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Markku S. Kulomaa - One of the best experts on this subject based on the ideXlab platform.

  • Internalization of novel Non-Viral Vector TAT-streptavidin into human cells
    BMC Biotechnology, 2007
    Co-Authors: Johanna Rinne, Brian Albarran, Teemu O. Ihalainen, Markku S. Kulomaa, Pasi Kankaanpaa, Juulia Jylhava, Patrick S. Stayton, Vesa P. Hytönen, Maija Vihinen-ranta
    Abstract:

    Background The cell-penetrating peptide derived from the Human immunodeficiency virus-1 transactivator protein Tat possesses the capacity to promote the effective uptake of various cargo molecules across the plasma membrane in vitro and in vivo. The objective of this study was to characterize the uptake and delivery mechanisms of a novel streptavidin fusion construct, TAT47–57-streptavidin (TAT-SA, 60 kD). SA represents a potentially useful TAT-fusion partner due to its ability to perform as a versatile intracellular delivery Vector for a wide array of biotinylated molecules or cargoes.

  • Internalization of novel Non-Viral Vector TAT-streptavidin into human cells
    BMC Biotechnology, 2007
    Co-Authors: Johanna Rinne, Brian Albarran, Teemu O. Ihalainen, Markku S. Kulomaa, Pasi Kankaanpaa, Juulia Jylhava, Patrick S. Stayton, Vesa P. Hytönen, Maija Vihinen-ranta
    Abstract:

    Background The cell-penetrating peptide derived from the Human immunodeficiency virus-1 transactivator protein Tat possesses the capacity to promote the effective uptake of various cargo molecules across the plasma membrane in vitro and in vivo . The objective of this study was to characterize the uptake and delivery mechanisms of a novel streptavidin fusion construct, TAT_47–57-streptavidin (TAT-SA, 60 kD). SA represents a potentially useful TAT-fusion partner due to its ability to perform as a versatile intracellular delivery Vector for a wide array of biotinylated molecules or cargoes. Results By confocal and immunoelectron microscopy the majority of internalized TAT-SA was shown to accumulate in perinuclear vesicles in both cancer and non-cancer cell lines. The uptake studies in living cells with various fluorescent endocytic markers and inhibiting agents suggested that TAT-SA is internalized into cells efficiently, using both clathrin-mediated endocytosis and lipid-raft-mediated macropinocytosis. When endosomal release of TAT-SA was enhanced through the incorporation of a biotinylated, pH-responsive polymer poly(propylacrylic acid) (PPAA), nuclear localization of TAT-SA and TAT-SA bound to biotin was markedly improved. Additionally, no significant cytotoxicity was detected in the TAT-SA constructs. Conclusion This study demonstrates that TAT-SA-PPAA is a potential Non-Viral Vector to be utilized in protein therapeutics to deliver biotinylated molecules both into cytoplasm and nucleus of human cells.

  • internalization of novel non viral Vector tat streptavidin into human cells
    BMC Biotechnology, 2007
    Co-Authors: Johanna Rinne, Brian Albarran, Teemu O. Ihalainen, Markku S. Kulomaa, Pasi Kankaanpaa, Juulia Jylhava, Patrick S. Stayton, Vesa P. Hytönen
    Abstract:

    The cell-penetrating peptide derived from the Human immunodeficiency virus-1 transactivator protein Tat possesses the capacity to promote the effective uptake of various cargo molecules across the plasma membrane in vitro and in vivo. The objective of this study was to characterize the uptake and delivery mechanisms of a novel streptavidin fusion construct, TAT47–57-streptavidin (TAT-SA, 60 kD). SA represents a potentially useful TAT-fusion partner due to its ability to perform as a versatile intracellular delivery Vector for a wide array of biotinylated molecules or cargoes. By confocal and immunoelectron microscopy the majority of internalized TAT-SA was shown to accumulate in perinuclear vesicles in both cancer and non-cancer cell lines. The uptake studies in living cells with various fluorescent endocytic markers and inhibiting agents suggested that TAT-SA is internalized into cells efficiently, using both clathrin-mediated endocytosis and lipid-raft-mediated macropinocytosis. When endosomal release of TAT-SA was enhanced through the incorporation of a biotinylated, pH-responsive polymer poly(propylacrylic acid) (PPAA), nuclear localization of TAT-SA and TAT-SA bound to biotin was markedly improved. Additionally, no significant cytotoxicity was detected in the TAT-SA constructs. This study demonstrates that TAT-SA-PPAA is a potential Non-Viral Vector to be utilized in protein therapeutics to deliver biotinylated molecules both into cytoplasm and nucleus of human cells.

