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J Biol Chem, Vol. 274, Issue 1, 135-142, January 1, 1999

Cooperative Role for Activated 41 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

José V. Moyano, Barbara Carnemolla^¶, Juan P. Albar, Alessandra Leprini^¶, Barbara Gaggero^¶, Luciano Zardi^¶, and Angeles Garcia-Pardo

From the  Departamento de Inmunología, Centro de Investigaciones Biológicas, CSIC, 28006 Madrid, Spain, the ^¶ Laboratory of Cell Biology, Istituto Nazionale per la Ricerca sul Cancro, 16132 Genoa, Italy, and the  Departamento de Inmunología y Oncología, Centro Nacional de Biotecnología, CSIC, 28049 Madrid, Spain

We recently reported that the heparin (Hep) III domain of fibronectin contains the H2 cell adhesion site in repeat III5 which binds activated 4 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-1). 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-4 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 41. 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 41 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 41 and CSPG and show that HBP/III5 is a novel heparin and CSPG-binding site contributing to cell adhesion to this domain.

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Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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