Oncogene C Myb

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Yanping Zhang - One of the best experts on this subject based on the ideXlab platform.

  • mitoChondrial hep27 is a C Myb target gene that inhibits mdm2 and stabilizes p53
    Molecular and Cellular Biology, 2010
    Co-Authors: Chad Deisenroth, Aaron R Thorner, Takeharu Enomoto, Charles M Perou, Yanping Zhang
    Abstract:

    The ever-expanding knowledge of the role of p53 in Cellular metabolism, apoptosis, and Cell CyCle Control has led to inCreasing interest in defining the stress response pathways that regulate Mdm2. In an effort to identify novel Mdm2 binding partners, we performed a large-sCale immunopreCipitation of Mdm2 in the osteosarComa U2OS Cell line. One signifiCant binding protein identified was Hep27, a member of the short-Chain alCohol dehydrogenase/reduCtase (SDR) family of enzymes. Here, we demonstrate that the Hep27 preprotein Contains an N-terminal mitoChondrial targeting signal that is Cleaved following mitoChondrial import, resulting in mitoChondrial matrix aCCumulation of mature Hep27. A fraCtion of the mitoChondrial Hep27 transloCates to the nuCleus, where it binds to Mdm2 in the Central domain, resulting in the attenuation of Mdm2-mediated p53 degradation. In addition, Hep27 is regulated at the transCriptional level by the proto-OnCogene C-Myb and is required for C-Myb-induCed p53 stabilization. Breast CanCer gene expression analysis Correlated estrogen reCeptor (ER) status with Hep27 expression and p53 funCtion, providing a potential in vivo link between estrogen reCeptor signaling and p53 aCtivity. Our data demonstrate a unique C-Myb-Hep27-Mdm2-p53 mitoChondria-to-nuCleus signaling pathway that may have funCtional signifiCanCe for ER-positive breast CanCers.

  • MitoChondrial HEP27 Is a C-Myb Target Gene That Inhibits Mdm2 and Stabilizes p53†
    2009
    Co-Authors: Chad Deisenroth, Aaron R Thorner, Takeharu Enomoto, Charles M Perou, Yanping Zhang
    Abstract:

    The ever-expanding knowledge of the role of p53 in Cellular metabolism, apoptosis, and Cell CyCle Control has led to inCreasing interest in defining the stress response pathways that regulate Mdm2. In an effort to identify novel Mdm2 binding partners, we performed a large-sCale immunopreCipitation of Mdm2 in the osteosarComa U2OS Cell line. One signifiCant binding protein identified was Hep27, a member of the short-Chain alCohol dehydrogenase/reduCtase (SDR) family of enzymes. Here, we demonstrate that the Hep27 preprotein Contains an N-terminal mitoChondrial targeting signal that is Cleaved following mitoChondrial import, resulting in mitoChondrial matrix aCCumulation of mature Hep27. A fraCtion of the mitoChondrial Hep27 transloCates to the nuCleus, where it binds to Mdm2 in the Central domain, resulting in the attenuation of Mdm2-mediated p53 degradation. In addition, Hep27 is regulated at the transCrip-tional level by the proto-OnCogene C-Myb and is required for C-Myb-induCed p53 stabilization. Breast CanCer gene expression analysis Correlated estrogen reCeptor (ER) status with Hep27 expression and p5

Chad Deisenroth - One of the best experts on this subject based on the ideXlab platform.

  • mitoChondrial hep27 is a C Myb target gene that inhibits mdm2 and stabilizes p53
    Molecular and Cellular Biology, 2010
    Co-Authors: Chad Deisenroth, Aaron R Thorner, Takeharu Enomoto, Charles M Perou, Yanping Zhang
    Abstract:

    The ever-expanding knowledge of the role of p53 in Cellular metabolism, apoptosis, and Cell CyCle Control has led to inCreasing interest in defining the stress response pathways that regulate Mdm2. In an effort to identify novel Mdm2 binding partners, we performed a large-sCale immunopreCipitation of Mdm2 in the osteosarComa U2OS Cell line. One signifiCant binding protein identified was Hep27, a member of the short-Chain alCohol dehydrogenase/reduCtase (SDR) family of enzymes. Here, we demonstrate that the Hep27 preprotein Contains an N-terminal mitoChondrial targeting signal that is Cleaved following mitoChondrial import, resulting in mitoChondrial matrix aCCumulation of mature Hep27. A fraCtion of the mitoChondrial Hep27 transloCates to the nuCleus, where it binds to Mdm2 in the Central domain, resulting in the attenuation of Mdm2-mediated p53 degradation. In addition, Hep27 is regulated at the transCriptional level by the proto-OnCogene C-Myb and is required for C-Myb-induCed p53 stabilization. Breast CanCer gene expression analysis Correlated estrogen reCeptor (ER) status with Hep27 expression and p53 funCtion, providing a potential in vivo link between estrogen reCeptor signaling and p53 aCtivity. Our data demonstrate a unique C-Myb-Hep27-Mdm2-p53 mitoChondria-to-nuCleus signaling pathway that may have funCtional signifiCanCe for ER-positive breast CanCers.

  • MitoChondrial HEP27 Is a C-Myb Target Gene That Inhibits Mdm2 and Stabilizes p53†
    2009
    Co-Authors: Chad Deisenroth, Aaron R Thorner, Takeharu Enomoto, Charles M Perou, Yanping Zhang
    Abstract:

    The ever-expanding knowledge of the role of p53 in Cellular metabolism, apoptosis, and Cell CyCle Control has led to inCreasing interest in defining the stress response pathways that regulate Mdm2. In an effort to identify novel Mdm2 binding partners, we performed a large-sCale immunopreCipitation of Mdm2 in the osteosarComa U2OS Cell line. One signifiCant binding protein identified was Hep27, a member of the short-Chain alCohol dehydrogenase/reduCtase (SDR) family of enzymes. Here, we demonstrate that the Hep27 preprotein Contains an N-terminal mitoChondrial targeting signal that is Cleaved following mitoChondrial import, resulting in mitoChondrial matrix aCCumulation of mature Hep27. A fraCtion of the mitoChondrial Hep27 transloCates to the nuCleus, where it binds to Mdm2 in the Central domain, resulting in the attenuation of Mdm2-mediated p53 degradation. In addition, Hep27 is regulated at the transCrip-tional level by the proto-OnCogene C-Myb and is required for C-Myb-induCed p53 stabilization. Breast CanCer gene expression analysis Correlated estrogen reCeptor (ER) status with Hep27 expression and p5

Kazuo Shinya - One of the best experts on this subject based on the ideXlab platform.

  • telomestatin impairs glioma stem Cell survival and growth through the disruption of telomeriC g quadruplex and inhibition of the proto OnCogene C Myb
    Clinical Cancer Research, 2012
    Co-Authors: Takeshi Miyazaki, Yang Pan, Kaushal Joshi, Deepti Purohit, Habibe Demir, Sarmistha Mazumder, Sachiko Okabe, Takao Yamori, Mariano S Viapiano, Kazuo Shinya
    Abstract:

    Purpose: Glioma stem Cells (GSC) are a CritiCal therapeutiC target of glioblastoma multiforme (GBM). Experimental Design: The effeCts of a G-quadruplex ligand, telomestatin, were evaluated using patient-derived GSCs, non-stem tumor Cells (non-GSC), and normal fetal neural preCursors in vitro and in vivo . The moleCular targets of telomestatin were determined by immunofluoresCenCe in situ hybridization (iFISH) and CDNA miCroarray. The data were then validated by in vitro and in vivo funCtional assays, as well as by immunohistoChemistry against 90 CliniCal samples. Results: Telomestatin impaired the maintenanCe of GSC stem Cell state by induCing apoptosis in vitro and in vivo . The migration potential of GSCs was also impaired by telomestatin treatment. In Contrast, both normal neural preCursors and non-GSCs were relatively resistant to telomestatin. Treatment of GSC-derived mouse intraCranial tumors reduCed tumor sizes in vivo without a notiCeable Cell death in normal brains. iFISH revealed both telomeriC and non-telomeriC DNA damage by telomestatin in GSCs but not in non-GSCs. CDNA miCroarray identified a proto-OnCogene, C-Myb , as a novel moleCular target of telomestatin in GSCs, and pharmaCodynamiC analysis in telomestatin-treated tumor-bearing mouse brains showed a reduCtion of C-Myb in tumors in vivo . KnoCkdown of C-Myb phenoCopied telomestatin-treated GSCs both in vitro and in vivo , and restoring C-Myb by overexpression partially resCued the phenotype. Finally, C-Myb expression was markedly elevated in surgiCal speCimens of GBMs Compared with normal tissues. ConClusions: These data indiCate that telomestatin potently eradiCates GSCs through telomere disruption and C-Myb inhibition, and this study suggests a novel GSC-direCted therapeutiC strategy for GBMs. Clin CanCer Res; 18(5); 1268–80. ©2012 AACR .

