The Experts below are selected from a list of 90 Experts worldwide ranked by ideXlab platform

Stuart H Orkin - One of the best experts on this subject based on the ideXlab platform.

  • requirement of NANOG dimerization for stem cell self renewal and pluripotency
    Proceedings of the National Academy of Sciences of the United States of America, 2008
    Co-Authors: Jianlong Wang, Dana N Levasseur, Stuart H Orkin
    Abstract:

    Pluripotency of embryonic stem (ES) cells is maintained by transcription factors that form a highly interconnected Protein interaction network surrounding the Homeobox Protein NANOG. Enforced expression of NANOG in mouse ES (mES) cells promotes self-renewal and alleviates their requirement for leukemia inhibitory factor (LIF). Understanding molecular mechanisms by which NANOG functions should illuminate fundamental properties of stem cells and the process of cellular reprogramming. Previously, we showed that NANOG forms multiple Protein complexes in mES cells. Here, we demonstrate that NANOG dimerizes through its C-terminal domain rather than the homeodomain. Dimerization is required for interaction with other pluripotency network Proteins. We also show that enforced expression of the NANOG dimer, but not the monomer, functionally replaces wild-type NANOG to sustain LIF-independent self-renewal of ES cells. Our results demonstrate that NANOG–NANOG homodimerization is a critical aspect of its function promoting stem cell pluripotency.

  • Requirement of NANOG dimerization for stem cell self-renewal and pluripotency
    Proceedings of the National Academy of Sciences of the United States of America, 2008
    Co-Authors: Jianlong Wang, Dana N Levasseur, Stuart H Orkin
    Abstract:

    Pluripotency of embryonic stem (ES) cells is maintained by transcription factors that form a highly interconnected Protein interaction network surrounding the Homeobox Protein NANOG. Enforced expression of NANOG in mouse ES (mES) cells promotes self-renewal and alleviates their requirement for leukemia inhibitory factor (LIF). Understanding molecular mechanisms by which NANOG functions should illuminate fundamental properties of stem cells and the process of cellular reprogramming. Previously, we showed that NANOG forms multiple Protein complexes in mES cells. Here, we demonstrate that NANOG dimerizes through its C-terminal domain rather than the homeodomain. Dimerization is required for interaction with other pluripotency network Proteins. We also show that enforced expression of the NANOG dimer, but not the monomer, functionally replaces wild-type NANOG to sustain LIF-independent self-renewal of ES cells. Our results demonstrate that NANOG–NANOG homodimerization is a critical aspect of its function promoting stem cell pluripotency.

Bing Zhu - One of the best experts on this subject based on the ideXlab platform.

  • Novel functionalized nanoparticles for tumor-targeting co-delivery of doxorubicin and siRNA to enhance cancer therapy
    International Journal of Nanomedicine, 2017
    Co-Authors: Yu Xia, Changbing Wang, Zhengfang Lin, Yinghua Li, Tiantian Xu, Mingqi Zhao, Bing Zhu
    Abstract:

    Human Homeobox Protein (NANOG) is highly expressed in most cancer cells and has gradually emerged as an excellent target in cancer therapy, owing to its regulation of cancer cell proliferation, metastasis and apoptosis. In this study, we prepared tumor-targeting functionalized selenium nanoparticles (RGDfC-SeNPs) to load chemotherapeutic doxorubicin (DOX) and NANOG siRNA. Herein, RGDfC peptide was used as a tumor-targeting moiety which could specifically bind to αvβ3 integrins overexpressed on various cancer cells. The sizes of RGDfC-SeNPs@DOX nanoparticles (~12 nm) were confirmed by both dynamic light scattering and transmission electron microscopy. The chemical structure of RGDfC-SeNPs@DOX was characterized via Fourier-transform infrared spectroscopy. The RGDfC-SeNPs@DOX was compacted with siRNA (anti-NANOG) by electrostatic interaction to fabricate the RGDfC-SeNPs@DOX/siRNA complex. The RGDfC-SeNPs@DOX/siRNA complex nanoparticles could efficiently enter into HepG2 cells via clathrin-associated endocytosis, and showed high gene transfection efficiency that resulted in enhanced gene silencing. The in vivo biodistribution experiment indicated that RGDfC-SeNPs@DOX/siRNA nanoparticles were capable of specifically accumulating in the tumor site. Furthermore, treatment with RGDfC-SeNPs@DOX/siRNA resulted in a more significant anticancer activity than the free DOX, RGDfC-SeNPs@DOX or RGDfC-SeNPs/siRNA in vitro and in vivo. In summary, this study shows a novel type of DOX and siRNA co-delivery system, thereby providing an alternative route for cancer treatment.

