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Chuanyue Wu - One of the best experts on this subject based on the ideXlab platform.

  • the mig 2 integrin interaction strengthens cell matrix Adhesion and modulates cell motility
    Journal of Biological Chemistry, 2007
    Co-Authors: Yan Qing, Edward F Plow, Ka Chen, Koichi Fukuda, Yizeng Tu, Shan Wu, Chuanyue Wu
    Abstract:

    Abstract Integrin-mediated Cell-Matrix Adhesion plays an important role in control of cell behavior. We report here that MIG-2, a widely expressed focal Adhesion protein, interacts with β1 and β3 integrin cytoplasmic domains. Integrin binding is mediated by a single site within the MIG-2 FERM domain. Functionally, the MIG-2/integrin interaction recruits MIG-2 to focal Adhesions. Furthermore, using αIIbβ3 integrin-expressing Chinese hamster ovary cells, a well described model system for integrin activation, we show that MIG-2 promotes integrin activation and enhances cell-extracellular matrix Adhesion. Although MIG-2 is expressed in many cell types, it is deficient in certain colon cancer cells. Expression of MIG-2, but not of an integrin binding-defective MIG-2 mutant, in MIG-2-null colon cancer cells strengthened Cell-Matrix Adhesion, promoted focal Adhesion formation, and reduced cell motility. These results suggest that the MIG-2/integrin interaction is an important element in the cellular control of integrin-mediated Cell-Matrix Adhesion and that loss of this interaction likely contributes to high motility of colon cancer cells.

  • assembly of the pinch ilk ch ilkbp complex precedes and is essential for localization of each component to cell matrix Adhesion sites
    Journal of Cell Science, 2002
    Co-Authors: Yongjun Zhang, Ka Chen, Yizeng Tu, Algirdas Velyvis, Yanwu Yang, Chuanyue Wu
    Abstract:

    PINCH, integrin-linked kinase (ILK) and calponin homology-containing ILK-binding protein (CH-ILKBP) form a ternary complex that plays crucial roles at cell-extracellular matrix Adhesion sites. To understand the mechanism underlying the complex formation and recruitment to cell-Adhesion sites we have undertaken a combined structural, mutational and cell biological analysis. Three-dimensional structure-based point mutations identified specific PINCH and ILK sites that mediate the complex formation. Analyses of the binding defective point mutants revealed that the assembly of the PINCH-ILK-CH-ILKBP complex is essential for their localization to cell-extracellular matrix Adhesion sites. The formation of the PINCH-ILK-CH-ILKBP complex precedes integrin-mediated cell Adhesion and spreading. Furthermore, inhibition of protein kinase C, but not that of actin polymerization, inhibited the PINCH-ILK-CH-ILKBP complex formation, suggesting that the PINCH-ILK-CH-ILKBP complex likely serves as a downstream effector of protein kinase C in the cellular control of focal Adhesion assembly. Finally, we provide evidence that the formation of the PINCH-ILK-CH-ILKBP complex, while necessary, is not sufficient for ILK localization to cell-extracellular matrix Adhesion sites. These results provide new insights into the molecular mechanism underlying the assembly and regulation of Cell-Matrix Adhesion structures.

Edward F Plow - One of the best experts on this subject based on the ideXlab platform.

  • the mig 2 integrin interaction strengthens cell matrix Adhesion and modulates cell motility
    Journal of Biological Chemistry, 2007
    Co-Authors: Xiaohua Shi, Ka Chen, Koichi Fukuda, Jun Qin, Edward F Plow
    Abstract:

