images are the representative results of three separate experiments. Quantitative graphs ( n = 3) showed the relative intensity of the target proteins compare with β-actin, including p -AKT (B) , p -GSK-3β (C) , total cyclin D1 (D) , p -cyclin D1 (E) , p -p21 (F) , p -p27 (G) , total p21 (H) and total p27 (I) . NaAsO 2 exposure induced increased expression of p -AKT, p -GSK-3β, total cyclin D1, p -p21, and p -p27, but decreased expression of p -cyclin D1, total p21, and total p27. Treatment of MK2206 significantly reversed the expression of all of the above proteins. Significant difference was defined as p less than 0.05. a, vs. the corresponding 0 μM group; b, vs. the corresponding 0.05 μM group; c, vs. the MK2206(-) group of the same NaAsO 2 concentration.

    Journal: Frontiers in Pharmacology

    Article Title: Akt Regulated Phosphorylation of GSK-3β/Cyclin D1, p21 and p27 Contributes to Cell Proliferation Through Cell Cycle Progression From G1 to S/G2M Phase in Low-Dose Arsenite Exposed HaCat Cells

    doi: 10.3389/fphar.2019.01176

    Figure Lengend Snippet: Repeated low-dose NaAsO 2 exposure induced phosphorylated protein expression of GSK-3β/cyclinD1, p21 and p27 was regulated by AKT. Protein expression was detected by the Western blot analysis. (A) Images are the representative results of three separate experiments. Quantitative graphs ( n = 3) showed the relative intensity of the target proteins compare with β-actin, including p -AKT (B) , p -GSK-3β (C) , total cyclin D1 (D) , p -cyclin D1 (E) , p -p21 (F) , p -p27 (G) , total p21 (H) and total p27 (I) . NaAsO 2 exposure induced increased expression of p -AKT, p -GSK-3β, total cyclin D1, p -p21, and p -p27, but decreased expression of p -cyclin D1, total p21, and total p27. Treatment of MK2206 significantly reversed the expression of all of the above proteins. Significant difference was defined as p less than 0.05. a, vs. the corresponding 0 μM group; b, vs. the corresponding 0.05 μM group; c, vs. the MK2206(-) group of the same NaAsO 2 concentration.

    Article Snippet: Antibodies against p -Akt (Ser473, #9271), Akt (#4685S), GSK-3β (#5676), p -cyclin D1 (Thr286, #3300), p21 (#2947), p27 (#3686), and MMP9 (#13667) were purchased from Cell Signaling Technology, USA.

    Techniques: Expressing, Western Blot, Concentration Assay

    Sonic hedgehog signaling is activated in the Ptc2 tm1/tm1 epidermis. Shown is marker gene analysis by in situ hybridization (A to F) and immunohistochemistry (G to H). Ptc1 (A and B), Gli1 (C and D), Shh (E and F), and cyclin D1/D2 (G to H) expression is increased in areas of epidermal hyperplasia in affected Ptc2 tm1/tm1 skin. Arrowheads indicate low levels of Gli1 , Shh , and cyclin D1/D2 expression in hair follicles of wild-type skin. ep, epidermis; ul, ulcer. Scale bar: 50 μM.

    Journal: Molecular and Cellular Biology

    Article Title: Mice with a Targeted Mutation of Patched2 Are Viable but Develop Alopecia and Epidermal Hyperplasia †

    doi: 10.1128/MCB.00295-06

    Figure Lengend Snippet: Sonic hedgehog signaling is activated in the Ptc2 tm1/tm1 epidermis. Shown is marker gene analysis by in situ hybridization (A to F) and immunohistochemistry (G to H). Ptc1 (A and B), Gli1 (C and D), Shh (E and F), and cyclin D1/D2 (G to H) expression is increased in areas of epidermal hyperplasia in affected Ptc2 tm1/tm1 skin. Arrowheads indicate low levels of Gli1 , Shh , and cyclin D1/D2 expression in hair follicles of wild-type skin. ep, epidermis; ul, ulcer. Scale bar: 50 μM.

    Article Snippet: The following primary antibodies were used: keratin-5, keratin-14, keratin-10, loricrin (Covance), cyclin D1/D2, PCNA, phospho-histone H3 (Ser10) (Cell Signaling Technology), and GATA-3 (Santa Cruz).

    Techniques: Marker, In Situ Hybridization, Immunohistochemistry, Expressing

    mRNA and protein expression of p21, Cyclin D1 and PCNA in the buccal pouch tissues of experimental and control animals. (mean ± SD; n = 3). A. Transcript expression level of p21, cyclin D1 and PCNA in various experimental groups as determined by kinetic PCR. Data are the mean ± SD of three independent experiments. ♣ p

    Journal: PLoS ONE

    Article Title: Astaxanthin Inhibits JAK/STAT-3 Signaling to Abrogate Cell Proliferation, Invasion and Angiogenesis in a Hamster Model of Oral Cancer

    doi: 10.1371/journal.pone.0109114

    Figure Lengend Snippet: mRNA and protein expression of p21, Cyclin D1 and PCNA in the buccal pouch tissues of experimental and control animals. (mean ± SD; n = 3). A. Transcript expression level of p21, cyclin D1 and PCNA in various experimental groups as determined by kinetic PCR. Data are the mean ± SD of three independent experiments. ♣ p

    Article Snippet: Antibodies for IL-6, GAPDH, Cyclin D1, PCNA, p21, MMP-2, MMP-9, TIMP-2, RECK, VEGF, VEGFR2, HIF1α, were purchased from Santa Cruz Biotechnology, USA. pJAK-2tyr1007/1008 , JAK-2, pSTAT-3tyr705 , STAT-3 and histone (H2B) antibodies and BrdU, STAT-3tyr705 , total cyclin D1 and pVEGFR2tyr1175 ELISA kits were from Cell Signaling Technology, USA.

    Techniques: Expressing, Polymerase Chain Reaction

    Effect of glutathione S-transferase π (GSTP1) overexpression on upstream kinases and cyclin D1. The cell lysates from HepG2 cells treated with GSTP1 for 48 h were resolved on 10% sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), then immunoblotted with antibodies as indicated in Materials and methods. EGF, epidermal growth factor; p, phosphorylated: EGFR, EGF receptor.

    Journal: Oncology Letters

    Article Title: GSTP1 negatively regulates Stat3 activation in epidermal growth factor signaling

    doi: 10.3892/ol.2012.1098

    Figure Lengend Snippet: Effect of glutathione S-transferase π (GSTP1) overexpression on upstream kinases and cyclin D1. The cell lysates from HepG2 cells treated with GSTP1 for 48 h were resolved on 10% sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), then immunoblotted with antibodies as indicated in Materials and methods. EGF, epidermal growth factor; p, phosphorylated: EGFR, EGF receptor.

    Article Snippet: Antibodies and reagents The p-Stat3 (Y705), Stat3 and cyclin D1 antibodies were purchased from Cell Signaling Technology, Inc. (Beverly, MA, USA).

