Počet záznamů: 1

Cyr61/CCN1 Displays High-Affinity Binding to the Somatomedin B (1-44) Domain of Vitronectin

  1. 1.
    0346232 - BC-A 2011 RIV US eng J - Článek v odborném periodiku
    Francischetti, I.M.B. - Kotsyfakis, Michalis - Andersen, J. F. - Lukszo, J.
    Cyr61/CCN1 Displays High-Affinity Binding to the Somatomedin B (1-44) Domain of Vitronectin.
    PLoS ONE. Roč. 5, č. 2 (2010), e9356 E-ISSN 1932-6203
    Výzkumný záměr: CEZ:AV0Z60220518
    Klíčová slova: PLASMINOGEN-ACTIVATOR INHIBITOR-1 * UROKINASE RECEPTOR * EXTRACELLULAR-MATRIX * CELL-ADHESION * CCN FAMILY * INTEGRIN ALPHA-V-BETA-3 * IXODES-SCAPULARIS * SALIVARY-GLAND * MELANOMA-CELLS * EXPRESSION
    Kód oboru RIV: GJ - Choroby a škůdci zvířat, veterinární medicína
    Impakt faktor: 4.411, rok: 2010

    Cyr61 is a member of the CCN (Cyr61, connective tissue growth, NOV) family of extracellular-associated (matricellular) proteins that present four distinct functional modules, namely insulin-like growth factor binding protein (IGFBP), von Willebrand factor type C (vWF), thrombospondin type 1 (TSP), and C-terminal growth factor cysteine knot (CT) domain. While heparin sulphate proteoglycans reportedly mediate the interaction of Cyr61 with the matrix and cell surface, the role of other extracellular associated proteins has not been revealed. Conclusions: The finding that Cyr61 interacts with the SMTB (1-44) domain suggests that VTNC represent a point of anchorage for CCN family members to the matrix. Results are discussed in the context of the role of CCN and VTNC in matrix biology and angiogenesis.
    Trvalý link: http://hdl.handle.net/11104/0187305