Selective Regulation of Lyn Tyrosine Kinase by CD45 in Immature B Cells
Autor: | Mami Ogimoto, Kiminori Hasegawa, Hidetaka Yakura, Kazuya Mizuno, Tatsuo Katagiri |
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Rok vydání: | 1995 |
Předmět: |
B-cell receptor
Phosphatase Gene Expression Receptors Antigen B-Cell Syk Biology Biochemistry Cell Line Substrate Specificity Mice chemistry.chemical_compound LYN Animals Homeostasis Syk Kinase Molecular Biology B-Lymphocytes Enzyme Precursors Kinase Intracellular Signaling Peptides and Proteins hemic and immune systems Tyrosine phosphorylation Cell Biology Protein-Tyrosine Kinases Cell biology Kinetics src-Family Kinases chemistry Leukocyte Common Antigens Signal transduction Tyrosine kinase |
Zdroj: | Journal of Biological Chemistry. 270:27987-27990 |
ISSN: | 0021-9258 |
Popis: | It has been well established that protein-tyrosine phosphatase CD45 is critically involved in the regulation of initial tyrosine phosphorylation and effector functions of T and B cells. However, the signaling pathway governed by CD45 is not completely understood. In B cells, it has not been unequivocally resolved as to which protein-tyrosine kinases (PTKs) associated with B cell antigen receptor are regulated by CD45 in intact cells. As a first step toward the elucidation of CD45-initiated signaling events, we have tried to identify physiological substrates for CD45 by analyzing PTK activity in CD45-deficient clones recently generated from the immature B cell line WEHI-231. The results clearly demonstrated that among PTKs examined (Lyn, Lck, and Syk), only Lyn kinase is dysregulated in the absence of CD45 such that without B cell antigen receptor ligation, Lyn is hyperphosphorylated and activated in CD45-negative clones. Thus, Lyn seems to be a selective in vivo substrate for CD45 in immature B cells. |
Databáze: | OpenAIRE |
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