    Techniques: Over Expression, Polyacrylamide Gel Electrophoresis, SDS Page

    Tbx2 regulated expression of endogenous Ccnd1 . Knockdown of Tbx2 led to down‐regulation of Ccnd1 expression (a, b). (a) Relative fold change in mRNA levels of candidate proliferation‐related genes in melan‐a cell transfected with si‐Tbx2‐1 or si‐Tbx2‐2 compared to mock cells. Down‐regulation of Tbx2 caused reduction of several proliferation‐related genes, including Ccnd1 , Bcl9l , Cdca7 , Mphosph9, and Dna2 . (b) Western blot analysis of TBX2 and Cyclin D1 expression in melan‐a cell transfected with si‐C, si‐Tbx2‐1 or si‐Tbx2‐2. Note that knockdown of Tbx2 lead to reduction in levels of Cyclin D1, consistent with reduction in Tbx2 mRNA seen in (a). Intensity of bands was measured using ImageJ software and fold‐change compared to level seen in mock cells is indicated. (c) Immunolabelling for TBX2, Cyclin D1, and MITF in melan‐a cells showed that TBX2 and Cyclin D1 colocalized in nuclei of melan‐a cells. Bar = 20 μm. (d, e) Overexpression of TBX2 up‐regulated expression of Ccnd1 . Melan‐a cells were infected with the GFP or GFP‐TBX2 lentivirus, respectively, and cells were continually cultured for at least a week. (d) Relative fold‐change in mRNA levels of candidate proliferation‐related genes in melan‐a cells overexpressing TBX2. Results show that overexpression of TBX2 lead to up‐regulation of Ccnd1 . (e) Western blot analysis of TBX2 and Cyclin D1 expression in TBX2‐overexpressing melan‐a cells. Note that expression of Cyclin D1 increased after overexpression of Tbx2 . Intensity of bands was measured using ImageJ software and fold‐change was compared to expression in mock cells. Data for (a) and (d) are from triplicate experiments and are represented as mean ± SD. * P

    Journal: Cell Proliferation

    Article Title: Microphthalmia‐associated transcription factor/T‐box factor‐2 axis acts through Cyclin D1 to regulate melanocyte proliferation

    doi: 10.1111/cpr.12227

    Figure Lengend Snippet: Tbx2 regulated expression of endogenous Ccnd1 . Knockdown of Tbx2 led to down‐regulation of Ccnd1 expression (a, b). (a) Relative fold change in mRNA levels of candidate proliferation‐related genes in melan‐a cell transfected with si‐Tbx2‐1 or si‐Tbx2‐2 compared to mock cells. Down‐regulation of Tbx2 caused reduction of several proliferation‐related genes, including Ccnd1 , Bcl9l , Cdca7 , Mphosph9, and Dna2 . (b) Western blot analysis of TBX2 and Cyclin D1 expression in melan‐a cell transfected with si‐C, si‐Tbx2‐1 or si‐Tbx2‐2. Note that knockdown of Tbx2 lead to reduction in levels of Cyclin D1, consistent with reduction in Tbx2 mRNA seen in (a). Intensity of bands was measured using ImageJ software and fold‐change compared to level seen in mock cells is indicated. (c) Immunolabelling for TBX2, Cyclin D1, and MITF in melan‐a cells showed that TBX2 and Cyclin D1 colocalized in nuclei of melan‐a cells. Bar = 20 μm. (d, e) Overexpression of TBX2 up‐regulated expression of Ccnd1 . Melan‐a cells were infected with the GFP or GFP‐TBX2 lentivirus, respectively, and cells were continually cultured for at least a week. (d) Relative fold‐change in mRNA levels of candidate proliferation‐related genes in melan‐a cells overexpressing TBX2. Results show that overexpression of TBX2 lead to up‐regulation of Ccnd1 . (e) Western blot analysis of TBX2 and Cyclin D1 expression in TBX2‐overexpressing melan‐a cells. Note that expression of Cyclin D1 increased after overexpression of Tbx2 . Intensity of bands was measured using ImageJ software and fold‐change was compared to expression in mock cells. Data for (a) and (d) are from triplicate experiments and are represented as mean ± SD. * P

    Article Snippet: Cyclin D1 is of interest here as it has been shown to work as a G1‐phase cell cycle regulator by serving as a regulatory subunit of CDK4 or CDK6 .

    Techniques: Expressing, Transfection, Western Blot, Software, Over Expression, Infection, Cell Culture

    MiR-374b increases GIST-T1 cell cycle entry (A) Results of GIST cell apoptosis in each group by flow cytometry. (B) Expressions of P53 and cyclinD1 by RT-qPCR. (C) Protein levels of P53 and cyclinD1 by Western blotting; p

    Journal: Molecules and Cells

    Article Title: MiR-374b Promotes Proliferation and Inhibits Apoptosis of Human GIST Cells by Inhibiting PTEN through Activation of the PI3K/Akt Pathway

    doi: 10.14348/molcells.2018.2211

    Figure Lengend Snippet: MiR-374b increases GIST-T1 cell cycle entry (A) Results of GIST cell apoptosis in each group by flow cytometry. (B) Expressions of P53 and cyclinD1 by RT-qPCR. (C) Protein levels of P53 and cyclinD1 by Western blotting; p

    Article Snippet: Compared with the blank group and the NC group, the levels of P53 and cyclinD1 was increased in the miR-374b mimics and siRNA-PTEN groups (all p < 0.05), and the levels of P53 and cyclinD1 was decreased in the miR-374b inhibitors group (all p < 0.05).

    Techniques: Flow Cytometry, Cytometry, Quantitative RT-PCR, Western Blot

    qRT-PCR analysis of β-catenin target gene expression in c-Met/∆N90-β-catenin and c-Met/β-cateninS45Y mouse HCC samples. a qRT-PCR analysis of mRNA levels of pan-β-catenin target genes: AXIN2, LGR5, c-Myc and cyclin D1. b qRT-PCR analysis of mRNA levels of liver specific β-catenin target genes: GS, TBX3, OAT, and LECT2. Student’s t-test: * P

    Journal: BMC Cancer

    Article Title: Oncogenic potential of N-terminal deletion and S45Y mutant β-catenin in promoting hepatocellular carcinoma development in mice

    doi: 10.1186/s12885-018-4870-z

    Figure Lengend Snippet: qRT-PCR analysis of β-catenin target gene expression in c-Met/∆N90-β-catenin and c-Met/β-cateninS45Y mouse HCC samples. a qRT-PCR analysis of mRNA levels of pan-β-catenin target genes: AXIN2, LGR5, c-Myc and cyclin D1. b qRT-PCR analysis of mRNA levels of liver specific β-catenin target genes: GS, TBX3, OAT, and LECT2. Student’s t-test: * P

    Article Snippet: Cyclin D1

    Techniques: Quantitative RT-PCR, Expressing

    Biochemical analysis of HCC lesions of c-Met/β-cateninS45Y c-Met/∆N90-β-catenin mice. Western blot analysis of c-Met, p-Met, β-catenin, Myc tag, p-β-catenin (S45), p-β-catenin (S33/S37/T41), p-β-catenin (S675), p-β-catenin (S552), GS, and cyclin D1 in normal liver as well as HCC lesions from c-Met/β-cateninS45Y c-Met/∆N90-β-catenin mice. GAPDH were used as a loading control. Please note the presence of two bands for the β-catenin protein. The upper band represents endogenous β-catenin protein or β-cateninS45Y protein. The lower band represents ectopically injected ∆N90-β-catenin protein

    Journal: BMC Cancer

    Article Title: Oncogenic potential of N-terminal deletion and S45Y mutant β-catenin in promoting hepatocellular carcinoma development in mice

    doi: 10.1186/s12885-018-4870-z

    Figure Lengend Snippet: Biochemical analysis of HCC lesions of c-Met/β-cateninS45Y c-Met/∆N90-β-catenin mice. Western blot analysis of c-Met, p-Met, β-catenin, Myc tag, p-β-catenin (S45), p-β-catenin (S33/S37/T41), p-β-catenin (S675), p-β-catenin (S552), GS, and cyclin D1 in normal liver as well as HCC lesions from c-Met/β-cateninS45Y c-Met/∆N90-β-catenin mice. GAPDH were used as a loading control. Please note the presence of two bands for the β-catenin protein. The upper band represents endogenous β-catenin protein or β-cateninS45Y protein. The lower band represents ectopically injected ∆N90-β-catenin protein

    Article Snippet: Cyclin D1

    Techniques: Mouse Assay, Western Blot, Injection

    Vitamin D 3 -dependent VDR signaling reduces β-catenin transcriptional activity A. Western analysis demonstrating a dose-dependent reduction in active β-catenin (ABC) levels in R7 cells treated with the designated concentrations of 1,25D 3 for 48 hours, but no change in total β-catenin. B. qRT-PCR analysis of β-catenin target genes cyclin D1, TCF-7, VEGF, and MMP7 in R7 cells treated with the designated concentrations of 1,25D 3 for 72 hours. Data represent mean values from three independent experiments ± SE. C. Dual luciferase assays in R7 cells co-transfected with Topflash and pRLTX (expressing Renilla ) plasmids for 48 hours, then treated with the designated concentrations of 1,25D 3 for 24 hours. Luciferase activities were normalized for transfection efficiency to Renilla activity. Data represent mean values from three independent experiments ± SE. D. Crystal violet staining of R7 cells transfected with a stabilized form of β-catenin (ΔN) or empty vector and treated with 100 nM 1,25D 3 or vehicle control (EtOH). Data represent mean values from four independent experiments ± SE. * P

