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Cyr61/CCN1 Displays High-Affinity Binding to the Somatomedin B (1-44) Domain of Vitronectin
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SYSNO ASEP 0346232 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Cyr61/CCN1 Displays High-Affinity Binding to the Somatomedin B (1-44) Domain of Vitronectin Tvůrce(i) Francischetti, I.M.B. (US)
Kotsyfakis, Michalis (BC-A) RID, ORCID
Andersen, J. F. (US)
Lukszo, J. (US)Zdroj.dok. PLoS ONE. - : Public Library of Science - ISSN 1932-6203
Roč. 5, č. 2 (2010), e9356Poč.str. 12 s. Jazyk dok. eng - angličtina Země vyd. US - Spojené státy americké Klíč. 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 Vědní obor RIV GJ - Choroby a škůdci zvířat, veterinární medicína CEZ AV0Z60220518 - PAU-O, BC-A (2005-2011) UT WOS 000274997000003 DOI 10.1371/journal.pone.0009356 Anotace 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. Pracoviště Biologické centrum (od r. 2006) Kontakt Dana Hypšová, eje@eje.cz, Tel.: 387 775 214 Rok sběru 2011
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