Abstract
B cell receptor (BCR) cross-linking induces tyrosine phosphorylation and activation of focal adhesion kinase (FAK), suggesting the role of this molecule in BCR-transduced signaling. The nature of FAK function in BCR-induced apoptosis of WEHI 231 lymphoblastoid cells was studied by overexpressing a C-terminal non-catalytic domain of FAK, termed focal adhesion targeted (FAT) domain. Clones overexpressing FAT protein exhibited a modified ability of induction of programmed cell death at low concentration threshold of anti-IgM antibodies, suggesting that FAK may play a role in modulating IgM-induced apoptotic signaling.
MeSH terms
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Antibodies, Anti-Idiotypic / pharmacology
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Apoptosis / physiology*
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B-Lymphocytes / cytology*
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B-Lymphocytes / enzymology*
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Focal Adhesion Kinase 1
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Focal Adhesion Protein-Tyrosine Kinases
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Gene Expression Regulation, Enzymologic
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Humans
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Immunoglobulin M / immunology
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Immunoglobulin M / metabolism
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Lymphoma, B-Cell
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Protein-Tyrosine Kinases / genetics
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Protein-Tyrosine Kinases / metabolism*
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Signal Transduction / physiology
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Tumor Cells, Cultured
Substances
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Antibodies, Anti-Idiotypic
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Immunoglobulin M
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anti-IgM
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Protein-Tyrosine Kinases
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Focal Adhesion Kinase 1
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Focal Adhesion Protein-Tyrosine Kinases
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PTK2 protein, human