    Journal: Oncotarget

    Article Title: Vitamin D3-dependent VDR signaling delays ron-mediated breast tumorigenesis through suppression of β-catenin activity

    doi:

    Figure Lengend Snippet: Vitamin D 3 -dependent VDR signaling reduces β-catenin transcriptional activity A. Western analysis demonstrating a dose-dependent reduction in active β-catenin (ABC) levels in R7 cells treated with the designated concentrations of 1,25D 3 for 48 hours, but no change in total β-catenin. B. qRT-PCR analysis of β-catenin target genes cyclin D1, TCF-7, VEGF, and MMP7 in R7 cells treated with the designated concentrations of 1,25D 3 for 72 hours. Data represent mean values from three independent experiments ± SE. C. Dual luciferase assays in R7 cells co-transfected with Topflash and pRLTX (expressing Renilla ) plasmids for 48 hours, then treated with the designated concentrations of 1,25D 3 for 24 hours. Luciferase activities were normalized for transfection efficiency to Renilla activity. Data represent mean values from three independent experiments ± SE. D. Crystal violet staining of R7 cells transfected with a stabilized form of β-catenin (ΔN) or empty vector and treated with 100 nM 1,25D 3 or vehicle control (EtOH). Data represent mean values from four independent experiments ± SE. * P

    Article Snippet: Between four and eight experimental cDNA samples were analyzed for VDR, Ron, β-catenin, cyclin D1, c-Myc, MMP7, TCF-7, VEGF, and DKK-1 mRNA expression in duplicate by real time PCR analysis using FastStart SYBR Green Master (Roche Diagnostics, Indianapolis, IN).

    Techniques: Activity Assay, Western Blot, Quantitative RT-PCR, Luciferase, Transfection, Expressing, Staining, Plasmid Preparation

    Enhanced downstream β-catenin signaling in Ron-mediated mammary tumorigenesis with VDR ablation A. Representative immunohistochemical staining for β-catenin in MMTV-Ron VDR+/+ and VDR−/− mammary glands from 4 month-old mice demonstrating enhanced expression in the absence of VDR ( n = 6 per genotype). B. qRT-PCR mRNA expression of β-catenin target genes Cyclin D1, c-Myc, TCF-7, VEGF, and MMP7 in mammary tumors from 8 month-old MMTV-Ron VDR+/+ and VDR−/− mice. Data represent mean values from three independent experiments ± SE. C. Western analysis demonstrating enhanced expression of active β-catenin (ABC) levels in two representative MMTV-Ron VDR−/− tumor lysates compared to two MMTV-Ron VDR+/+ tumors that correlates with increased expression of β-catenin target genes cyclin D1 and c-Myc. * P

    Journal: Oncotarget

    Article Title: Vitamin D3-dependent VDR signaling delays ron-mediated breast tumorigenesis through suppression of β-catenin activity

    doi:

    Figure Lengend Snippet: Enhanced downstream β-catenin signaling in Ron-mediated mammary tumorigenesis with VDR ablation A. Representative immunohistochemical staining for β-catenin in MMTV-Ron VDR+/+ and VDR−/− mammary glands from 4 month-old mice demonstrating enhanced expression in the absence of VDR ( n = 6 per genotype). B. qRT-PCR mRNA expression of β-catenin target genes Cyclin D1, c-Myc, TCF-7, VEGF, and MMP7 in mammary tumors from 8 month-old MMTV-Ron VDR+/+ and VDR−/− mice. Data represent mean values from three independent experiments ± SE. C. Western analysis demonstrating enhanced expression of active β-catenin (ABC) levels in two representative MMTV-Ron VDR−/− tumor lysates compared to two MMTV-Ron VDR+/+ tumors that correlates with increased expression of β-catenin target genes cyclin D1 and c-Myc. * P

    Article Snippet: Between four and eight experimental cDNA samples were analyzed for VDR, Ron, β-catenin, cyclin D1, c-Myc, MMP7, TCF-7, VEGF, and DKK-1 mRNA expression in duplicate by real time PCR analysis using FastStart SYBR Green Master (Roche Diagnostics, Indianapolis, IN).

    Techniques: Immunohistochemistry, Staining, Mouse Assay, Expressing, Quantitative RT-PCR, Western Blot

    Vitamin D 3 -dependent VDR signaling induces DKK-1 expression and binds to β-catenin to disrupt interaction at consensus sequences within promoters of TCF/LEF target genes A. qRT-PCR mRNA expression of DKK-1 in R7 cells treated with the designated concentrations of 1,25D 3 for 72 hours. Data represent mean values from three independent experiments ± SE. B. qRT-PCR mRNA expression of DKK-1 in tumors and mammary glands (MG) from 8 month-old MMTV-Ron VDR+/+ and VDR−/− mice demonstrating a reduction in DKK-1 levels in tumors with loss of VDR. Data represent mean values from three independent experiments ± SE. C. Western blot demonstrating loss of DKK-1 protein expression with siRNA-mediated silencing in R7 cells. D. R7 cells transfected with siRNA against DKK-1 were treated with the designated concentrations of 1,25D 3 for 72 hours and cell viability/number was determined by crystal violet assays. Data are normalized to the respective vehicle treated cells set at 1 and represent mean values from two independent experiments performed in quadruplicate ± SE. E. Chromatin immunoprecipitation (ChIP) assays with a mouse IgG isotype control and an anti-active β-catenin (ABC) antibody. ChIP-ABC quantitative real time PCR (qRT-PCR) analysis of R7 cells treated with 100 nM 1,25D 3 for 72 hours. The graph shows qRT-PCR on DNA purified from ChIP-ABC, using primers designed to the LEF-1 binding sequence within the mouse cyclin D1 promoter and relative to the respective input controls. Vitamin D 3 treatment significantly reduces enrichment compared to the vehicle control (EtOH). Data represent mean values from three independent experiments ± SE. F. Representative agarose gel from ChIP-ABC PCR showing reduced cyclin D1 promoter enrichment with vitamin D 3 treatment in R7 cells. Negative control primers designed to a site 4000 bp upstream of the LEF-1 binding sequence within the cyclin D1 promoter (Off-Target) verify specificity of cyclin D1 primers to the sheared DNA product. G. Densitometry analysis of PCR products from three separate ChIP-ABC experiments supporting loss of ABC interaction with the cyclin D1 promoter. Error bars represent SE. H. Re-ChIP qRT-PCR analysis of R7 cells treated with 100 nM 1,25D 3 for 72 hours and sequentially immunoprecipitated with anti-ABC then anti-VDR antibodies. The graph shows qRT-PCR of DNA purified from ChIP-ABC-VDR, using primers designed to the LEF-1 binding sequence within the mouse cyclin D1 promoter, and showing less interaction of the ABC-VDR complex at the cyclin D1 promoter. Data represent the relative mean CT values from two experiments ± standard deviation. * P

    Journal: Oncotarget

    Article Title: Vitamin D3-dependent VDR signaling delays ron-mediated breast tumorigenesis through suppression of β-catenin activity

    doi:

    Figure Lengend Snippet: Vitamin D 3 -dependent VDR signaling induces DKK-1 expression and binds to β-catenin to disrupt interaction at consensus sequences within promoters of TCF/LEF target genes A. qRT-PCR mRNA expression of DKK-1 in R7 cells treated with the designated concentrations of 1,25D 3 for 72 hours. Data represent mean values from three independent experiments ± SE. B. qRT-PCR mRNA expression of DKK-1 in tumors and mammary glands (MG) from 8 month-old MMTV-Ron VDR+/+ and VDR−/− mice demonstrating a reduction in DKK-1 levels in tumors with loss of VDR. Data represent mean values from three independent experiments ± SE. C. Western blot demonstrating loss of DKK-1 protein expression with siRNA-mediated silencing in R7 cells. D. R7 cells transfected with siRNA against DKK-1 were treated with the designated concentrations of 1,25D 3 for 72 hours and cell viability/number was determined by crystal violet assays. Data are normalized to the respective vehicle treated cells set at 1 and represent mean values from two independent experiments performed in quadruplicate ± SE. E. Chromatin immunoprecipitation (ChIP) assays with a mouse IgG isotype control and an anti-active β-catenin (ABC) antibody. ChIP-ABC quantitative real time PCR (qRT-PCR) analysis of R7 cells treated with 100 nM 1,25D 3 for 72 hours. The graph shows qRT-PCR on DNA purified from ChIP-ABC, using primers designed to the LEF-1 binding sequence within the mouse cyclin D1 promoter and relative to the respective input controls. Vitamin D 3 treatment significantly reduces enrichment compared to the vehicle control (EtOH). Data represent mean values from three independent experiments ± SE. F. Representative agarose gel from ChIP-ABC PCR showing reduced cyclin D1 promoter enrichment with vitamin D 3 treatment in R7 cells. Negative control primers designed to a site 4000 bp upstream of the LEF-1 binding sequence within the cyclin D1 promoter (Off-Target) verify specificity of cyclin D1 primers to the sheared DNA product. G. Densitometry analysis of PCR products from three separate ChIP-ABC experiments supporting loss of ABC interaction with the cyclin D1 promoter. Error bars represent SE. H. Re-ChIP qRT-PCR analysis of R7 cells treated with 100 nM 1,25D 3 for 72 hours and sequentially immunoprecipitated with anti-ABC then anti-VDR antibodies. The graph shows qRT-PCR of DNA purified from ChIP-ABC-VDR, using primers designed to the LEF-1 binding sequence within the mouse cyclin D1 promoter, and showing less interaction of the ABC-VDR complex at the cyclin D1 promoter. Data represent the relative mean CT values from two experiments ± standard deviation. * P

    Article Snippet: Between four and eight experimental cDNA samples were analyzed for VDR, Ron, β-catenin, cyclin D1, c-Myc, MMP7, TCF-7, VEGF, and DKK-1 mRNA expression in duplicate by real time PCR analysis using FastStart SYBR Green Master (Roche Diagnostics, Indianapolis, IN).

    Techniques: Expressing, Quantitative RT-PCR, Mouse Assay, Western Blot, Transfection, Chromatin Immunoprecipitation, Real-time Polymerase Chain Reaction, Purification, Binding Assay, Sequencing, Agarose Gel Electrophoresis, Polymerase Chain Reaction, Negative Control, Immunoprecipitation, Standard Deviation

    Canonical miR-34a growth control targets are poorly expressed in LCLs relative to HCT-116 cells. (a) Relative mRNA levels as determined by qRT-PCR of cyclin D1, D2, and E2; cdk4; cdk6; and c-Met in LCLs and HCT-116 cells. The asterisk indicates a value below the threshold for detection. (b) Western analysis of miR-34a targets in HCT-116 cells and EF3D LCLs expressing pcDNA3 vector (−) or pCDNA3-miR-34a (+). Quantitation of protein expression is noted below each band.

    Journal: Journal of Virology

    Article Title: The Epstein-Barr Virus (EBV)-Induced Tumor Suppressor MicroRNA MiR-34a Is Growth Promoting in EBV-Infected B Cells

    doi: 10.1128/JVI.07056-11

    Figure Lengend Snippet: Canonical miR-34a growth control targets are poorly expressed in LCLs relative to HCT-116 cells. (a) Relative mRNA levels as determined by qRT-PCR of cyclin D1, D2, and E2; cdk4; cdk6; and c-Met in LCLs and HCT-116 cells. The asterisk indicates a value below the threshold for detection. (b) Western analysis of miR-34a targets in HCT-116 cells and EF3D LCLs expressing pcDNA3 vector (−) or pCDNA3-miR-34a (+). Quantitation of protein expression is noted below each band.

    Article Snippet: In contrast, HCT-116 cells expressed higher levels of cyclin D1 and E2 than LCLs.

    Techniques: Quantitative RT-PCR, Western Blot, Expressing, Plasmid Preparation, Quantitation Assay

    SNHG20 knockdown regulated several genes related to proliferation and metastasis ( A , B ) The mRNA level of P21, Cyclin D1, Vimentin, and E-cadherin was detected by qRT-PCR in A2780 and CAOV-3 cells transfecting with si-SNHG20-1 or -2 (* P

    Journal: Bioscience Reports

    Article Title: LncRNA SNHG20 predicts a poor prognosis and promotes cell progression in epithelial ovarian cancer

    doi: 10.1042/BSR20182186

    Figure Lengend Snippet: SNHG20 knockdown regulated several genes related to proliferation and metastasis ( A , B ) The mRNA level of P21, Cyclin D1, Vimentin, and E-cadherin was detected by qRT-PCR in A2780 and CAOV-3 cells transfecting with si-SNHG20-1 or -2 (* P

    Article Snippet: As shown in A,B, we found that the mRNAs of P21 and E-cadherin were significantly increased, while Cyclin D1 and Vimentin were down-regulated at post-transfection with SNHG20 siRNA-1 and -2.

    Techniques: Quantitative RT-PCR

    Cyclin D1 strong positive expression in invasive ductal carcinoma of no special type (× 100)

    Journal: Indian Journal of Surgical Oncology

    Article Title: Prognostic Utility of Cyclin D1 in Invasive Breast Carcinoma

    doi: 10.1007/s13193-018-0839-2

    Figure Lengend Snippet: Cyclin D1 strong positive expression in invasive ductal carcinoma of no special type (× 100)

    Article Snippet: Four-micron sections were prepared from each formalin-fixed and paraffin-embedded tissue sample and stained with antibody against ER (monoclonal mouse anti-human; Clone: 1D5; Dako), PgR (monoclonal mouse anti-human; Clone PgR 636, Dako), HER2 (polyclonal rabbit antihuman antibody against c-erbB-2 oncoprotein, Dako) and against cyclin D1 (monoclonal Rabbit Anti-Human, Clone EP12, Dako).

    Techniques: Expressing

    Cyclin D1 strong positive expression in invasive ductal carcinoma of no special type (× 400)

    Journal: Indian Journal of Surgical Oncology

    Article Title: Prognostic Utility of Cyclin D1 in Invasive Breast Carcinoma

    doi: 10.1007/s13193-018-0839-2

    Figure Lengend Snippet: Cyclin D1 strong positive expression in invasive ductal carcinoma of no special type (× 400)

    Article Snippet: Four-micron sections were prepared from each formalin-fixed and paraffin-embedded tissue sample and stained with antibody against ER (monoclonal mouse anti-human; Clone: 1D5; Dako), PgR (monoclonal mouse anti-human; Clone PgR 636, Dako), HER2 (polyclonal rabbit antihuman antibody against c-erbB-2 oncoprotein, Dako) and against cyclin D1 (monoclonal Rabbit Anti-Human, Clone EP12, Dako).

    Techniques: Expressing

    Cyclin D1 strong positive expression in mucinous carcinoma (× 400)

    Journal: Indian Journal of Surgical Oncology

    Article Title: Prognostic Utility of Cyclin D1 in Invasive Breast Carcinoma

    doi: 10.1007/s13193-018-0839-2

    Figure Lengend Snippet: Cyclin D1 strong positive expression in mucinous carcinoma (× 400)

    Article Snippet: Four-micron sections were prepared from each formalin-fixed and paraffin-embedded tissue sample and stained with antibody against ER (monoclonal mouse anti-human; Clone: 1D5; Dako), PgR (monoclonal mouse anti-human; Clone PgR 636, Dako), HER2 (polyclonal rabbit antihuman antibody against c-erbB-2 oncoprotein, Dako) and against cyclin D1 (monoclonal Rabbit Anti-Human, Clone EP12, Dako).