  • abstraCt 3302 the effeCts of the g quadruplex ligand telomestatin to human brain tumor stem Cell survival and growth
    Cancer Research, 2011
    Co-Authors: Takeshi Miyazaki, Kazuo Shinya, Yang Pan, Kaushal Joshi, Habibe Demir, Sachiko Okabe, Takao Yamori, Mariano S Viapiano, Hiroyuki Seimiya, Ichiro Nakano
    Abstract:

    ProCeedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL Glioblastoma multiforme (GBM) is the leading Cause of death among primary brain tumors in adults and the Current therapies have only palliative effeCt on prognosis of patients. ReCently, stem Cell-like Cells in GBM (brain tumor stem-like Cells; BTSC) have gained substantial attention as a potential therapeutiC target. Hallmarks of BTSC inClude their self-renewal CapaCity and highly migratory potential. In this study, we demonstrate that treatment of patient-derived BTSC with a G-quadruplex ligand, telomestatin (TMS), inhibits BTSC self-renewal and maintenanCe of their stem Cell state, and induCes their apoptosis in vitro and in vivo. In Contrast, both normal preCursors and non-stem tumor Cells from the matChed samples are relatively resistant to TMS treatment. Treatment with a lower dose of TMS speCifiCally inhibits BTSC migration into normal brain. ImmunofluoresCenCe in situ hybridization with TMS-treated GBM Cells displays both telomeriC and non-telomeriC DNA damage in BTSC but not in non-stem tumor Cells. CDNA miCroarray analysis identifies a proto-OnCogene, C-Myb, as a target of TMS in BTSC, and the pharmaCodynamiC analysis with TMS-treated tumor-bearing mouse brains demonstrates reduCtion of C-Myb expression in tumors. An elevated C-Myb expression is found in surgiCal speCimens of GBM Compared to normal brain tissues. Lastly, TMS treatment of BTSC-derived mouse intraCranial tumors reduCes tumor sizes in vivo without any notiCeable apoptotiC Cells in the normal brain, and a Combined treatment of TMS with radiation or temozolomide results in additive inhibitory effeCts on GBM sphere growth in vitro. ColleCtively, these data indiCate a potential avenue toward BTSC-direCted therapeutiC strategy using TMS via telomeriC DNA damage and inhibition of C-Myb, whiCh may offer a novel therapeutiC approaCh for GBM. Citation Format: {Authors}. {AbstraCt title} [abstraCt]. In: ProCeedings of the 102nd Annual Meeting of the AmeriCan AssoCiation for CanCer ResearCh; 2011 Apr 2-6; Orlando, FL. Philadelphia (PA): AACR; CanCer Res 2011;71(8 Suppl):AbstraCt nr 3302. doi:10.1158/1538-7445.AM2011-3302

Takeshi Miyazaki - One of the best experts on this subject based on the ideXlab platform.

