The Experts below are selected from a list of 169284 Experts worldwide ranked by ideXlab platform

Florence A Scholl - One of the best experts on this subject based on the ideXlab platform.

  • modeling inducible human tissue neoplasia identifies an extracellular Matrix Interaction network involved in cancer progression
    Cancer Cell, 2009
    Co-Authors: Jason A Reuter, Susana Ortizurda, Markus Kretz, John Garcia, Florence A Scholl, Anna M G Pasmooij, David S Cassarino, Howard Y Chang, Paul A Khavari
    Abstract:

    Summary To elucidate mechanisms of cancer progression, we generated inducible human neoplasia in three-dimensionally intact epithelial tissue. Gene expression profiling of both epithelia and stroma at specific time points during tumor progression revealed sequential enrichment of genes mediating discrete biologic functions in each tissue compartment. A core cancer progression signature was distilled using the increased signaling specificity of downstream oncogene effectors and subjected to network modeling. Network topology predicted that tumor development depends on specific extracellular Matrix-interacting network hubs. Blockade of one such hub, the β1 integrin subunit, disrupted network gene expression and attenuated tumorigenesis in vivo. Thus, integrating network modeling and temporal gene expression analysis of inducible human neoplasia provides an approach to prioritize and characterize genes functioning in cancer progression.

  • modeling inducible human tissue neoplasia identifies an extracellular Matrix Interaction network involved in cancer progression
    Cancer Cell, 2009
    Co-Authors: Jason A Reuter, Susana Ortizurda, Markus Kretz, John Garcia, Florence A Scholl
    Abstract:

    To elucidate mechanisms of cancer progression, we generated inducible human neoplasia in three-dimensionally intact epithelial tissue. Gene expression profiling of both epithelia and stroma at specific time points during tumor progression revealed sequential enrichment of genes mediating discrete biologic functions in each tissue compartment. A core cancer progression signature was distilled using the increased signaling specificity of downstream oncogene effectors and subjected to network modeling. Network topology predicted that tumor development depends on specific extracellular Matrix-interacting network hubs. Blockade of one such hub, the beta1 integrin subunit, disrupted network gene expression and attenuated tumorigenesis in vivo. Thus, integrating network modeling and temporal gene expression analysis of inducible human neoplasia provides an approach to prioritize and characterize genes functioning in cancer progression.

Healy Smith - One of the best experts on this subject based on the ideXlab platform.

  • icap 1 a novel β1 integrin cytoplasmic domain associated protein binds to a conserved and functionally important npxy sequence motif of β1 integrin
    Journal of Cell Biology, 1997
    Co-Authors: David D Chang, Carol Wong, Healy Smith
    Abstract:

    The cytoplasmic domains of integrins are essential for cell adhesion. We report identification of a novel protein, ICAP-1 (integrin cytoplasmic domain– associated protein-1), which binds to the β1 integrin cytoplasmic domain. The Interaction between ICAP-1 and β1 integrins is highly specific, as demonstrated by the lack of Interaction between ICAP-1 and the cytoplasmic domains of other β integrins, and requires a conserved and functionally important NPXY sequence motif found in the COOH-terminal region of the β1 integrin cytoplasmic domain. Mutational studies reveal that Asn and Tyr of the NPXY motif and a Val residue located NH2-terminal to this motif are critical for the ICAP-1 binding. Two isoforms of ICAP-1, a 200–amino acid protein (ICAP-1α) and a shorter 150–amino acid protein (ICAP-1β), derived from alternatively spliced mRNA, are expressed in most cells. ICAP-1α is a phosphoprotein and the extent of its phosphorylation is regulated by the cell–Matrix Interaction. First, an enhancement of ICAP-1α phosphorylation is observed when cells were plated on fibronectin-coated but not on nonspecific poly-l-lysine–coated surface. Second, the expression of a constitutively activated RhoA protein that disrupts the cell–Matrix Interaction results in dephosphorylation of ICAP-1α. The regulation of ICAP-1α phosphorylation by the cell–Matrix Interaction suggests an important role of ICAP-1 during integrin-dependent cell adhesion.

