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© The Rockefeller University Press, 0021-9525/1999//777 $5.00
The Journal of Cell Biology, Volume 144, Number 4, , 1999 777-788

Regular Articles

Matrix Valency Regulates Integrin-mediated Lymphoid Adhesion via Syk Kinase



Dwayne G. Stupack*, Erguang Li*, Steve A. Silletti*, Jacqueline A. Kehler*, Robert L. Geahlen{ddagger}, Klaus Hahn§, Glen R. Nemerow*, and David A. Cheresh*,||

* Department of Immunology, § Department of Cell Biology, and || Department of Vascular Biology, The Scripps Research Institute, La Jolla, California 92037; and {ddagger} Department of Medicinal Chemistry and Pharmacology, Purdue University, West Lafayette, Indiana 47907

Lymphocytes accumulate within the extracellular matrix (ECM) of tumor, wound, or inflammatory tissues. These tissues are largely comprised of polymerized adhesion proteins such as fibrin and fibronectin or their fragments. Nonactivated lymphoid cells attach preferentially to polymerized ECM proteins yet are unable to attach to monomeric forms or fragments of these proteins without previous activation. This adhesion event depends on the appropriate spacing of integrin adhesion sites. Adhesion of nonactivated lymphoid cells to polymeric ECM components results in activation of the antigen receptor-associated Syk kinase that accumulates in adhesion-promoting podosomes. In fact, activation of Syk by antigen or agonists, as well as expression of an activated Syk mutant in lymphoid cells, facilitates their adhesion to monomeric ECM proteins or their fragments. These results reveal a cooperative interaction between signals emanating from integrins and antigen receptors that can serve to regulate stable lymphoid cell adhesion and retention within a remodeling ECM.

Key Words: integrin • lymphocyte • extracellular matrix • protein tyrosine kinase • cell adhesion

Abbreviations used in this paper: CTL, cytotoxic lymphocyte; ECM, extracellular matrix; LCL, lymphoblastoid cell line; LCMV, lymphocytic choriomenginitis virus; LIBS, ligand-induced binding site; MAP kinase, mitogen-activated protein kinase; PB, penton base; PE, phycoerythrin; PI(3)K, phosphoinositide-3-kinase.


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