    Integrin-mediated Cell-Matrix Adhesion plays an important role in control of cell behavior. We report here that MIG-2, a widely expressed focal Adhesion protein, interacts with beta1 and beta3 integrin cytoplasmic domains. Integrin binding is mediated by a single site within the MIG-2 FERM domain. Functionally, the MIG-2/integrin interaction recruits MIG-2 to focal Adhesions. Furthermore, using alphaIIbbeta3 integrin-expressing Chinese hamster ovary cells, a well described model system for integrin activation, we show that MIG-2 promotes integrin activation and enhances cell-extracellular matrix Adhesion. Although MIG-2 is expressed in many cell types, it is deficient in certain colon cancer cells. Expression of MIG-2, but not of an integrin binding-defective MIG-2 mutant, in MIG-2-null colon cancer cells strengthened Cell-Matrix Adhesion, promoted focal Adhesion formation, and reduced cell motility. These results suggest that the MIG-2/integrin interaction is an important element in the cellular control of integrin-mediated Cell-Matrix Adhesion and that loss of this interaction likely contributes to high motility of colon cancer cells.

  • the mig 2 integrin interaction strengthens cell matrix Adhesion and modulates cell motility
    Journal of Biological Chemistry, 2007
    Co-Authors: Yan Qing, Edward F Plow, Ka Chen, Koichi Fukuda, Yizeng Tu, Shan Wu, Chuanyue Wu
    Abstract:

    Abstract Integrin-mediated Cell-Matrix Adhesion plays an important role in control of cell behavior. We report here that MIG-2, a widely expressed focal Adhesion protein, interacts with β1 and β3 integrin cytoplasmic domains. Integrin binding is mediated by a single site within the MIG-2 FERM domain. Functionally, the MIG-2/integrin interaction recruits MIG-2 to focal Adhesions. Furthermore, using αIIbβ3 integrin-expressing Chinese hamster ovary cells, a well described model system for integrin activation, we show that MIG-2 promotes integrin activation and enhances cell-extracellular matrix Adhesion. Although MIG-2 is expressed in many cell types, it is deficient in certain colon cancer cells. Expression of MIG-2, but not of an integrin binding-defective MIG-2 mutant, in MIG-2-null colon cancer cells strengthened Cell-Matrix Adhesion, promoted focal Adhesion formation, and reduced cell motility. These results suggest that the MIG-2/integrin interaction is an important element in the cellular control of integrin-mediated Cell-Matrix Adhesion and that loss of this interaction likely contributes to high motility of colon cancer cells.

Ka Chen - One of the best experts on this subject based on the ideXlab platform.

  • the mig 2 integrin interaction strengthens cell matrix Adhesion and modulates cell motility
    Journal of Biological Chemistry, 2007
    Co-Authors: Xiaohua Shi, Ka Chen, Koichi Fukuda, Jun Qin, Edward F Plow
    Abstract:

    Integrin-mediated Cell-Matrix Adhesion plays an important role in control of cell behavior. We report here that MIG-2, a widely expressed focal Adhesion protein, interacts with beta1 and beta3 integrin cytoplasmic domains. Integrin binding is mediated by a single site within the MIG-2 FERM domain. Functionally, the MIG-2/integrin interaction recruits MIG-2 to focal Adhesions. Furthermore, using alphaIIbbeta3 integrin-expressing Chinese hamster ovary cells, a well described model system for integrin activation, we show that MIG-2 promotes integrin activation and enhances cell-extracellular matrix Adhesion. Although MIG-2 is expressed in many cell types, it is deficient in certain colon cancer cells. Expression of MIG-2, but not of an integrin binding-defective MIG-2 mutant, in MIG-2-null colon cancer cells strengthened Cell-Matrix Adhesion, promoted focal Adhesion formation, and reduced cell motility. These results suggest that the MIG-2/integrin interaction is an important element in the cellular control of integrin-mediated Cell-Matrix Adhesion and that loss of this interaction likely contributes to high motility of colon cancer cells.