    Techniques: Expressing

    Pim-1 depletion altered the RUNX3, Cyclin D1 and CDK4 levels. A . Western blot analysis showed the expression of RUNX3 protein in SACC cells after Pim-1 siRNA transfection. The expression of GAPDH was used as a loading control. B . Western blot analysis showed the expression Cyclin D1 and CDK4 protein in SACC cells after Pim-1 siRNA transfection. The expression of β-actin was used as a loading control.

    Journal: Journal of Experimental & Clinical Cancer Research : CR

    Article Title: Pim-1 acts as an oncogene in human salivary gland adenoid cystic carcinoma

    doi: 10.1186/s13046-014-0114-5

    Figure Lengend Snippet: Pim-1 depletion altered the RUNX3, Cyclin D1 and CDK4 levels. A . Western blot analysis showed the expression of RUNX3 protein in SACC cells after Pim-1 siRNA transfection. The expression of GAPDH was used as a loading control. B . Western blot analysis showed the expression Cyclin D1 and CDK4 protein in SACC cells after Pim-1 siRNA transfection. The expression of β-actin was used as a loading control.

    Article Snippet: Cyclin D1 and CDK4 work together to form the complex and to promote G1 phase progression and regulate the cell cycle G1/S transition [ ].

    Techniques: Western Blot, Expressing, Transfection

    GCN5 directly binds to the cyclin E1, cyclin D1, and E2F1 promoters, increasing histone H3 and H4 acetylation levels within these regions. A, cyclin E1, cyclin D1, and E2F1 luciferase reporter assay performed in HEK293T cells. Empty control vector and

    Journal: The Journal of Biological Chemistry

    Article Title: Lysine Acetyltransferase GCN5 Potentiates the Growth of Non-small Cell Lung Cancer via Promotion of E2F1, Cyclin D1, and Cyclin E1 Expression *

    doi: 10.1074/jbc.M113.458737

    Figure Lengend Snippet: GCN5 directly binds to the cyclin E1, cyclin D1, and E2F1 promoters, increasing histone H3 and H4 acetylation levels within these regions. A, cyclin E1, cyclin D1, and E2F1 luciferase reporter assay performed in HEK293T cells. Empty control vector and

    Article Snippet: To test this possibility, luciferase reporters driven by the promoter regions from cyclin D1 (Addgene 32726), cyclin E1 (Addgene 8458), or E2F1 (Addgene 20950) ( – ) were used to evaluate the effect of GCN5 on the promoter activity of these genes.

    Techniques: Luciferase, Reporter Assay, Plasmid Preparation

    GCN5 increases both mRNA and protein levels of cyclin D1, cyclin E1, and E2F1 . A and B, Western blotting analysis of the protein levels of cell cycle regulators in GCN5-knockdown A549 cells, or GCN5-overexpressing A549 cells and control cell lines. GAPDH

    Journal: The Journal of Biological Chemistry

    Article Title: Lysine Acetyltransferase GCN5 Potentiates the Growth of Non-small Cell Lung Cancer via Promotion of E2F1, Cyclin D1, and Cyclin E1 Expression *

    doi: 10.1074/jbc.M113.458737

    Figure Lengend Snippet: GCN5 increases both mRNA and protein levels of cyclin D1, cyclin E1, and E2F1 . A and B, Western blotting analysis of the protein levels of cell cycle regulators in GCN5-knockdown A549 cells, or GCN5-overexpressing A549 cells and control cell lines. GAPDH

    Article Snippet: To test this possibility, luciferase reporters driven by the promoter regions from cyclin D1 (Addgene 32726), cyclin E1 (Addgene 8458), or E2F1 (Addgene 20950) ( – ) were used to evaluate the effect of GCN5 on the promoter activity of these genes.

    Techniques: Western Blot

    Effects of PKF 115–584 on Cyclin D1 expression. A, B : Cyclin D1 mRNA expression in non-treated endometrial epithelial (A) and stromal (B) cells of patients with and without endometriosis. Endo (+) (M: n = 6, P: n = 20, ES: n = 7, MS: n = 15, LS: n = 6). Endo (–) (M: n = 4, P: n = 11; ES: n = 8, MS: n = 8; LS: n = 4). C, D : Cyclin D1 mRNA expression in PKF 115–584–treated endometrial epithelial (C) and stromal (D) cells of patients with and without endometriosis. Endo (+):(M: n = 6, P: n = 20, ES: n = 7, MS: n = 15, LS: n = 6). Endo (–):(M: n = 4, P: n = 11, ES: n = 8, MS: n = 8, LS: n = 4). E : Cyclin D1 protein expression in non-treated and PKF 115–584–treated endometrial epithelial cells from the mid-secretory and menstrual phases. Endo (+):(M: n = 4, MS: n = 5). Endo (–):(M: n = 4, MS: n = 5). F : Representative photomicrographs of western blot analysis in non-treated and PKF 115–584–treated endometrial epithelial from the mid-secretory phase. Numerical values are presented as the mean+SEM. Expression levels of Cyclin D1 mRNA are given relative to the expression levels of the reference gene, GAPDH. Relative density is density of Cyclin D1 relative to that of Actin. M: menstrual phase, P: proliferative phase, ES: early secretory phase, MS: mid- secretory phase, LS: late secretory phase. a: p

    Journal: PLoS ONE

    Article Title: In Vitro Effects of a Small-Molecule Antagonist of the Tcf/ss-Catenin Complex on Endometrial and Endometriotic Cells of Patients with Endometriosis

    doi: 10.1371/journal.pone.0061690

    Figure Lengend Snippet: Effects of PKF 115–584 on Cyclin D1 expression. A, B : Cyclin D1 mRNA expression in non-treated endometrial epithelial (A) and stromal (B) cells of patients with and without endometriosis. Endo (+) (M: n = 6, P: n = 20, ES: n = 7, MS: n = 15, LS: n = 6). Endo (–) (M: n = 4, P: n = 11; ES: n = 8, MS: n = 8; LS: n = 4). C, D : Cyclin D1 mRNA expression in PKF 115–584–treated endometrial epithelial (C) and stromal (D) cells of patients with and without endometriosis. Endo (+):(M: n = 6, P: n = 20, ES: n = 7, MS: n = 15, LS: n = 6). Endo (–):(M: n = 4, P: n = 11, ES: n = 8, MS: n = 8, LS: n = 4). E : Cyclin D1 protein expression in non-treated and PKF 115–584–treated endometrial epithelial cells from the mid-secretory and menstrual phases. Endo (+):(M: n = 4, MS: n = 5). Endo (–):(M: n = 4, MS: n = 5). F : Representative photomicrographs of western blot analysis in non-treated and PKF 115–584–treated endometrial epithelial from the mid-secretory phase. Numerical values are presented as the mean+SEM. Expression levels of Cyclin D1 mRNA are given relative to the expression levels of the reference gene, GAPDH. Relative density is density of Cyclin D1 relative to that of Actin. M: menstrual phase, P: proliferative phase, ES: early secretory phase, MS: mid- secretory phase, LS: late secretory phase. a: p

    Article Snippet: In addition, Cyclin D1 and Survivin might not be essential for the regulation of endometriotic cell proliferation.