Jianlong Wang - One of the best experts on this subject based on the ideXlab platform.

  • requirement of NANOG dimerization for stem cell self renewal and pluripotency
    Proceedings of the National Academy of Sciences of the United States of America, 2008
    Co-Authors: Jianlong Wang, Dana N Levasseur, Stuart H Orkin
    Abstract:

    Pluripotency of embryonic stem (ES) cells is maintained by transcription factors that form a highly interconnected Protein interaction network surrounding the Homeobox Protein NANOG. Enforced expression of NANOG in mouse ES (mES) cells promotes self-renewal and alleviates their requirement for leukemia inhibitory factor (LIF). Understanding molecular mechanisms by which NANOG functions should illuminate fundamental properties of stem cells and the process of cellular reprogramming. Previously, we showed that NANOG forms multiple Protein complexes in mES cells. Here, we demonstrate that NANOG dimerizes through its C-terminal domain rather than the homeodomain. Dimerization is required for interaction with other pluripotency network Proteins. We also show that enforced expression of the NANOG dimer, but not the monomer, functionally replaces wild-type NANOG to sustain LIF-independent self-renewal of ES cells. Our results demonstrate that NANOG–NANOG homodimerization is a critical aspect of its function promoting stem cell pluripotency.

  • Requirement of NANOG dimerization for stem cell self-renewal and pluripotency
    Proceedings of the National Academy of Sciences of the United States of America, 2008
    Co-Authors: Jianlong Wang, Dana N Levasseur, Stuart H Orkin
    Abstract:

    Pluripotency of embryonic stem (ES) cells is maintained by transcription factors that form a highly interconnected Protein interaction network surrounding the Homeobox Protein NANOG. Enforced expression of NANOG in mouse ES (mES) cells promotes self-renewal and alleviates their requirement for leukemia inhibitory factor (LIF). Understanding molecular mechanisms by which NANOG functions should illuminate fundamental properties of stem cells and the process of cellular reprogramming. Previously, we showed that NANOG forms multiple Protein complexes in mES cells. Here, we demonstrate that NANOG dimerizes through its C-terminal domain rather than the homeodomain. Dimerization is required for interaction with other pluripotency network Proteins. We also show that enforced expression of the NANOG dimer, but not the monomer, functionally replaces wild-type NANOG to sustain LIF-independent self-renewal of ES cells. Our results demonstrate that NANOG–NANOG homodimerization is a critical aspect of its function promoting stem cell pluripotency.

Yu Xia - One of the best experts on this subject based on the ideXlab platform.

  • Novel functionalized nanoparticles for tumor-targeting co-delivery of doxorubicin and siRNA to enhance cancer therapy
    International Journal of Nanomedicine, 2017
    Co-Authors: Yu Xia, Changbing Wang, Zhengfang Lin, Yinghua Li, Tiantian Xu, Mingqi Zhao, Bing Zhu
    Abstract:

    Human Homeobox Protein (NANOG) is highly expressed in most cancer cells and has gradually emerged as an excellent target in cancer therapy, owing to its regulation of cancer cell proliferation, metastasis and apoptosis. In this study, we prepared tumor-targeting functionalized selenium nanoparticles (RGDfC-SeNPs) to load chemotherapeutic doxorubicin (DOX) and NANOG siRNA. Herein, RGDfC peptide was used as a tumor-targeting moiety which could specifically bind to αvβ3 integrins overexpressed on various cancer cells. The sizes of RGDfC-SeNPs@DOX nanoparticles (~12 nm) were confirmed by both dynamic light scattering and transmission electron microscopy. The chemical structure of RGDfC-SeNPs@DOX was characterized via Fourier-transform infrared spectroscopy. The RGDfC-SeNPs@DOX was compacted with siRNA (anti-NANOG) by electrostatic interaction to fabricate the RGDfC-SeNPs@DOX/siRNA complex. The RGDfC-SeNPs@DOX/siRNA complex nanoparticles could efficiently enter into HepG2 cells via clathrin-associated endocytosis, and showed high gene transfection efficiency that resulted in enhanced gene silencing. The in vivo biodistribution experiment indicated that RGDfC-SeNPs@DOX/siRNA nanoparticles were capable of specifically accumulating in the tumor site. Furthermore, treatment with RGDfC-SeNPs@DOX/siRNA resulted in a more significant anticancer activity than the free DOX, RGDfC-SeNPs@DOX or RGDfC-SeNPs/siRNA in vitro and in vivo. In summary, this study shows a novel type of DOX and siRNA co-delivery system, thereby providing an alternative route for cancer treatment.

Dana N Levasseur - One of the best experts on this subject based on the ideXlab platform.

  • requirement of NANOG dimerization for stem cell self renewal and pluripotency
    Proceedings of the National Academy of Sciences of the United States of America, 2008
    Co-Authors: Jianlong Wang, Dana N Levasseur, Stuart H Orkin
    Abstract:

    Pluripotency of embryonic stem (ES) cells is maintained by transcription factors that form a highly interconnected Protein interaction network surrounding the Homeobox Protein NANOG. Enforced expression of NANOG in mouse ES (mES) cells promotes self-renewal and alleviates their requirement for leukemia inhibitory factor (LIF). Understanding molecular mechanisms by which NANOG functions should illuminate fundamental properties of stem cells and the process of cellular reprogramming. Previously, we showed that NANOG forms multiple Protein complexes in mES cells. Here, we demonstrate that NANOG dimerizes through its C-terminal domain rather than the homeodomain. Dimerization is required for interaction with other pluripotency network Proteins. We also show that enforced expression of the NANOG dimer, but not the monomer, functionally replaces wild-type NANOG to sustain LIF-independent self-renewal of ES cells. Our results demonstrate that NANOG–NANOG homodimerization is a critical aspect of its function promoting stem cell pluripotency.

  • Requirement of NANOG dimerization for stem cell self-renewal and pluripotency
    Proceedings of the National Academy of Sciences of the United States of America, 2008
    Co-Authors: Jianlong Wang, Dana N Levasseur, Stuart H Orkin
    Abstract:

    Pluripotency of embryonic stem (ES) cells is maintained by transcription factors that form a highly interconnected Protein interaction network surrounding the Homeobox Protein NANOG. Enforced expression of NANOG in mouse ES (mES) cells promotes self-renewal and alleviates their requirement for leukemia inhibitory factor (LIF). Understanding molecular mechanisms by which NANOG functions should illuminate fundamental properties of stem cells and the process of cellular reprogramming. Previously, we showed that NANOG forms multiple Protein complexes in mES cells. Here, we demonstrate that NANOG dimerizes through its C-terminal domain rather than the homeodomain. Dimerization is required for interaction with other pluripotency network Proteins. We also show that enforced expression of the NANOG dimer, but not the monomer, functionally replaces wild-type NANOG to sustain LIF-independent self-renewal of ES cells. Our results demonstrate that NANOG–NANOG homodimerization is a critical aspect of its function promoting stem cell pluripotency.