  • the mig 2 integrin interaction strengthens cell matrix Adhesion and modulates cell motility
    Journal of Biological Chemistry, 2007
    Co-Authors: Yan Qing, Edward F Plow, Ka Chen, Koichi Fukuda, Yizeng Tu, Shan Wu, Chuanyue Wu
    Abstract:

    Abstract Integrin-mediated Cell-Matrix Adhesion plays an important role in control of cell behavior. We report here that MIG-2, a widely expressed focal Adhesion protein, interacts with β1 and β3 integrin cytoplasmic domains. Integrin binding is mediated by a single site within the MIG-2 FERM domain. Functionally, the MIG-2/integrin interaction recruits MIG-2 to focal Adhesions. Furthermore, using αIIbβ3 integrin-expressing Chinese hamster ovary cells, a well described model system for integrin activation, we show that MIG-2 promotes integrin activation and enhances cell-extracellular matrix Adhesion. Although MIG-2 is expressed in many cell types, it is deficient in certain colon cancer cells. Expression of MIG-2, but not of an integrin binding-defective MIG-2 mutant, in MIG-2-null colon cancer cells strengthened Cell-Matrix Adhesion, promoted focal Adhesion formation, and reduced cell motility. These results suggest that the MIG-2/integrin interaction is an important element in the cellular control of integrin-mediated Cell-Matrix Adhesion and that loss of this interaction likely contributes to high motility of colon cancer cells.

  • assembly of the pinch ilk ch ilkbp complex precedes and is essential for localization of each component to cell matrix Adhesion sites
    Journal of Cell Science, 2002
    Co-Authors: Yongjun Zhang, Ka Chen, Yizeng Tu, Algirdas Velyvis, Yanwu Yang, Chuanyue Wu
    Abstract:

    PINCH, integrin-linked kinase (ILK) and calponin homology-containing ILK-binding protein (CH-ILKBP) form a ternary complex that plays crucial roles at cell-extracellular matrix Adhesion sites. To understand the mechanism underlying the complex formation and recruitment to cell-Adhesion sites we have undertaken a combined structural, mutational and cell biological analysis. Three-dimensional structure-based point mutations identified specific PINCH and ILK sites that mediate the complex formation. Analyses of the binding defective point mutants revealed that the assembly of the PINCH-ILK-CH-ILKBP complex is essential for their localization to cell-extracellular matrix Adhesion sites. The formation of the PINCH-ILK-CH-ILKBP complex precedes integrin-mediated cell Adhesion and spreading. Furthermore, inhibition of protein kinase C, but not that of actin polymerization, inhibited the PINCH-ILK-CH-ILKBP complex formation, suggesting that the PINCH-ILK-CH-ILKBP complex likely serves as a downstream effector of protein kinase C in the cellular control of focal Adhesion assembly. Finally, we provide evidence that the formation of the PINCH-ILK-CH-ILKBP complex, while necessary, is not sufficient for ILK localization to cell-extracellular matrix Adhesion sites. These results provide new insights into the molecular mechanism underlying the assembly and regulation of Cell-Matrix Adhesion structures.

Koichi Fukuda - One of the best experts on this subject based on the ideXlab platform.

  • the mig 2 integrin interaction strengthens cell matrix Adhesion and modulates cell motility
    Journal of Biological Chemistry, 2007
    Co-Authors: Xiaohua Shi, Ka Chen, Koichi Fukuda, Jun Qin, Edward F Plow
    Abstract:

    Integrin-mediated Cell-Matrix Adhesion plays an important role in control of cell behavior. We report here that MIG-2, a widely expressed focal Adhesion protein, interacts with beta1 and beta3 integrin cytoplasmic domains. Integrin binding is mediated by a single site within the MIG-2 FERM domain. Functionally, the MIG-2/integrin interaction recruits MIG-2 to focal Adhesions. Furthermore, using alphaIIbbeta3 integrin-expressing Chinese hamster ovary cells, a well described model system for integrin activation, we show that MIG-2 promotes integrin activation and enhances cell-extracellular matrix Adhesion. Although MIG-2 is expressed in many cell types, it is deficient in certain colon cancer cells. Expression of MIG-2, but not of an integrin binding-defective MIG-2 mutant, in MIG-2-null colon cancer cells strengthened Cell-Matrix Adhesion, promoted focal Adhesion formation, and reduced cell motility. These results suggest that the MIG-2/integrin interaction is an important element in the cellular control of integrin-mediated Cell-Matrix Adhesion and that loss of this interaction likely contributes to high motility of colon cancer cells.