K C Gupta - One of the best experts on this subject based on the ideXlab platform.

  • recent trends in non viral Vector mediated gene delivery
    Biotechnology Journal, 2009
    Co-Authors: Atul Pathak, S Patnaik, K C Gupta
    Abstract:

    Nucleic acids-based next generation biopharmaceuticals (i.e., pDNA, oligonucleotides, short interfering RNA) are potential pioneering materials to cope with various incurable diseases. However, several biological barriers present a challenge for efficient gene delivery. On the other hand, developments in nanotechnology now offer numerous Non-Viral Vectors that have been fabricated and found capable of transmitting the biopharmaceuticals into the cell and even into specific subcellular compartments like mitochondria. This overview illustrates cellular barriers and current status of Non-Viral gene Vectors, i.e., lipoplexes, liposomes, polyplexes, and nanoparticles, to relocate therapeutic DNA-based nanomedicine into the target cell. Despite the awesome impact of physical methods (i.e., ultrasound, electroporation), chemical methods have been shown to accomplish high-level and safe transgene expression. Further comprehension of barriers and the mechanism of cellular uptake will facilitate development of nucleic acids-based nanotherapy for alleviation of various disorders.

Johanna Rinne - One of the best experts on this subject based on the ideXlab platform.

  • Internalization of novel Non-Viral Vector TAT-streptavidin into human cells
    BMC Biotechnology, 2007
    Co-Authors: Johanna Rinne, Brian Albarran, Teemu O. Ihalainen, Markku S. Kulomaa, Pasi Kankaanpaa, Juulia Jylhava, Patrick S. Stayton, Vesa P. Hytönen, Maija Vihinen-ranta
    Abstract:

    Background The cell-penetrating peptide derived from the Human immunodeficiency virus-1 transactivator protein Tat possesses the capacity to promote the effective uptake of various cargo molecules across the plasma membrane in vitro and in vivo. The objective of this study was to characterize the uptake and delivery mechanisms of a novel streptavidin fusion construct, TAT47–57-streptavidin (TAT-SA, 60 kD). SA represents a potentially useful TAT-fusion partner due to its ability to perform as a versatile intracellular delivery Vector for a wide array of biotinylated molecules or cargoes.

  • Internalization of novel Non-Viral Vector TAT-streptavidin into human cells
    BMC Biotechnology, 2007
    Co-Authors: Johanna Rinne, Brian Albarran, Teemu O. Ihalainen, Markku S. Kulomaa, Pasi Kankaanpaa, Juulia Jylhava, Patrick S. Stayton, Vesa P. Hytönen, Maija Vihinen-ranta
    Abstract:

    Background The cell-penetrating peptide derived from the Human immunodeficiency virus-1 transactivator protein Tat possesses the capacity to promote the effective uptake of various cargo molecules across the plasma membrane in vitro and in vivo . The objective of this study was to characterize the uptake and delivery mechanisms of a novel streptavidin fusion construct, TAT_47–57-streptavidin (TAT-SA, 60 kD). SA represents a potentially useful TAT-fusion partner due to its ability to perform as a versatile intracellular delivery Vector for a wide array of biotinylated molecules or cargoes. Results By confocal and immunoelectron microscopy the majority of internalized TAT-SA was shown to accumulate in perinuclear vesicles in both cancer and non-cancer cell lines. The uptake studies in living cells with various fluorescent endocytic markers and inhibiting agents suggested that TAT-SA is internalized into cells efficiently, using both clathrin-mediated endocytosis and lipid-raft-mediated macropinocytosis. When endosomal release of TAT-SA was enhanced through the incorporation of a biotinylated, pH-responsive polymer poly(propylacrylic acid) (PPAA), nuclear localization of TAT-SA and TAT-SA bound to biotin was markedly improved. Additionally, no significant cytotoxicity was detected in the TAT-SA constructs. Conclusion This study demonstrates that TAT-SA-PPAA is a potential Non-Viral Vector to be utilized in protein therapeutics to deliver biotinylated molecules both into cytoplasm and nucleus of human cells.