    Techniques: Expressing, Mass Spectrometry, Western Blot

    Effects of PKF 115–584 on Cyclin D1 expression. A, B : Cyclin D1 mRNA expression in non-treated epithelial (A) and stromal (B) cells of endometriotic tissue and matched eutopic endometrium of the same patients. C, D : Cyclin D1 mRNA expression in PKF 115–584–treated epithelial (C) and stromal (D) cells of endometriotic tissue and matched eutopic endometrium of the same patients. Numerical values are presented as the mean+SEM. Expression levels of Cyclin D1 mRNA are given relative to the expression levels of the reference gene, GAPDH. P: proliferative phase, S: secretory phase. DE: deep infiltrating endometriosis (epithelial cells: P: n = 6, S: n = 6, stromal cells: P: n = 6, S: n = 6). OE: ovarian endometriosis (epithelial cells: P: n = 6, S: n = 6; stromal cells: P: n = 6, S: n = 6). SE: superficial peritoneal endometriosis (epithelial cells: P: n = 4, S: n = 4; stromal cells: P: n = 4, S: n = 4). a: p

    Journal: PLoS ONE

    Article Title: In Vitro Effects of a Small-Molecule Antagonist of the Tcf/ss-Catenin Complex on Endometrial and Endometriotic Cells of Patients with Endometriosis

    doi: 10.1371/journal.pone.0061690

    Figure Lengend Snippet: Effects of PKF 115–584 on Cyclin D1 expression. A, B : Cyclin D1 mRNA expression in non-treated epithelial (A) and stromal (B) cells of endometriotic tissue and matched eutopic endometrium of the same patients. C, D : Cyclin D1 mRNA expression in PKF 115–584–treated epithelial (C) and stromal (D) cells of endometriotic tissue and matched eutopic endometrium of the same patients. Numerical values are presented as the mean+SEM. Expression levels of Cyclin D1 mRNA are given relative to the expression levels of the reference gene, GAPDH. P: proliferative phase, S: secretory phase. DE: deep infiltrating endometriosis (epithelial cells: P: n = 6, S: n = 6, stromal cells: P: n = 6, S: n = 6). OE: ovarian endometriosis (epithelial cells: P: n = 6, S: n = 6; stromal cells: P: n = 6, S: n = 6). SE: superficial peritoneal endometriosis (epithelial cells: P: n = 4, S: n = 4; stromal cells: P: n = 4, S: n = 4). a: p

    Article Snippet: In addition, Cyclin D1 and Survivin might not be essential for the regulation of endometriotic cell proliferation.

    Techniques: Expressing

    Effect of lovastatin and docetaxel on expression of genes involved in the initiation and progression of mitosis, cytokinesis, and MAP kinases signalling pathway. HGT-1 cells were treated with 12.5 μ lovastatin (L12.5) or with 5 or 10 n docetaxel (D5 or D10) alone or in combination for 48 h. Cyclin D1, cyclin B1, aurora kinase A ( A ), aurora kinase B and survivin ( B ) mRNA levels were analysed by real-time RT–PCR. Relative mRNA levels were normalised to P0 mRNA levels. Values are means±s.d. ( n =4). * Compared with control, #compared with docetaxel treatment, † compared with lovastatin treatment. One symbol: P

    Journal: British Journal of Cancer

    Article Title: The association of statins and taxanes: an efficient combination trigger of cancer cell apoptosis

    doi: 10.1038/bjc.2012.6

    Figure Lengend Snippet: Effect of lovastatin and docetaxel on expression of genes involved in the initiation and progression of mitosis, cytokinesis, and MAP kinases signalling pathway. HGT-1 cells were treated with 12.5 μ lovastatin (L12.5) or with 5 or 10 n docetaxel (D5 or D10) alone or in combination for 48 h. Cyclin D1, cyclin B1, aurora kinase A ( A ), aurora kinase B and survivin ( B ) mRNA levels were analysed by real-time RT–PCR. Relative mRNA levels were normalised to P0 mRNA levels. Values are means±s.d. ( n =4). * Compared with control, #compared with docetaxel treatment, † compared with lovastatin treatment. One symbol: P

    Article Snippet: Lovastatin reduced strongly (aurora kinases, Mcl-1) or more weakly (cyclin D1, Bax), or induced (p21) protein levels similarly in HGT-1 and HGT-1-D5 cells.

    Techniques: Expressing, Quantitative RT-PCR

    LMP1 increased the binding ability of transcription factors EGFR and STAT3 to cyclin D1 promoter in vitro . (A) STAT3 binding activities within the cyclin D1 promoter were examined by EMSA. A biotin-labeled wild-type STAT3 oligonucleotide probe was incubated with nuclear extracts of CNE1 and CNE1-LMP1 cells in the presence of a 200-fold excess of unlabeled wild-type STAT3 (lane 4), unlabeled mutant STAT3 oligonucleotides (lane 5), or noncompetitive unlabeled NF-κB oligonucleotide (NS, lane 6). Biotin-labeled mutant STAT3 oligonucleotide probe was incubated with nuclear extracts of the indicated NPC cell lines (lanes 8–9). (B) Ten micrograms of nuclear extracts were pre-incubated with biotin-labeled STAT3 oligonucleotide probe in the presence of inhibitors directed against different phosphorylation sites of STAT3 (indicated above each lane). (C) The biotin-labeled wild-type EGFR oligonucleotide probe was incubated with nuclear extracts of CNE1 and CNE1-LMP1 cells in the presence of a 200-fold excess of unlabeled wild-type EGFR (lane 4), unlabeled mutant EGFR oligonucleotides (lane 6) or noncompetitive unlabeled NFκB oligonucleotide (NS, lane 7), and then EGFR DNA binding activities were examined by EMSA. (D-E) The nuclear extracts of CNE1 and CNE1-LMP1 cells were pre-incubated with biotin-labeled EGFR oligonucleotide probe in the presence of inhibitors AG1478, directed against phosphorylation of EGFR, or DNAzyme 1 (DZ1), targeting LMP1. RD: relative density.

    Journal: Journal of Experimental & Clinical Cancer Research : CR

    Article Title: Epstein-Barr Virus encoded LMP1 regulates cyclin D1 promoter activity by nuclear EGFR and STAT3 in CNE1 cells

    doi: 10.1186/1756-9966-32-90

    Figure Lengend Snippet: LMP1 increased the binding ability of transcription factors EGFR and STAT3 to cyclin D1 promoter in vitro . (A) STAT3 binding activities within the cyclin D1 promoter were examined by EMSA. A biotin-labeled wild-type STAT3 oligonucleotide probe was incubated with nuclear extracts of CNE1 and CNE1-LMP1 cells in the presence of a 200-fold excess of unlabeled wild-type STAT3 (lane 4), unlabeled mutant STAT3 oligonucleotides (lane 5), or noncompetitive unlabeled NF-κB oligonucleotide (NS, lane 6). Biotin-labeled mutant STAT3 oligonucleotide probe was incubated with nuclear extracts of the indicated NPC cell lines (lanes 8–9). (B) Ten micrograms of nuclear extracts were pre-incubated with biotin-labeled STAT3 oligonucleotide probe in the presence of inhibitors directed against different phosphorylation sites of STAT3 (indicated above each lane). (C) The biotin-labeled wild-type EGFR oligonucleotide probe was incubated with nuclear extracts of CNE1 and CNE1-LMP1 cells in the presence of a 200-fold excess of unlabeled wild-type EGFR (lane 4), unlabeled mutant EGFR oligonucleotides (lane 6) or noncompetitive unlabeled NFκB oligonucleotide (NS, lane 7), and then EGFR DNA binding activities were examined by EMSA. (D-E) The nuclear extracts of CNE1 and CNE1-LMP1 cells were pre-incubated with biotin-labeled EGFR oligonucleotide probe in the presence of inhibitors AG1478, directed against phosphorylation of EGFR, or DNAzyme 1 (DZ1), targeting LMP1. RD: relative density.

    Article Snippet: We provide the evidence showing cyclin D1 might be modulated by STAT3 induced by EBV LMP1, illustrating the importance of the JAK/STAT signaling pathway on EBV LMP1 induced cyclin D1 transcription and expression.