  • the mig 2 integrin interaction strengthens cell matrix Adhesion and modulates cell motility
    Journal of Biological Chemistry, 2007
    Co-Authors: Yan Qing, Edward F Plow, Ka Chen, Koichi Fukuda, Yizeng Tu, Shan Wu, Chuanyue Wu
    Abstract:

    Abstract Integrin-mediated Cell-Matrix Adhesion plays an important role in control of cell behavior. We report here that MIG-2, a widely expressed focal Adhesion protein, interacts with β1 and β3 integrin cytoplasmic domains. Integrin binding is mediated by a single site within the MIG-2 FERM domain. Functionally, the MIG-2/integrin interaction recruits MIG-2 to focal Adhesions. Furthermore, using αIIbβ3 integrin-expressing Chinese hamster ovary cells, a well described model system for integrin activation, we show that MIG-2 promotes integrin activation and enhances cell-extracellular matrix Adhesion. Although MIG-2 is expressed in many cell types, it is deficient in certain colon cancer cells. Expression of MIG-2, but not of an integrin binding-defective MIG-2 mutant, in MIG-2-null colon cancer cells strengthened Cell-Matrix Adhesion, promoted focal Adhesion formation, and reduced cell motility. These results suggest that the MIG-2/integrin interaction is an important element in the cellular control of integrin-mediated Cell-Matrix Adhesion and that loss of this interaction likely contributes to high motility of colon cancer cells.

D K Turgeon - One of the best experts on this subject based on the ideXlab platform.

  • calcium induced differentiation in normal human colonoid cultures cell cell cell matrix Adhesion barrier formation and tissue integrity
    PLOS ONE, 2019
    Co-Authors: Durga Attili, Michael K Dame, Shannon D Mcclintock, Areeba H Rizvi, Shailja Pandya, Humza Rehman, Daniyal M Nadeem, Aliah Richter, Dafydd G Thomas, D K Turgeon
    Abstract:

    Background and aims The goal of the study was to assess calcium alone and Aquamin, a multi-mineral natural product that contains magnesium and detectable levels of 72 trace elements in addition to calcium, for capacity to affect growth and differentiation in colonoid cultures derived from histologically-normal human colon tissue. Methods Colonoid cultures were maintained in a low-calcium (0.25 mM) medium or in medium supplemented with an amount of calcium (1.5–3.0 mM), either from calcium alone or Aquamin for a period of two weeks. This was shown in a previous study to induce differentiation in colonoids derived from large adenomas. Changes in growth, morphological features and protein expression profile were assessed at the end of the incubation period using a combination of phase-contrast and scanning electron microscopy, histology and immunohistology, proteomic assessment and transmission electron microscopy. Results Unlike the previously-studied tumor-derived colonoids (which remained un-differentiated in the absence of calcium-supplementation), normal tissue colonoids underwent differentiation as indicated by gross and microscopic appearance, a low proliferative index and high-level expression of cytokeratin 20 in the absence of intervention (i.e., in control condition). Only modest additional changes were seen in these parameters with either calcium alone or Aquamin (providing up to 3.0 mM calcium). In spite of this, proteomic analysis and immunohistochemistry revealed that both interventions induced strong up-regulation of proteins that promote cell-cell and Cell-Matrix adhesive functions, barrier formation and tissue integrity. Transmission electron microscopy revealed an increase in desmosomes in response to intervention. Conclusions These findings demonstrate that colonoids derived from histologically normal human tissue can undergo differentiation in the presence of a low ambient calcium concentration. However, higher calcium levels induce elaboration of proteins that promote cell-cell and Cell-Matrix Adhesion. These changes could lead to improved barrier function and improved colon tissue health.