  • internalization of novel non viral Vector tat streptavidin into human cells
    BMC Biotechnology, 2007
    Co-Authors: Johanna Rinne, Brian Albarran, Teemu O. Ihalainen, Markku S. Kulomaa, Pasi Kankaanpaa, Juulia Jylhava, Patrick S. Stayton, Vesa P. Hytönen
    Abstract:

    The cell-penetrating peptide derived from the Human immunodeficiency virus-1 transactivator protein Tat possesses the capacity to promote the effective uptake of various cargo molecules across the plasma membrane in vitro and in vivo. The objective of this study was to characterize the uptake and delivery mechanisms of a novel streptavidin fusion construct, TAT47–57-streptavidin (TAT-SA, 60 kD). SA represents a potentially useful TAT-fusion partner due to its ability to perform as a versatile intracellular delivery Vector for a wide array of biotinylated molecules or cargoes. By confocal and immunoelectron microscopy the majority of internalized TAT-SA was shown to accumulate in perinuclear vesicles in both cancer and non-cancer cell lines. The uptake studies in living cells with various fluorescent endocytic markers and inhibiting agents suggested that TAT-SA is internalized into cells efficiently, using both clathrin-mediated endocytosis and lipid-raft-mediated macropinocytosis. When endosomal release of TAT-SA was enhanced through the incorporation of a biotinylated, pH-responsive polymer poly(propylacrylic acid) (PPAA), nuclear localization of TAT-SA and TAT-SA bound to biotin was markedly improved. Additionally, no significant cytotoxicity was detected in the TAT-SA constructs. This study demonstrates that TAT-SA-PPAA is a potential Non-Viral Vector to be utilized in protein therapeutics to deliver biotinylated molecules both into cytoplasm and nucleus of human cells.

Maija Vihinen-ranta - One of the best experts on this subject based on the ideXlab platform.

  • Internalization of novel Non-Viral Vector TAT-streptavidin into human cells
    BMC Biotechnology, 2007
    Co-Authors: Johanna Rinne, Brian Albarran, Teemu O. Ihalainen, Markku S. Kulomaa, Pasi Kankaanpaa, Juulia Jylhava, Patrick S. Stayton, Vesa P. Hytönen, Maija Vihinen-ranta
    Abstract:

    Background The cell-penetrating peptide derived from the Human immunodeficiency virus-1 transactivator protein Tat possesses the capacity to promote the effective uptake of various cargo molecules across the plasma membrane in vitro and in vivo. The objective of this study was to characterize the uptake and delivery mechanisms of a novel streptavidin fusion construct, TAT47–57-streptavidin (TAT-SA, 60 kD). SA represents a potentially useful TAT-fusion partner due to its ability to perform as a versatile intracellular delivery Vector for a wide array of biotinylated molecules or cargoes.

  • Internalization of novel Non-Viral Vector TAT-streptavidin into human cells
    BMC Biotechnology, 2007
    Co-Authors: Johanna Rinne, Brian Albarran, Teemu O. Ihalainen, Markku S. Kulomaa, Pasi Kankaanpaa, Juulia Jylhava, Patrick S. Stayton, Vesa P. Hytönen, Maija Vihinen-ranta
    Abstract:

    Background The cell-penetrating peptide derived from the Human immunodeficiency virus-1 transactivator protein Tat possesses the capacity to promote the effective uptake of various cargo molecules across the plasma membrane in vitro and in vivo . The objective of this study was to characterize the uptake and delivery mechanisms of a novel streptavidin fusion construct, TAT_47–57-streptavidin (TAT-SA, 60 kD). SA represents a potentially useful TAT-fusion partner due to its ability to perform as a versatile intracellular delivery Vector for a wide array of biotinylated molecules or cargoes. Results By confocal and immunoelectron microscopy the majority of internalized TAT-SA was shown to accumulate in perinuclear vesicles in both cancer and non-cancer cell lines. The uptake studies in living cells with various fluorescent endocytic markers and inhibiting agents suggested that TAT-SA is internalized into cells efficiently, using both clathrin-mediated endocytosis and lipid-raft-mediated macropinocytosis. When endosomal release of TAT-SA was enhanced through the incorporation of a biotinylated, pH-responsive polymer poly(propylacrylic acid) (PPAA), nuclear localization of TAT-SA and TAT-SA bound to biotin was markedly improved. Additionally, no significant cytotoxicity was detected in the TAT-SA constructs. Conclusion This study demonstrates that TAT-SA-PPAA is a potential Non-Viral Vector to be utilized in protein therapeutics to deliver biotinylated molecules both into cytoplasm and nucleus of human cells.

Vesa P. Hytönen - One of the best experts on this subject based on the ideXlab platform.

