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Matrix valency regulates integrin-mediated lymphoid adhesion via syk kinase

Academic Article
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Overview

authors

  • Stupack, D. G.
  • Li, E. G.
  • Silletti, S. A.
  • Kehler, J. A.
  • Geahien, R. L.
  • Hahn, K.
  • Nemerow, Glen
  • Cheresh, D. A.

publication date

  • February 1999

journal

  • Journal of Cell Biology  Journal

abstract

  • 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.

subject areas

  • Cell Adhesion
  • Cell Line
  • Enzyme Precursors
  • Extracellular Matrix
  • Humans
  • Inflammation
  • Integrins
  • Intracellular Signaling Peptides and Proteins
  • Ligands
  • Lymphocytes
  • Neoplasms
  • Protein-Tyrosine Kinases
  • Signal Transduction
  • Wound Healing
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Research

keywords

  • cell adhesion
  • extracellular matrix
  • integrin
  • lymphocyte
  • protein tyrosine kinase
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Identity

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.144.4.777

PubMed ID

  • 10037798
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Additional Document Info

start page

  • 777

end page

  • 787

volume

  • 144

issue

  • 4

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