    Techniques: Binding Assay, In Vitro, Labeling, Incubation, Mutagenesis

    Identification of an EGFR and STAT3 response element in the cyclin D1 promoter. (A) Schematic diagram of mutant cyclin D1 promoter constructs are shown. The expansion for EGFR and STAT3 binding site illustrates the wild-type sequence and frames the nucleotides replaced by mutations. (B-C) Dual luciferase-reporter assays were performed in LMP1-negative and LMP-positive CNE1 cells after co-transfection of a wild type or mutant cyclin D1 promoter-reporter construct, plasmids expressing wild-type EGFR or STAT3, and a Renilla luciferase transfection control plasmid. The fold induction by EGFR and STAT3 is displayed as the ratio of promoter activity obtained with wild-type compared to the DNA-binding mutant. (mean ± SD, n = 3, * p

    Journal: Journal of Experimental & Clinical Cancer Research : CR

    Article Title: Epstein-Barr Virus encoded LMP1 regulates cyclin D1 promoter activity by nuclear EGFR and STAT3 in CNE1 cells

    doi: 10.1186/1756-9966-32-90

    Figure Lengend Snippet: Identification of an EGFR and STAT3 response element in the cyclin D1 promoter. (A) Schematic diagram of mutant cyclin D1 promoter constructs are shown. The expansion for EGFR and STAT3 binding site illustrates the wild-type sequence and frames the nucleotides replaced by mutations. (B-C) Dual luciferase-reporter assays were performed in LMP1-negative and LMP-positive CNE1 cells after co-transfection of a wild type or mutant cyclin D1 promoter-reporter construct, plasmids expressing wild-type EGFR or STAT3, and a Renilla luciferase transfection control plasmid. The fold induction by EGFR and STAT3 is displayed as the ratio of promoter activity obtained with wild-type compared to the DNA-binding mutant. (mean ± SD, n = 3, * p

    Article Snippet: We provide the evidence showing cyclin D1 might be modulated by STAT3 induced by EBV LMP1, illustrating the importance of the JAK/STAT signaling pathway on EBV LMP1 induced cyclin D1 transcription and expression.

    Techniques: Mutagenesis, Construct, Binding Assay, Sequencing, Luciferase, Cotransfection, Expressing, Transfection, Plasmid Preparation, Activity Assay

    Inhibitors and dominant negative mutants targeting the EGFR and STAT3 pathways attenuated LMP1-augmented cyclin D1 promoter activity. (A-B) Stable expression of EGFR-DN and STAT3β inhibited the LMP1-increased activity of cyclin D1. The indicated NPC cell lines were transfected with a cyclin D1 promoter-reporter construct, a Renilla luciferase transfection control plasmid, and an EGFR-DN or STAT3-β expression plasmid. Twenty-four hrs. after transfection, the cells were treated with DNAzymes or a control oligo (2 μM) for 12 hrs. Cells were harvested at 36 hrs. after transfection and subjected to the luciferase assay. Firefly luciferase was measured and normalized to Renilla luciferase activity. The results were expressed as fold induction of the reporter activity in vector-transfected CNE1 cells, which was assigned a value of 1. (mean ± SD, n =3, * p

    Journal: Journal of Experimental & Clinical Cancer Research : CR

    Article Title: Epstein-Barr Virus encoded LMP1 regulates cyclin D1 promoter activity by nuclear EGFR and STAT3 in CNE1 cells

    doi: 10.1186/1756-9966-32-90

    Figure Lengend Snippet: Inhibitors and dominant negative mutants targeting the EGFR and STAT3 pathways attenuated LMP1-augmented cyclin D1 promoter activity. (A-B) Stable expression of EGFR-DN and STAT3β inhibited the LMP1-increased activity of cyclin D1. The indicated NPC cell lines were transfected with a cyclin D1 promoter-reporter construct, a Renilla luciferase transfection control plasmid, and an EGFR-DN or STAT3-β expression plasmid. Twenty-four hrs. after transfection, the cells were treated with DNAzymes or a control oligo (2 μM) for 12 hrs. Cells were harvested at 36 hrs. after transfection and subjected to the luciferase assay. Firefly luciferase was measured and normalized to Renilla luciferase activity. The results were expressed as fold induction of the reporter activity in vector-transfected CNE1 cells, which was assigned a value of 1. (mean ± SD, n =3, * p

    Article Snippet: We provide the evidence showing cyclin D1 might be modulated by STAT3 induced by EBV LMP1, illustrating the importance of the JAK/STAT signaling pathway on EBV LMP1 induced cyclin D1 transcription and expression.

    Techniques: Dominant Negative Mutation, Activity Assay, Expressing, Transfection, Construct, Luciferase, Plasmid Preparation

    Cyclin D1 expression is reduced in CNE1-LMP1 cells after treatment with EGFR siRNA and STAT3 siRNA. (A) Dual luciferase-reporter assays were performed in CNE1-LMP1 cells after co-transfection with either control siRNA (siControl), EGFR siRNA (siEGFR), or STAT3 siRNA (siSTAT3) in addition to cyclin D1 promoter-reporter constructs and a Renilla luciferase transfection control plasmid. Firefly luciferase was measured and normalized to Renilla luciferase activity. The fold change in cyclin D1 expression by the indicated siRNA is displayed in each case. The control siRNA served as a non-targeting control. (mean ± SD, n =3, * p

    Journal: Journal of Experimental & Clinical Cancer Research : CR

    Article Title: Epstein-Barr Virus encoded LMP1 regulates cyclin D1 promoter activity by nuclear EGFR and STAT3 in CNE1 cells

    doi: 10.1186/1756-9966-32-90

    Figure Lengend Snippet: Cyclin D1 expression is reduced in CNE1-LMP1 cells after treatment with EGFR siRNA and STAT3 siRNA. (A) Dual luciferase-reporter assays were performed in CNE1-LMP1 cells after co-transfection with either control siRNA (siControl), EGFR siRNA (siEGFR), or STAT3 siRNA (siSTAT3) in addition to cyclin D1 promoter-reporter constructs and a Renilla luciferase transfection control plasmid. Firefly luciferase was measured and normalized to Renilla luciferase activity. The fold change in cyclin D1 expression by the indicated siRNA is displayed in each case. The control siRNA served as a non-targeting control. (mean ± SD, n =3, * p

    Article Snippet: We provide the evidence showing cyclin D1 might be modulated by STAT3 induced by EBV LMP1, illustrating the importance of the JAK/STAT signaling pathway on EBV LMP1 induced cyclin D1 transcription and expression.

    Techniques: Expressing, Luciferase, Cotransfection, Construct, Transfection, Plasmid Preparation, Activity Assay

    Protein expression of Cyclin D1, p-Akt and Akt increased in miR-17 mimic-transfected rat glioma C6 cells. Protein expression of Cyclin D1, p-Akt and Akt in glioma C6 cells was detected by Western Blot. After glioma C6 cells were transfected with inhibitor of miR-17 (200 nM) for 72 h, the protein expression of Cyclin D1, Akt and p-Akt increased compared to Lipofectamine and negative control groups. * indicates that p

    Journal: PLoS ONE

    Article Title: Decreased MiR-17 in glioma cells increased cell viability and migration by increasing the expression of Cyclin D1, p-Akt and Akt

    doi: 10.1371/journal.pone.0190515

    Figure Lengend Snippet: Protein expression of Cyclin D1, p-Akt and Akt increased in miR-17 mimic-transfected rat glioma C6 cells. Protein expression of Cyclin D1, p-Akt and Akt in glioma C6 cells was detected by Western Blot. After glioma C6 cells were transfected with inhibitor of miR-17 (200 nM) for 72 h, the protein expression of Cyclin D1, Akt and p-Akt increased compared to Lipofectamine and negative control groups. * indicates that p

    Article Snippet: The main reagents used in the studies and their suppliers were as follows: Trizol (Invitrogen Inc., Grand Island, NY, USA); miRNA reverse transcription kit (Tiangen Inc., Beijing, China); Takara reverse transcriptase M-MLV; common qPCR kit (Tiangen Inc., Beijing, China); RIPA tissue lysis buffer (Beyotime Inc; Shanghai, China); BCA protein quantification kit (Pierce Inc., Rockford, IL, USA); 30% acrylamide; Tris-HCl; sodium dodecyl sulfate (SDS), ammonium persulfate, tetramethylethylenediamine (TEMED); polyvinylidene fluoride (PVDF) membrane; phosphate buffered solution (PBS); Tween-20; electrochemiluminescence (ECL) solution; developing powder; fixing powder; X-ray films; inhibitor of micro-RNA-17); Trim8); specific primer for Cyclin D1 (Sangon Biotech Inc., Shanghai, China); primary antibody of β-actin (ZSGB-BIO Inc., Beijing, China); HRP-labeled goat anti-rabbit secondary antibody (Invitrogen Inc.; Grand Island, NY, USA); HRP-labeled goat anti-mouse secondary antibody (Beyotime Inc.; Shanghai, China).

