173 research outputs found

    Recombinant carboxyl-terminal fibrin-binding domain of human fibronectin expressed in mouse L cells

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    This research was originally published in the Journal of Biological Chemistry. K Ichihara-Tanaka, K Titani and K Sekiguchi. Recombinant carboxyl-terminal fibrin-binding domain of human fibronectin expressed in mouse L cells. J. Biol. Chem. 1990; 265: 401-407 © the American Society for Biochemistry and Molecular Biolog

    Laminin-10/11 and Fibronectin Differentially Regulate Integrin- dependent Rho and Rac Activation via p130Cas-CrkII-DOCK180 Pathway

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    This research was originally published in the Journal of Biological Chemistry. Jianguo Gu, Yasuhiro Sumida, Noriko Sanzen and Kiyotoshi Sekiguchi. Laminin-10/11 and Fibronectin Differentially Regulate Integrin- dependent Rho and Rac Activation via p130Cas-CrkII-DOCK180 Pathway. J. Biol. Chem. 2001; 276: 27090–27097 © the American Society for Biochemistry and Molecular Biolog

    Alternatively Spliced EDA Segment Regulates Fibronectin-dependent Cell Cycle Progression and Mitogenic Signal Transduction

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    This research was originally published in the Journal of Biological Chemistry. Ri-ichiroh Manabe, Naoko Oh-e and Kiyotoshi Sekiguchi. Alternatively Spliced EDA Segment Regulates Fibronectin-dependent Cell Cycle Progression and Mitogenic Signal Transduction. J. Biol. Chem. 1999; 274: 5919-5924 © the American Society for Biochemistry and Molecular Biolog

    A monoclonal antibody directed to N-acetylneuraminosyl-alpha 2 leads to 6-galactosyl residue in gangliosides and glycoproteins

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    This research was originally published in the Journal of Biological Chemistry. S Hakomori, C M Patterson, E Nudelman and K Sekiguchi. A monoclonal antibody directed to N-acetylneuraminosyl-alpha 2 leads to 6-galactosyl residue in gangliosides and glycoproteins. J. Biol. Chem. 1983; 258: 11819-11822 © the American Society for Biochemistry and Molecular Biolog

    Deregulation of alternative splicing of fibronectin pre-mRNA in malignant human liver tumors

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    This research was originally published in the Journal of Biological Chemistry. F Oyama, S Hirohashi, Y Shimosato, K Titani and K Sekiguchi. Deregulation of alternative splicing of fibronectin pre-mRNA in malignant human liver tumors. J. Biol. Chem. 1989; 264: 10331-10334 © the American Society for Biochemistry and Molecular Biolog

    CD151 regulates epithelial cell–cell adhesion through PKC- and Cdc42-dependent actin cytoskeletal reorganization

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    CD151, a member of the tetraspanin family proteins, tightly associates with integrin α3β1 and localizes at basolateral surfaces of epithelial cells. We found that overexpression of CD151 in A431 cells accelerated intercellular adhesion, whereas treatment of cells with anti-CD151 mAb perturbed the integrity of cortical actin filaments and cell polarity. E-Cadherin puncta formation, indicative of filopodia-based adhesion zipper formation, as well as E-cadherin anchorage to detergent-insoluble cytoskeletal matrix, was enhanced in CD151-overexpressing cells. Levels of GTP-bound Cdc42 and Rac were also elevated in CD151-overexpressing cells, suggesting the role of CD151 in E-cadherin–mediated cell–cell adhesion as a modulator of actin cytoskeletal reorganization. Consistent with this possibility, engagement of CD151 by the substrate-adsorbed anti-CD151 mAb induced prominent Cdc42-dependent filopodial extension, which along with E-cadherin puncta formation, was strongly inhibited by calphostin C, a protein kinase C (PKC) inhibitor. Together, these results indicate that CD151 is involved in epithelial cell–cell adhesion as a modulator of PKC- and Cdc42-dependent actin cytoskeletal reorganization

    Mechanistic basis for the recognition of laminin-511 by α6β1 integrin

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    Mamoru Takizawa, Takao Arimori, Yukimasa Taniguchi, Yu Kitago, Erika Yamashita, Junichi Takagi and Kiyotoshi Sekiguchi, "Mechanistic basis for the recognition of laminin-511 by α6β1 integrin", Science Advances, Vol. 3, No. 9, e1701497, AAAS, 201

    Pretreatment with Perlecan-Conjugated Laminin-E8 Fragment Enhances Maturation of Grafted Dopaminergic Progenitors in Parkinson’s Disease Model

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    The therapeutic effect of a cell replacement therapy for Parkinson's disease (PD) depends on the proper maturation of grafted dopaminergic (DA) neurons and their functional innervation in the host brain. In the brain, laminin, an extracellular matrix protein, regulates signaling pathways for the survival and development of neurons by interacting with integrins. The heparan sulfate (HS) chain binds mildly to various neurotrophic factors and regulates their intracellular signaling. Perlecan-conjugated laminin 511/521-E8 fragments (p511/p521) were designed to contain an integrin-binding site and HS chains. Here we examined the effect of treating DA progenitors with p511/p521 prior to transplantation in rodent PD models. In vitro and in vivo experiments showed that p511/p521 treatment enhanced the maturation and neurite extension of the grafted DA progenitors by activating RAS-ERK1/2 signaling. This strategy will contribute to an efficient cell replacement therapy for PD in the future

    A novel cell adhesive protein engineered by insertion of the Arg-Gly-Asp-Ser tetrapeptide

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    This research was originally published in the Journal of Biological Chemistry. T Maeda, R Oyama, K Ichihara-Tanaka, F Kimizuka, I Kato, K Titani and K Sekiguchi. A novel cell adhesive protein engineered by insertion of the Arg-Gly-Asp-Ser tetrapeptide. J. Biol. Chem. 1989; 264: 15165-15168 © the American Society for Biochemistry and Molecular Biolog
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