  • icap 1 a novel β1 integrin cytoplasmic domain associated protein binds to a conserved and functionally important npxy sequence motif of β1 integrin
    Journal of Cell Biology, 1997
    Co-Authors: David D Chang, Carol Wong, Healy Smith, Jenny Yichun Liu
    Abstract:

    The cytoplasmic domains of integrins are essential for cell adhesion. We report identification of a novel protein, ICAP-1 (integrin cytoplasmic domain- associated protein-1), which binds to the 1 integrin cytoplasmic domain. The Interaction between ICAP-1 and beta1 integrins is highly specific, as demonstrated by the lack of Interaction between ICAP-1 and the cytoplasmic domains of other beta integrins, and requires a conserved and functionally important NPXY sequence motif found in the COOH-terminal region of the beta1 integrin cytoplasmic domain. Mutational studies reveal that Asn and Tyr of the NPXY motif and a Val residue located NH2-terminal to this motif are critical for the ICAP-1 binding. Two isoforms of ICAP-1, a 200-amino acid protein (ICAP-1alpha) and a shorter 150-amino acid protein (ICAP-1beta), derived from alternatively spliced mRNA, are expressed in most cells. ICAP-1alpha is a phosphoprotein and the extent of its phosphorylation is regulated by the cell-Matrix Interaction. First, an enhancement of ICAP-1alpha phosphorylation is observed when cells were plated on fibronectin-coated but not on nonspecific poly-L-lysine-coated surface. Second, the expression of a constitutively activated RhoA protein that disrupts the cell-Matrix Interaction results in dephosphorylation of ICAP-1alpha. The regulation of ICAP-1alpha phosphorylation by the cell-Matrix Interaction suggests an important role of ICAP-1 during integrin-dependent cell adhesion.

Jason A Reuter - One of the best experts on this subject based on the ideXlab platform.

  • modeling inducible human tissue neoplasia identifies an extracellular Matrix Interaction network involved in cancer progression
    Cancer Cell, 2009
    Co-Authors: Jason A Reuter, Susana Ortizurda, Markus Kretz, John Garcia, Florence A Scholl, Anna M G Pasmooij, David S Cassarino, Howard Y Chang, Paul A Khavari
    Abstract:

    Summary To elucidate mechanisms of cancer progression, we generated inducible human neoplasia in three-dimensionally intact epithelial tissue. Gene expression profiling of both epithelia and stroma at specific time points during tumor progression revealed sequential enrichment of genes mediating discrete biologic functions in each tissue compartment. A core cancer progression signature was distilled using the increased signaling specificity of downstream oncogene effectors and subjected to network modeling. Network topology predicted that tumor development depends on specific extracellular Matrix-interacting network hubs. Blockade of one such hub, the β1 integrin subunit, disrupted network gene expression and attenuated tumorigenesis in vivo. Thus, integrating network modeling and temporal gene expression analysis of inducible human neoplasia provides an approach to prioritize and characterize genes functioning in cancer progression.

  • modeling inducible human tissue neoplasia identifies an extracellular Matrix Interaction network involved in cancer progression
    Cancer Cell, 2009
    Co-Authors: Jason A Reuter, Susana Ortizurda, Markus Kretz, John Garcia, Florence A Scholl
    Abstract:

    To elucidate mechanisms of cancer progression, we generated inducible human neoplasia in three-dimensionally intact epithelial tissue. Gene expression profiling of both epithelia and stroma at specific time points during tumor progression revealed sequential enrichment of genes mediating discrete biologic functions in each tissue compartment. A core cancer progression signature was distilled using the increased signaling specificity of downstream oncogene effectors and subjected to network modeling. Network topology predicted that tumor development depends on specific extracellular Matrix-interacting network hubs. Blockade of one such hub, the beta1 integrin subunit, disrupted network gene expression and attenuated tumorigenesis in vivo. Thus, integrating network modeling and temporal gene expression analysis of inducible human neoplasia provides an approach to prioritize and characterize genes functioning in cancer progression.

David D Chang - One of the best experts on this subject based on the ideXlab platform.

  • icap 1 a novel β1 integrin cytoplasmic domain associated protein binds to a conserved and functionally important npxy sequence motif of β1 integrin
    Journal of Cell Biology, 1997
    Co-Authors: David D Chang, Carol Wong, Healy Smith
    Abstract:

