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Related Collections Hemostasis, Thrombosis, and Vascular Biology Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, Vol. 93 No. 4 (February 15), 1999: pp. 1221-1230 Cooperative Activity of 41 and 47 Integrins in Mediating Human B-Cell Lymphoma Adhesion and Chemotaxis on Fibronectin Through Recognition of Multiple Synergizing Binding Sites Within the Central Cell-Binding Domain Zhinan Yin, Emiliana Giacomello, Elena Gabriele, Luciano Zardi, Shin-ichi Aota, Kenneth M. Yamada, Barbara Skerlavaji, Roberto Doliana, Alfonso Colombatti, and Roberto Perris From the Division for Experimental Oncology 2, Centro di Riferimento Oncologico Aviano, Istituto Nazionale Centroeuropeo, Aviano, Italy; the Department of Evolutionary and Functional Biology, University of Parma, Parma, Italy; the Istituto Nazionale per la Ricerca sul Cancro, Centro di Biotecnologie Avanzate, Genova, Italy; the Craniofacial Developmental Biology and Regeneration Branch, National Institute of Dental Research, National Institutes of Health, Bethesda, MD; and the Dipartimento di Scienze e Tecnologie Biomediche, University of Udine, Udine, Italy. We have quantitated the relative contributions of the constitutively active 41 and 47 integrins and the domains embodying their cognate binding sites in mediating human B-cell lymphoma adhesion and chemotaxis on fibronectin. By cooperating, the central cell-binding and IIICS carboxy-terminal domains were entirely responsible for the adhesion activity displayed by fibronectin, and their relative contribution to this process was estimated to be 30% versus 70%. Assessment of the leukocyte-substrate binding strength (ie, dynes/cell) indicated a 10-fold higher avidity of the cell-IIICS domain interaction. The two integrins interchangeably recognized both domains, but differed quantitatively in their participation in the adhesive event, as well as in domain preference. The use of 3Fn (according to the nomenclature proposed by Bork and Koonin [Curr Opin Struct Biol 6:366, 1996] for the type III fibronectin modules) module-specific antibodies and recombinant polypeptides showed that 4 integrins recognized both the RGD sequence (3Fn10) and an apparently novel synergistic site located within the 3Fn8 module; even in this case, the integrins displayed a distinct binding site preference. Interleukin-1 (IL-1)/IL-2-induced chemotaxis also involved cooperative function of the central cell-binding and IIICS domains, but the mechanisms regulating this phenomenon differed markedly from those controlling cell adhesion. First, the relative contribution of the individual domains was comparable, but neither of the individual domains promoted migration to the extent observed on intact fibronectin. Secondly, 41 and 47 integrins were both involved in the domain-binding necessary for initiation of migration, but the relative contribution of each receptor in the chemotactic process was less disparate than for initial cell adhesion. Thirdly, the mode by which chemotactic B-lymphoma movement was supported by the central cell-binding domain differed from that sustaining cell adhesion in that it involved independent recognition of either the 3Fn8 or the 3Fn9 module, which acted in synergy with the 3Fn10 module. Our data provide novel evidence concerning the relative importance of the constitutively active 41 and 47 integrins for the interaction of B-cell lymphoma cells with fibronectin, and they emphasize a multiple and diverse recognition of sites responsible for either anchorage or locomotion of tumor leukocytes on this matrix molecule. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: A. L. Gonzalez, W. El-Bjeirami, J. L. West, L. V. McIntire, and C. W. Smith Transendothelial migration enhances integrin-dependent human neutrophil chemokinesis J. Leukoc. Biol., March 1, 2007; 81(3): 686 - 695. [Abstract] [Full Text] [PDF] C. G. Lo, T. T. Lu, and J. G. Cyster Integrin-dependence of Lymphocyte Entry into the Splenic White Pulp J. Exp. Med., February 3, 2003; 197(3): 353 - 361. [Abstract] [Full Text] [PDF] H. Altroff, L. Choulier, and H. J. 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