English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/169616
COMPARTIR / IMPACTO:
Estadísticas
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:
Título

Cooperative role for activated alpha 4 beta 1 integrin and chondroitin sulfate proteoglycans in cell adhesion to the heparin III domain of fibronectin - Identification of a novel heparin and cell binding sequence in repeat III5

AutorMoyano, José V.; Carnemolla, Barbara; Albar, Juan Pablo; Leprini, Alessandra; Gaggero, Barbara; Zardi, Luciano; García-Pardo, Angeles
Palabras claveHuman-plasma fibronectin
fn-c/h-v
Synthetic peptide
Monoclonal-antibody
Melanoma adhesion
Region
Recognition
Fibroblasts
Receptor
Progenitors
Fecha de publicación1-ene-1999
EditorAmerican Society for Biochemistry and Molecular Biology
CitaciónThe Journal of Biological Chemistry 274 (1)135-142 (1999)
ResumenWe recently reported that the heparin (Hep) III domain of fibronectin contains the H2 cell adhesion site in repeat III5 which binds activated α4 integrins. We have now further characterized the heparin and cell binding activities of this domain. A recombinant fragment containing repeats III4-III5 (FN-III4–5) induced Jurkat cell adhesion upon integrin activation with Mn2+ or TS2/16 monoclonal antibody (anti-β1). Adhesion of Mn2+-treated cells to FN-III4–5 or FN-III5 fragments was inhibited by chondroitinase ABC and ACII but not by the anti-α4 monoclonal antibody HP2/1. In contrast, HP2/1 completely blocked adhesion of TS2/16-treated cells while chondroitinase had a partial (FN-III4–5) or minor (FN-III5) effect. Thus, the role of each receptor depended on the stimulus used to activate α4β1. The combination of HP2/1 and chondroitinase at dilutions which did not inhibit when used individually abolished adhesion of Mn2+ or TS2/16-treated cells to both fragments, indicating a cooperative effect between α4β1 and chondroitin sulfate proteoglycans (CSPG). Furthermore, we have identified a 20-amino acid sequence in III5 (HBP/III5) which binds heparin and induces cell adhesion via CSPG exclusively. Although soluble HBP/III5 was a poor inhibitor, when combined with H2, it abolished adhesion to FN-III4–5 and FN-III5 fragments. These results establish that adhesion to the Hep III domain involves the cooperation of activated α4β1 and CSPG and show that HBP/III5 is a novel heparin and CSPG-binding site contributing to cell adhesion to this domain.
Descripción9 p.-9 fig.-1 tab.
Versión del editorhttp://dx.doi.org/10.1074/jbc.274.1.135
URIhttp://hdl.handle.net/10261/169616
DOI10.1074/jbc.274.1.135
ISSN0021-9258
E-ISSN1083-351X
Aparece en las colecciones: (CIB) Artículos
Ficheros en este ítem:
Fichero Descripción Tamaño Formato  
J. Biol. Chem.-1999-Moyano-135-42.pdfArtículo principal333,97 kBAdobe PDFVista previa
Visualizar/Abrir
Mostrar el registro completo
 

Artículos relacionados:


NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.