  • Internalization of novel Non-Viral Vector TAT-streptavidin into human cells
    BMC Biotechnology, 2007
    Co-Authors: Johanna Rinne, Brian Albarran, Teemu O. Ihalainen, Markku S. Kulomaa, Pasi Kankaanpaa, Juulia Jylhava, Patrick S. Stayton, Vesa P. Hytönen, Maija Vihinen-ranta
    Abstract:

    Background The cell-penetrating peptide derived from the Human immunodeficiency virus-1 transactivator protein Tat possesses the capacity to promote the effective uptake of various cargo molecules across the plasma membrane in vitro and in vivo. The objective of this study was to characterize the uptake and delivery mechanisms of a novel streptavidin fusion construct, TAT47–57-streptavidin (TAT-SA, 60 kD). SA represents a potentially useful TAT-fusion partner due to its ability to perform as a versatile intracellular delivery Vector for a wide array of biotinylated molecules or cargoes.

  • Internalization of novel Non-Viral Vector TAT-streptavidin into human cells
    BMC Biotechnology, 2007
    Co-Authors: Johanna Rinne, Brian Albarran, Teemu O. Ihalainen, Markku S. Kulomaa, Pasi Kankaanpaa, Juulia Jylhava, Patrick S. Stayton, Vesa P. Hytönen, Maija Vihinen-ranta
    Abstract:

    Background The cell-penetrating peptide derived from the Human immunodeficiency virus-1 transactivator protein Tat possesses the capacity to promote the effective uptake of various cargo molecules across the plasma membrane in vitro and in vivo . The objective of this study was to characterize the uptake and delivery mechanisms of a novel streptavidin fusion construct, TAT_47–57-streptavidin (TAT-SA, 60 kD). SA represents a potentially useful TAT-fusion partner due to its ability to perform as a versatile intracellular delivery Vector for a wide array of biotinylated molecules or cargoes. Results By confocal and immunoelectron microscopy the majority of internalized TAT-SA was shown to accumulate in perinuclear vesicles in both cancer and non-cancer cell lines. The uptake studies in living cells with various fluorescent endocytic markers and inhibiting agents suggested that TAT-SA is internalized into cells efficiently, using both clathrin-mediated endocytosis and lipid-raft-mediated macropinocytosis. When endosomal release of TAT-SA was enhanced through the incorporation of a biotinylated, pH-responsive polymer poly(propylacrylic acid) (PPAA), nuclear localization of TAT-SA and TAT-SA bound to biotin was markedly improved. Additionally, no significant cytotoxicity was detected in the TAT-SA constructs. Conclusion This study demonstrates that TAT-SA-PPAA is a potential Non-Viral Vector to be utilized in protein therapeutics to deliver biotinylated molecules both into cytoplasm and nucleus of human cells.

  • internalization of novel non viral Vector tat streptavidin into human cells
    BMC Biotechnology, 2007
    Co-Authors: Johanna Rinne, Brian Albarran, Teemu O. Ihalainen, Markku S. Kulomaa, Pasi Kankaanpaa, Juulia Jylhava, Patrick S. Stayton, Vesa P. Hytönen
    Abstract:

    The cell-penetrating peptide derived from the Human immunodeficiency virus-1 transactivator protein Tat possesses the capacity to promote the effective uptake of various cargo molecules across the plasma membrane in vitro and in vivo. The objective of this study was to characterize the uptake and delivery mechanisms of a novel streptavidin fusion construct, TAT47–57-streptavidin (TAT-SA, 60 kD). SA represents a potentially useful TAT-fusion partner due to its ability to perform as a versatile intracellular delivery Vector for a wide array of biotinylated molecules or cargoes. By confocal and immunoelectron microscopy the majority of internalized TAT-SA was shown to accumulate in perinuclear vesicles in both cancer and non-cancer cell lines. The uptake studies in living cells with various fluorescent endocytic markers and inhibiting agents suggested that TAT-SA is internalized into cells efficiently, using both clathrin-mediated endocytosis and lipid-raft-mediated macropinocytosis. When endosomal release of TAT-SA was enhanced through the incorporation of a biotinylated, pH-responsive polymer poly(propylacrylic acid) (PPAA), nuclear localization of TAT-SA and TAT-SA bound to biotin was markedly improved. Additionally, no significant cytotoxicity was detected in the TAT-SA constructs. This study demonstrates that TAT-SA-PPAA is a potential Non-Viral Vector to be utilized in protein therapeutics to deliver biotinylated molecules both into cytoplasm and nucleus of human cells.