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  1. Article ; Online: Identification of the Axis β-Catenin–BTK in the Dynamic Adhesion of Chronic Lymphocytic Leukemia Cells to Their Microenvironment

    Imane Mihoub / Tareck Rharass / Souhaïl Ouriemmi / Antonin Oudar / Laure Aubard / Valérie Gratio / Gregory Lazarian / Jordan Ferreira / Elisabetta Dondi / Florence Cymbalista / Vincent Levy / Fanny Baran-Marszak / Nadine Varin-Blank / Dominique Ledoux / Christine Le Roy / Laura Gardano

    International Journal of Molecular Sciences, Vol 24, Iss 24, p

    2023  Volume 17623

    Abstract: In the microenvironment, cell interactions are established between different cell types to regulate their migration, survival and activation. β-Catenin is a multifunctional protein that stabilizes cell–cell interactions and regulates cell survival ... ...

    Abstract In the microenvironment, cell interactions are established between different cell types to regulate their migration, survival and activation. β-Catenin is a multifunctional protein that stabilizes cell–cell interactions and regulates cell survival through its transcriptional activity. We used chronic lymphocytic leukemia (CLL) cells as a cellular model to study the role of β-catenin in regulating the adhesion of tumor cells to their microenvironment, which is necessary for tumor cell survival and accumulation. When co-cultured with a stromal cell line (HS-5), a fraction of the CLL cells adhere to stromal cells in a dynamic fashion regulated by the different levels of β-catenin expression. In non-adherent cells, β-catenin is stabilized in the cytosol and translocates into the nucleus, increasing the expression of cyclin D1. In adherent cells, the level of cytosolic β-catenin is low but membrane β-catenin helps to stabilize the adhesion of CLL to stromal cells. Indeed, the overexpression of β-catenin enhances the interaction of CLL with HS-5 cells, suggesting that this protein behaves as a regulator of cell adhesion to the stromal component and of the transcriptional regulation of cell survival. Inhibitors that block the stabilization of β-catenin alter this equilibrium and effectively disrupt the support that CLL cells receive from the cross-talk with the stroma.
    Keywords β-catenin ; microenvironment ; CLL ; BTK ; stromal cells ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
    Subject code 570
    Language English
    Publishing date 2023-12-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article ; Online: Extracellular matrix metalloproteinase inducer (EMMPRIN/CD147) as a novel regulator of myogenic cell differentiation.

    Attia, Mohamed / Mohamed, Attia / Huet, Eric / Eric, Huet / Delbé, Jean / Jean, Delbé / Ledoux, Dominique / Dominique, Ledoux / Menashi, Suzanne / Suzanne, Menashi / Martelly, Isabelle / Isabelle, Martelly

    Journal of cellular physiology

    2011  Volume 226, Issue 1, Page(s) 141–149

    Abstract: Matrix metalloproteinases (MMPs) are thought to play an important role in skeletal muscle cell growth and differentiation. In view of the MMP inducing function of EMMPRIN/CD147, its role in myogenic cell differentiation was investigated. EMMPRIN level ... ...

    Abstract Matrix metalloproteinases (MMPs) are thought to play an important role in skeletal muscle cell growth and differentiation. In view of the MMP inducing function of EMMPRIN/CD147, its role in myogenic cell differentiation was investigated. EMMPRIN level increased during differentiation of both rat primary myoblasts derived from satellite cells and mouse C2.7 myogenic cells and was associated with an alteration in its molecular forms. In parallel, expression of pro-MMP-9 gradually decreased and that of pro-MMP-2 and active MMP-2 increased. While small interfering RNA (siRNA) inhibition of EMMPRIN expression accelerated cell differentiation, exogenously added recombinant EMMPRIN inhibited differentiation by an MMP-mediated mechanism, as the MMP inhibitor marimastat abrogated EMMPRIN's effect. Our results further suggest that EMMPRIN regulates differentiation through an MMP activation of transforming growth factor beta (TGFβ), a known inhibitor of myoblast's differentiation, as the increased activation and signaling of TGFβ by EMMPRIN was attenuated in the presence of marimastat. EMMPRIN inhibition may thus represent a novel strategy in the treatment of muscular degenerative disorders.
    MeSH term(s) Animals ; Basigin/genetics ; Basigin/metabolism ; Cell Differentiation/physiology ; Cell Line ; Cells, Cultured ; Enzyme Induction ; Extracellular Matrix/enzymology ; Extracellular Matrix/physiology ; Gene Silencing ; Matrix Metalloproteinases/biosynthesis ; Matrix Metalloproteinases/genetics ; Matrix Metalloproteinases/metabolism ; Mice ; Muscle Development/physiology ; Myoblasts/cytology ; Myoblasts/physiology ; RNA, Small Interfering/metabolism ; Rats ; Rats, Wistar ; Satellite Cells, Skeletal Muscle/cytology ; Satellite Cells, Skeletal Muscle/physiology ; Transforming Growth Factor beta/metabolism
    Chemical Substances RNA, Small Interfering ; Transforming Growth Factor beta ; Basigin (136894-56-9) ; Matrix Metalloproteinases (EC 3.4.24.-)
    Language English
    Publishing date 2011-01
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 3116-1
    ISSN 1097-4652 ; 0021-9541
    ISSN (online) 1097-4652
    ISSN 0021-9541
    DOI 10.1002/jcp.22315
    Database MEDical Literature Analysis and Retrieval System OnLINE

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