  • Calcium-induced differentiation in normal human colonoid cultures: Cell-cell / Cell-Matrix Adhesion, barrier formation and tissue integrity
    2019
    Co-Authors: Durga Attili, Michael K Dame, Shannon D Mcclintock, Areeba H Rizvi, Shailja Pandya, Humza Rehman, Daniyal M Nadeem, Aliah Richter, Dafydd Thomas, D K Turgeon
    Abstract:

    Background and aimsThe goal of the study was to assess calcium alone and Aquamin, a multi-mineral natural product that contains magnesium and detectable levels of 72 trace elements in addition to calcium, for capacity to affect growth and differentiation in colonoid cultures derived from histologically-normal human colon tissue.MethodsColonoid cultures were maintained in a low-calcium (0.25 mM) medium or in medium supplemented with an amount of calcium (1.5–3.0 mM), either from calcium alone or Aquamin for a period of two weeks. This was shown in a previous study to induce differentiation in colonoids derived from large adenomas. Changes in growth, morphological features and protein expression profile were assessed at the end of the incubation period using a combination of phase-contrast and scanning electron microscopy, histology and immunohistology, proteomic assessment and transmission electron microscopy.ResultsUnlike the previously-studied tumor-derived colonoids (which remained un-differentiated in the absence of calcium-supplementation), normal tissue colonoids underwent differentiation as indicated by gross and microscopic appearance, a low proliferative index and high-level expression of cytokeratin 20 in the absence of intervention (i.e., in control condition). Only modest additional changes were seen in these parameters with either calcium alone or Aquamin (providing up to 3.0 mM calcium). In spite of this, proteomic analysis and immunohistochemistry revealed that both interventions induced strong up-regulation of proteins that promote cell-cell and Cell-Matrix adhesive functions, barrier formation and tissue integrity. Transmission electron microscopy revealed an increase in desmosomes in response to intervention.ConclusionsThese findings demonstrate that colonoids derived from histologically normal human tissue can undergo differentiation in the presence of a low ambient calcium concentration. However, higher calcium levels induce elaboration of proteins that promote cell-cell and Cell-Matrix Adhesion. These changes could lead to improved barrier function and improved colon tissue health.

  • calcium induced differentiation in normal human colonoid cultures cell cell cell matrix Adhesion barrier formation and tissue integrity
    bioRxiv, 2018
    Co-Authors: Durga Attili, Michael K Dame, Shannon D Mcclintock, Areeba H Rizvi, Shailja Pandya, Humza Rehman, Daniyal M Nadeem, Aliah Richter, Dafydd G Thomas, D K Turgeon
    Abstract:

    ABSTRACT Colonoid cultures were established from histologically-normal human colon tissue and maintained in a low-calcium (0.25 mM) medium or in medium supplemented with an amount of calcium (1.5 - 3.0 mM) that was shown in a previous study to induce differentiation in colonoids derived from large adenomas. Calcium alone was compared to Aquamin, a multi-mineral natural product that contains magnesium and detectable levels of 72 additional trace elements in addition to calcium. Unlike the previously-studied tumor-derived colonoids (which remained un-differentiated in the absence of calcium-supplementation), normal tissue colonoids underwent differentiation as indicated by gross and microscopic appearance, a low proliferative index and high-level expression of cytokeratin 20 (CK20) in the absence of intervention. Only modest additional changes were seen in these parameters with either calcium alone or Aquamin (providing up to 3.0 mM calcium). In spite of this, proteomic analysis and immunohistochemistry revealed that both interventions induced strong up-regulation of proteins that promote cell-cell and Cell-Matrix adhesive functions, barrier formation and tissue integrity. Transmission electron microscopy revealed an increase in desmosomes in response to intervention. These findings demonstrate that histologically normal human colonoids can undergo differentiation in the presence of a low ambient calcium concentration. However, higher calcium levels can induce elaboration of proteins that promote cell-cell and Cell-Matrix Adhesion. These changes could lead to improved barrier function and improved colon tissue health.