    Techniques: Expressing, Transfection, Western Blot, Negative Control

    Protein expression of Cyclin D1 in rat glioma C6 cells and normal brain tissue. (A) Representative Western Blot image demonstrating the protein expression of Cyclin D1. (B) Quantification of Cyclin D1 expression. Results showed that the expression of Cyclin D1 was significantly higher in rat glioma C6 cells compared to normal brain tissue. *** indicates that p

    Journal: PLoS ONE

    Article Title: Decreased MiR-17 in glioma cells increased cell viability and migration by increasing the expression of Cyclin D1, p-Akt and Akt

    doi: 10.1371/journal.pone.0190515

    Figure Lengend Snippet: Protein expression of Cyclin D1 in rat glioma C6 cells and normal brain tissue. (A) Representative Western Blot image demonstrating the protein expression of Cyclin D1. (B) Quantification of Cyclin D1 expression. Results showed that the expression of Cyclin D1 was significantly higher in rat glioma C6 cells compared to normal brain tissue. *** indicates that p

    Article Snippet: The main reagents used in the studies and their suppliers were as follows: Trizol (Invitrogen Inc., Grand Island, NY, USA); miRNA reverse transcription kit (Tiangen Inc., Beijing, China); Takara reverse transcriptase M-MLV; common qPCR kit (Tiangen Inc., Beijing, China); RIPA tissue lysis buffer (Beyotime Inc; Shanghai, China); BCA protein quantification kit (Pierce Inc., Rockford, IL, USA); 30% acrylamide; Tris-HCl; sodium dodecyl sulfate (SDS), ammonium persulfate, tetramethylethylenediamine (TEMED); polyvinylidene fluoride (PVDF) membrane; phosphate buffered solution (PBS); Tween-20; electrochemiluminescence (ECL) solution; developing powder; fixing powder; X-ray films; inhibitor of micro-RNA-17); Trim8); specific primer for Cyclin D1 (Sangon Biotech Inc., Shanghai, China); primary antibody of β-actin (ZSGB-BIO Inc., Beijing, China); HRP-labeled goat anti-rabbit secondary antibody (Invitrogen Inc.; Grand Island, NY, USA); HRP-labeled goat anti-mouse secondary antibody (Beyotime Inc.; Shanghai, China).

    Techniques: Expressing, Western Blot

    Protein expression of Cyclin D1, p-Akt and Akt decreased in miR-17 mimic-transfected rat glioma C6 cells. Protein expression of Cyclin D1, p-Akt and Akt in glioma C6 cells was detected by Western Blot. After glioma C6 cells were transfected withmiR-17 mimics (50 nM) for 72 h, the protein expression of Cyclin D1, Akt and p-Akt decreased compared to Lipofectamine and negative control groups. * indicates that p

    Journal: PLoS ONE

    Article Title: Decreased MiR-17 in glioma cells increased cell viability and migration by increasing the expression of Cyclin D1, p-Akt and Akt

    doi: 10.1371/journal.pone.0190515

    Figure Lengend Snippet: Protein expression of Cyclin D1, p-Akt and Akt decreased in miR-17 mimic-transfected rat glioma C6 cells. Protein expression of Cyclin D1, p-Akt and Akt in glioma C6 cells was detected by Western Blot. After glioma C6 cells were transfected withmiR-17 mimics (50 nM) for 72 h, the protein expression of Cyclin D1, Akt and p-Akt decreased compared to Lipofectamine and negative control groups. * indicates that p

    Article Snippet: The main reagents used in the studies and their suppliers were as follows: Trizol (Invitrogen Inc., Grand Island, NY, USA); miRNA reverse transcription kit (Tiangen Inc., Beijing, China); Takara reverse transcriptase M-MLV; common qPCR kit (Tiangen Inc., Beijing, China); RIPA tissue lysis buffer (Beyotime Inc; Shanghai, China); BCA protein quantification kit (Pierce Inc., Rockford, IL, USA); 30% acrylamide; Tris-HCl; sodium dodecyl sulfate (SDS), ammonium persulfate, tetramethylethylenediamine (TEMED); polyvinylidene fluoride (PVDF) membrane; phosphate buffered solution (PBS); Tween-20; electrochemiluminescence (ECL) solution; developing powder; fixing powder; X-ray films; inhibitor of micro-RNA-17); Trim8); specific primer for Cyclin D1 (Sangon Biotech Inc., Shanghai, China); primary antibody of β-actin (ZSGB-BIO Inc., Beijing, China); HRP-labeled goat anti-rabbit secondary antibody (Invitrogen Inc.; Grand Island, NY, USA); HRP-labeled goat anti-mouse secondary antibody (Beyotime Inc.; Shanghai, China).

    Techniques: Expressing, Transfection, Western Blot, Negative Control

    miR-614 suppresses PPP2R2A expression by directly targeting the PPP2R2A 3′-UTR and altered levels of proteins associated with cell proliferation and cell apoptosis in A2780 cells. (A) Predicted miR-614c target sequence in the 3′-UTR of PPP2R2A (PPP2R2A-3′-UTR) and positions of three mutated nucleotides (red) in the 3′-UTR of miR-614 (miR-614-mut). (B) Expression of PPP2R2A in A2780 cells transfected with miR-614 or the miR-614-in were detected by western blotting analysis. α-tubulin served as the loading control. (C) Luciferase reporter assay of A2780 cells transfected with the pGL3-PPP2R2A-3′-UTR reporter and miR-614 or miR-614-in or miR-614-mut oligonucleotides. (D) Reverse transcription-quantitative polymerase chain reaction analysis of expression of BAD and Cyclin D1 in A2780 cells. (E) Western blot analysis of protein expression of Cyclin D1, BAD, p-Rb and Rb in A2780 cells. α-tubulin served as the loading control. *P

    Journal: Molecular Medicine Reports

    Article Title: Upregulation of miR-614 promotes proliferation and inhibits apoptosis in ovarian cancer by suppressing PPP2R2A expression

    doi: 10.3892/mmr.2018.8714

    Figure Lengend Snippet: miR-614 suppresses PPP2R2A expression by directly targeting the PPP2R2A 3′-UTR and altered levels of proteins associated with cell proliferation and cell apoptosis in A2780 cells. (A) Predicted miR-614c target sequence in the 3′-UTR of PPP2R2A (PPP2R2A-3′-UTR) and positions of three mutated nucleotides (red) in the 3′-UTR of miR-614 (miR-614-mut). (B) Expression of PPP2R2A in A2780 cells transfected with miR-614 or the miR-614-in were detected by western blotting analysis. α-tubulin served as the loading control. (C) Luciferase reporter assay of A2780 cells transfected with the pGL3-PPP2R2A-3′-UTR reporter and miR-614 or miR-614-in or miR-614-mut oligonucleotides. (D) Reverse transcription-quantitative polymerase chain reaction analysis of expression of BAD and Cyclin D1 in A2780 cells. (E) Western blot analysis of protein expression of Cyclin D1, BAD, p-Rb and Rb in A2780 cells. α-tubulin served as the loading control. *P

    Article Snippet: Following blocking with 5% dried milk for 2 h at room temperature, membranes were then incubated with anti-PPP2R2A, anti-Cyclin D1 (cat. no. 2978; 1:1,000), anti-BAD, anti-phosphorylated (p)-Rb (cat. no. 8516; 1:1,000), anti-Rb (cat. no. 9313; 1:1,000) and anti-α-tubulin antibodies (cat. no. 2144; 1:1,000; all from Cell Signaling Technology, Inc.) overnight at 4°C, and then incubated with corresponding horseradish peroxidase-conjugated secondary antibodies (cat. no. 7074; 1:5,000, Cell Signaling Technology, Inc.) for 2 h at room temperature.

    Techniques: Expressing, Sequencing, Transfection, Western Blot, Luciferase, Reporter Assay, Real-time Polymerase Chain Reaction