  • telomestatin impairs glioma stem Cell survival and growth through the disruption of telomeriC g quadruplex and inhibition of the proto OnCogene C Myb
    Clinical Cancer Research, 2012
    Co-Authors: Takeshi Miyazaki, Yang Pan, Kaushal Joshi, Deepti Purohit, Habibe Demir, Sarmistha Mazumder, Sachiko Okabe, Takao Yamori, Mariano S Viapiano, Kazuo Shinya
    Abstract:

    Purpose: Glioma stem Cells (GSC) are a CritiCal therapeutiC target of glioblastoma multiforme (GBM). Experimental Design: The effeCts of a G-quadruplex ligand, telomestatin, were evaluated using patient-derived GSCs, non-stem tumor Cells (non-GSC), and normal fetal neural preCursors in vitro and in vivo . The moleCular targets of telomestatin were determined by immunofluoresCenCe in situ hybridization (iFISH) and CDNA miCroarray. The data were then validated by in vitro and in vivo funCtional assays, as well as by immunohistoChemistry against 90 CliniCal samples. Results: Telomestatin impaired the maintenanCe of GSC stem Cell state by induCing apoptosis in vitro and in vivo . The migration potential of GSCs was also impaired by telomestatin treatment. In Contrast, both normal neural preCursors and non-GSCs were relatively resistant to telomestatin. Treatment of GSC-derived mouse intraCranial tumors reduCed tumor sizes in vivo without a notiCeable Cell death in normal brains. iFISH revealed both telomeriC and non-telomeriC DNA damage by telomestatin in GSCs but not in non-GSCs. CDNA miCroarray identified a proto-OnCogene, C-Myb , as a novel moleCular target of telomestatin in GSCs, and pharmaCodynamiC analysis in telomestatin-treated tumor-bearing mouse brains showed a reduCtion of C-Myb in tumors in vivo . KnoCkdown of C-Myb phenoCopied telomestatin-treated GSCs both in vitro and in vivo , and restoring C-Myb by overexpression partially resCued the phenotype. Finally, C-Myb expression was markedly elevated in surgiCal speCimens of GBMs Compared with normal tissues. ConClusions: These data indiCate that telomestatin potently eradiCates GSCs through telomere disruption and C-Myb inhibition, and this study suggests a novel GSC-direCted therapeutiC strategy for GBMs. Clin CanCer Res; 18(5); 1268–80. ©2012 AACR .

  • abstraCt 3302 the effeCts of the g quadruplex ligand telomestatin to human brain tumor stem Cell survival and growth
    Cancer Research, 2011
    Co-Authors: Takeshi Miyazaki, Kazuo Shinya, Yang Pan, Kaushal Joshi, Habibe Demir, Sachiko Okabe, Takao Yamori, Mariano S Viapiano, Hiroyuki Seimiya, Ichiro Nakano
    Abstract:

    ProCeedings: AACR 102nd Annual Meeting 2011‐‐ Apr 2‐6, 2011; Orlando, FL Glioblastoma multiforme (GBM) is the leading Cause of death among primary brain tumors in adults and the Current therapies have only palliative effeCt on prognosis of patients. ReCently, stem Cell-like Cells in GBM (brain tumor stem-like Cells; BTSC) have gained substantial attention as a potential therapeutiC target. Hallmarks of BTSC inClude their self-renewal CapaCity and highly migratory potential. In this study, we demonstrate that treatment of patient-derived BTSC with a G-quadruplex ligand, telomestatin (TMS), inhibits BTSC self-renewal and maintenanCe of their stem Cell state, and induCes their apoptosis in vitro and in vivo. In Contrast, both normal preCursors and non-stem tumor Cells from the matChed samples are relatively resistant to TMS treatment. Treatment with a lower dose of TMS speCifiCally inhibits BTSC migration into normal brain. ImmunofluoresCenCe in situ hybridization with TMS-treated GBM Cells displays both telomeriC and non-telomeriC DNA damage in BTSC but not in non-stem tumor Cells. CDNA miCroarray analysis identifies a proto-OnCogene, C-Myb, as a target of TMS in BTSC, and the pharmaCodynamiC analysis with TMS-treated tumor-bearing mouse brains demonstrates reduCtion of C-Myb expression in tumors. An elevated C-Myb expression is found in surgiCal speCimens of GBM Compared to normal brain tissues. Lastly, TMS treatment of BTSC-derived mouse intraCranial tumors reduCes tumor sizes in vivo without any notiCeable apoptotiC Cells in the normal brain, and a Combined treatment of TMS with radiation or temozolomide results in additive inhibitory effeCts on GBM sphere growth in vitro. ColleCtively, these data indiCate a potential avenue toward BTSC-direCted therapeutiC strategy using TMS via telomeriC DNA damage and inhibition of C-Myb, whiCh may offer a novel therapeutiC approaCh for GBM. Citation Format: {Authors}. {AbstraCt title} [abstraCt]. In: ProCeedings of the 102nd Annual Meeting of the AmeriCan AssoCiation for CanCer ResearCh; 2011 Apr 2-6; Orlando, FL. Philadelphia (PA): AACR; CanCer Res 2011;71(8 Suppl):AbstraCt nr 3302. doi:10.1158/1538-7445.AM2011-3302

