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    Activation of the Syk tyrosine kinase is insufficient for downstream signal transduction in B lymphocytes.

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    Name:
    Activation of the Syk tyrosine ...
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    Genre
    Journal Article
    Date
    2002-12-06
    Author
    Hsueh, RC
    Hammill, AM
    Lee, JA
    Uhr, JW
    Scheuermann, RH
    Subject
    Amino Acid Substitution
    Animals
    Apoptosis
    B-Lymphocyte Subsets
    B-Lymphocytes
    Cell Division
    Cell Line, Tumor
    Cell Survival
    Cyclin D1
    Enzyme Activation
    Enzyme Precursors
    Gene Expression Regulation, Enzymologic
    Intracellular Signaling Peptides and Proteins
    Lymphoma, B-Cell
    Mice
    Mutation
    Phenylalanine
    Protein-Tyrosine Kinases
    Receptors, Antigen, B-Cell
    Signal Transduction
    Syk Kinase
    Tyrosine
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    Permanent link to this record
    http://hdl.handle.net/20.500.12613/5664
    
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    DOI
    10.1186/1471-2172-3-16
    Abstract
    BACKGROUND: Immature B lymphocytes and certain B cell lymphomas undergo apoptotic cell death following activation of the B cell antigen receptor (BCR) signal transduction pathway. Several biochemical changes occur in response to BCR engagement, including activation of the Syk tyrosine kinase. Although Syk activation appears to be necessary for some downstream biochemical and cellular responses, the signaling events that precede Syk activation remain ill defined. In addition, the requirements for complete activation of the Syk-dependent signaling step remain to be elucidated. RESULTS: A mutant form of Syk carrying a combination of a K395A substitution in the kinase domain and substitutions of three phenylalanines (3F) for the three C-terminal tyrosines was expressed in a murine B cell lymphoma cell line, BCL1.3B3 to interfere with normal Syk regulation as a means to examine the Syk activation step in BCR signaling. Introduction of this kinase-inactive mutant led to the constitutive activation of the endogenous wildtype Syk enzyme in the absence of receptor engagement through a 'dominant-positive' effect. Under these conditions, Syk kinase activation occurred in the absence of phosphorylation on Syk tyrosine residues. Although Syk appears to be required for BCR-induced apoptosis in several systems, no increase in spontaneous cell death was observed in these cells. Surprisingly, although the endogenous Syk kinase was enzymatically active, no enhancement in the phosphorylation of cytoplasmic proteins, including phospholipase Cgamma2 (PLCgamma2), a direct Syk target, was observed. CONCLUSION: These data indicate that activation of Syk kinase enzymatic activity is insufficient for Syk-dependent signal transduction. This observation suggests that other events are required for efficient signaling. We speculate that localization of the active enzyme to a receptor complex specifically assembled for signal transduction may be the missing event.
    Citation to related work
    Springer Science and Business Media LLC
    Has part
    BMC immunology [electronic resource]
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    ae974a485f413a2113503eed53cd6c53
    http://dx.doi.org/10.34944/dspace/5646
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