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Journal article

The beta1 and beta3 integrins promote T cell receptor-mediated cytotoxic T lymphocyte activation.

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  • 2003-04-12
Published in:
  • The Journal of biological chemistry. - 2003
Animals
CD8 Antigens
Calcium Signaling
Cell Adhesion
Cell Degranulation
Cell Line
Cytoskeletal Proteins
Cytotoxicity, Immunologic
Fibronectins
Focal Adhesion Kinase 2
H-2 Antigens
Integrin beta1
Integrin beta3
Lymphocyte Activation
Lymphocyte Specific Protein Tyrosine Kinase p56(lck)
Mice
Paxillin
Phosphoproteins
Protein-Tyrosine Kinases
Proto-Oncogene Proteins
Proto-Oncogene Proteins c-fyn
Receptor-CD3 Complex, Antigen, T-Cell
Receptors, Antigen, T-Cell
Signal Transduction
T-Lymphocytes, Cytotoxic
English Recognition by CD8+ cytotoxic T lymphocytes (CTLs) of antigenic peptides bound to major histocompatibility class (MHC) I molecules on target cells leads to sustained calcium mobilization and CTL degranulation resulting in perforin-dependent killing. We report that beta1 and beta3 integrin-mediated adhesion to extracellular matrix proteins on target cells and/or surfaces dramatically promotes CTL degranulation. CTLs, when adhered to fibronectin but not CTL in suspension, efficiently degranulate upon exposure to soluble MHC.peptide complexes, even monomeric ones. This adhesion induces recruitment and activation of the focal adhesion kinase Pyk2, the cytoskeleton linker paxillin, and the Src kinases Lck and Fyn in the contact site. The T cell receptor, by association with Pyk2, becomes part of this adhesion-induced activation cluster, which greatly increases its signaling.
Language
  • English
Open access status
bronze
Identifiers
Persistent URL
https://folia.unifr.ch/global/documents/290357
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