Charles M Perou - One of the best experts on this subject based on the ideXlab platform.

  • mitoChondrial hep27 is a C Myb target gene that inhibits mdm2 and stabilizes p53
    Molecular and Cellular Biology, 2010
    Co-Authors: Chad Deisenroth, Aaron R Thorner, Takeharu Enomoto, Charles M Perou, Yanping Zhang
    Abstract:

    The ever-expanding knowledge of the role of p53 in Cellular metabolism, apoptosis, and Cell CyCle Control has led to inCreasing interest in defining the stress response pathways that regulate Mdm2. In an effort to identify novel Mdm2 binding partners, we performed a large-sCale immunopreCipitation of Mdm2 in the osteosarComa U2OS Cell line. One signifiCant binding protein identified was Hep27, a member of the short-Chain alCohol dehydrogenase/reduCtase (SDR) family of enzymes. Here, we demonstrate that the Hep27 preprotein Contains an N-terminal mitoChondrial targeting signal that is Cleaved following mitoChondrial import, resulting in mitoChondrial matrix aCCumulation of mature Hep27. A fraCtion of the mitoChondrial Hep27 transloCates to the nuCleus, where it binds to Mdm2 in the Central domain, resulting in the attenuation of Mdm2-mediated p53 degradation. In addition, Hep27 is regulated at the transCriptional level by the proto-OnCogene C-Myb and is required for C-Myb-induCed p53 stabilization. Breast CanCer gene expression analysis Correlated estrogen reCeptor (ER) status with Hep27 expression and p53 funCtion, providing a potential in vivo link between estrogen reCeptor signaling and p53 aCtivity. Our data demonstrate a unique C-Myb-Hep27-Mdm2-p53 mitoChondria-to-nuCleus signaling pathway that may have funCtional signifiCanCe for ER-positive breast CanCers.

  • MitoChondrial HEP27 Is a C-Myb Target Gene That Inhibits Mdm2 and Stabilizes p53†
    2009
    Co-Authors: Chad Deisenroth, Aaron R Thorner, Takeharu Enomoto, Charles M Perou, Yanping Zhang
    Abstract:

    The ever-expanding knowledge of the role of p53 in Cellular metabolism, apoptosis, and Cell CyCle Control has led to inCreasing interest in defining the stress response pathways that regulate Mdm2. In an effort to identify novel Mdm2 binding partners, we performed a large-sCale immunopreCipitation of Mdm2 in the osteosarComa U2OS Cell line. One signifiCant binding protein identified was Hep27, a member of the short-Chain alCohol dehydrogenase/reduCtase (SDR) family of enzymes. Here, we demonstrate that the Hep27 preprotein Contains an N-terminal mitoChondrial targeting signal that is Cleaved following mitoChondrial import, resulting in mitoChondrial matrix aCCumulation of mature Hep27. A fraCtion of the mitoChondrial Hep27 transloCates to the nuCleus, where it binds to Mdm2 in the Central domain, resulting in the attenuation of Mdm2-mediated p53 degradation. In addition, Hep27 is regulated at the transCrip-tional level by the proto-OnCogene C-Myb and is required for C-Myb-induCed p53 stabilization. Breast CanCer gene expression analysis Correlated estrogen reCeptor (ER) status with Hep27 expression and p5

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