    The cytoplasmic domains of integrins are essential for cell adhesion. We report identification of a novel protein, ICAP-1 (integrin cytoplasmic domain– associated protein-1), which binds to the β1 integrin cytoplasmic domain. The Interaction between ICAP-1 and β1 integrins is highly specific, as demonstrated by the lack of Interaction between ICAP-1 and the cytoplasmic domains of other β integrins, and requires a conserved and functionally important NPXY sequence motif found in the COOH-terminal region of the β1 integrin cytoplasmic domain. Mutational studies reveal that Asn and Tyr of the NPXY motif and a Val residue located NH2-terminal to this motif are critical for the ICAP-1 binding. Two isoforms of ICAP-1, a 200–amino acid protein (ICAP-1α) and a shorter 150–amino acid protein (ICAP-1β), derived from alternatively spliced mRNA, are expressed in most cells. ICAP-1α is a phosphoprotein and the extent of its phosphorylation is regulated by the cell–Matrix Interaction. First, an enhancement of ICAP-1α phosphorylation is observed when cells were plated on fibronectin-coated but not on nonspecific poly-l-lysine–coated surface. Second, the expression of a constitutively activated RhoA protein that disrupts the cell–Matrix Interaction results in dephosphorylation of ICAP-1α. The regulation of ICAP-1α phosphorylation by the cell–Matrix Interaction suggests an important role of ICAP-1 during integrin-dependent cell adhesion.

  • icap 1 a novel β1 integrin cytoplasmic domain associated protein binds to a conserved and functionally important npxy sequence motif of β1 integrin
    Journal of Cell Biology, 1997
    Co-Authors: David D Chang, Carol Wong, Healy Smith, Jenny Yichun Liu
    Abstract:

    The cytoplasmic domains of integrins are essential for cell adhesion. We report identification of a novel protein, ICAP-1 (integrin cytoplasmic domain- associated protein-1), which binds to the 1 integrin cytoplasmic domain. The Interaction between ICAP-1 and beta1 integrins is highly specific, as demonstrated by the lack of Interaction between ICAP-1 and the cytoplasmic domains of other beta integrins, and requires a conserved and functionally important NPXY sequence motif found in the COOH-terminal region of the beta1 integrin cytoplasmic domain. Mutational studies reveal that Asn and Tyr of the NPXY motif and a Val residue located NH2-terminal to this motif are critical for the ICAP-1 binding. Two isoforms of ICAP-1, a 200-amino acid protein (ICAP-1alpha) and a shorter 150-amino acid protein (ICAP-1beta), derived from alternatively spliced mRNA, are expressed in most cells. ICAP-1alpha is a phosphoprotein and the extent of its phosphorylation is regulated by the cell-Matrix Interaction. First, an enhancement of ICAP-1alpha phosphorylation is observed when cells were plated on fibronectin-coated but not on nonspecific poly-L-lysine-coated surface. Second, the expression of a constitutively activated RhoA protein that disrupts the cell-Matrix Interaction results in dephosphorylation of ICAP-1alpha. The regulation of ICAP-1alpha phosphorylation by the cell-Matrix Interaction suggests an important role of ICAP-1 during integrin-dependent cell adhesion.

Jenny Yichun Liu - One of the best experts on this subject based on the ideXlab platform.

  • icap 1 a novel β1 integrin cytoplasmic domain associated protein binds to a conserved and functionally important npxy sequence motif of β1 integrin
    Journal of Cell Biology, 1997
    Co-Authors: David D Chang, Carol Wong, Healy Smith, Jenny Yichun Liu
    Abstract:

    The cytoplasmic domains of integrins are essential for cell adhesion. We report identification of a novel protein, ICAP-1 (integrin cytoplasmic domain- associated protein-1), which binds to the 1 integrin cytoplasmic domain. The Interaction between ICAP-1 and beta1 integrins is highly specific, as demonstrated by the lack of Interaction between ICAP-1 and the cytoplasmic domains of other beta integrins, and requires a conserved and functionally important NPXY sequence motif found in the COOH-terminal region of the beta1 integrin cytoplasmic domain. Mutational studies reveal that Asn and Tyr of the NPXY motif and a Val residue located NH2-terminal to this motif are critical for the ICAP-1 binding. Two isoforms of ICAP-1, a 200-amino acid protein (ICAP-1alpha) and a shorter 150-amino acid protein (ICAP-1beta), derived from alternatively spliced mRNA, are expressed in most cells. ICAP-1alpha is a phosphoprotein and the extent of its phosphorylation is regulated by the cell-Matrix Interaction. First, an enhancement of ICAP-1alpha phosphorylation is observed when cells were plated on fibronectin-coated but not on nonspecific poly-L-lysine-coated surface. Second, the expression of a constitutively activated RhoA protein that disrupts the cell-Matrix Interaction results in dephosphorylation of ICAP-1alpha. The regulation of ICAP-1alpha phosphorylation by the cell-Matrix Interaction suggests an important role of ICAP-1 during integrin-dependent cell adhesion.