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  • 1
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    TCR-induced transmembrane signaling by peptide/MHC class II via associated Ig-alpha/beta dimers (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-02-27
    Description: Previous findings suggest that during cognate T cell-B cell interactions, major histocompatability complex (MHC) class II molecules transduce signals, leading to Src-family kinase activation, Ca2+ mobilization, and proliferation. Here, we show that antigen stimulation of resting B cells induces MHC class II molecules to associate with Immunoglobulin (Ig)-alpha/Ig-beta (CD79a/CD79b) heterodimers, which function as signal transducers upon MHC class II aggregation by the T cell receptor (TCR). The B cell receptor (BCR) and MHC class II/Ig-alpha/Ig-beta are distinct complexes, yet class II-associated Ig-alpha/beta appears to be derived from BCR. Hence, Ig-alpha/beta are used in a sequential fashion for transduction of antigen and cognate T cell help signals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lang, P -- Stolpa, J C -- Freiberg, B A -- Crawford, F -- Kappler, J -- Kupfer, A -- Cambier, J C -- AI 20519/AI/NIAID NIH HHS/ -- AI 22295/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2001 Feb 23;291(5508):1537-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Integrated Department of Immunology, University of Colorado Health Sciences Center, and National Jewish Medical and Research Center, 1400 Jackson Street, Denver, CO 80206, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11222857" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens/immunology ; Antigens, CD/*metabolism ; Antigens, CD79 ; B-Lymphocytes/*immunology/metabolism ; Cells, Cultured ; Dimerization ; Enzyme Activation ; Histocompatibility Antigens Class II/immunology/*metabolism ; Immunoblotting ; Lymphocyte Activation ; Mice ; Mice, Transgenic ; Phosphorylation ; Phosphotyrosine/metabolism ; Precipitin Tests ; Protein-Tyrosine Kinases/metabolism ; Receptors, Antigen, B-Cell/immunology/*metabolism ; Receptors, Antigen, T-Cell/immunology/*metabolism ; *Signal Transduction ; T-Lymphocytes/immunology/metabolism ; Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    B cell antigen receptor signaling: roles in cell development and disease (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-01
    Description: Signals propagated through the B cell antigen receptor (BCR) are vital for the development and survival of B lymphocytes in both the bone marrow and the periphery. These signals not only guide maturation and activation but also affect the removal of potentially self-reactive B lymphocytes. Interestingly, these signals are known to be either ligand-independent ("tonic" signals) or induced by ligand (antigen) binding to the BCR. We focus on the problems that occur in B cell development due to defects in signals emanating from the BCR. In addition, we present the B Cell Antigen Receptor Pathway, an STKE Connections Map that illustrates the events involved in B cell signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gauld, Stephen B -- Dal Porto, Joseph M -- Cambier, John C -- New York, N.Y. -- Science. 2002 May 31;296(5573):1641-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Integrated Department of Immunology, University of Colorado Health Sciences Center, and National Jewish Medical Research Center, 1400 Jackson Street, Denver, CO 80206, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12040177" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD19/metabolism ; Autoimmune Diseases/immunology ; B-Lymphocytes/*immunology/metabolism/physiology ; Humans ; Immunologic Deficiency Syndromes/immunology ; Lymphocyte Activation ; Phosphorylation ; Protein-Tyrosine Kinases/metabolism ; Receptors, Antigen, B-Cell/chemistry/*metabolism ; *Signal Transduction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    The B cell antigen receptor complex: association of Ig-alpha and Ig-beta with distinct cytoplasmic effectors (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-10-02
    Description: The B cell antigen receptor complex is a hetero-oligomeric structure composed of antigen binding, membrane immunoglobulin, and transducer-transporter substructures. The transducer-transporter substructure is composed of disulfide-linked dimers of immunoglobulin (Ig)-alpha and Ig-beta/gamma subunits that are products of the mb-1(alpha) and B29 (beta/gamma) genes. Although the receptor complex associates with Src family kinases that are activated after receptor ligation, the site of interaction of these and other cytoplasmic effector molecules with receptor subunits is unknown. The cytoplasmic tails of Ig-alpha and Ig-beta chains were found to associate with distinct sets of effector molecules. The Ig-alpha chain cytoplasmic domain bound to the Src family kinases Lyn and Fyn, phosphatidylinositol-3 kinase (PI-3 kinase), and an unidentified 38-kilodalton phosphoprotein; the cytoplasmic tail of Ig-beta bound PI-3 kinase and unidentified 40- and 42-kilodalton phosphoproteins. Binding activity was found to occur within a 26-amino acid sequence of Ig-alpha and Ig-beta that contains a motif [(Asp or Glu)-(any amino acid)7-(Asp or Glu)-Tyr-(any amino acid)3-Leu-(any amino acid)7-Tyr-(any amino acid)2-(Leu or Ile)] previously implicated in signal transduction via other receptors including the Fc epsilon receptor I and the T cell antigen receptor. These findings indicate that the subunits act independently to activate distinct second messenger pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clark, M R -- Campbell, K S -- Kazlauskas, A -- Johnson, S A -- Hertz, M -- Potter, T A -- Pleiman, C -- Cambier, J C -- AI20519/AI/NIAID NIH HHS/ -- AI21768/AI/NIAID NIH HHS/ -- AR01864/AR/NIAMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1992 Oct 2;258(5079):123-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Basic Sciences, National Jewish Center for Immunology and Respiratory Medicine, Denver, CO 80206.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1439759" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigens, CD/*metabolism ; Antigens, CD79 ; Base Sequence ; Cytoplasm/*metabolism ; Electrophoresis, Polyacrylamide Gel ; Genes, src ; Humans ; Immunoblotting ; Immunoglobulin M/*metabolism ; Molecular Sequence Data ; Polymerase Chain Reaction ; Protein Kinases/metabolism ; Receptors, Antigen, B-Cell/*metabolism ; Recombinant Fusion Proteins ; Signal Transduction/physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Regulation of B cell antigen receptor signal transduction and phosphorylation by CD45 (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-06-28
    Description: CD45 is a member of a family of membrane proteins that possess phosphotyrosine phosphatase activity, and is the source of much of the tyrosine phosphatase activity in lymphocytes. In view of its enzymatic activity and high copy number, it seems likely that CD45 functions in transmembrane signal transduction by lymphocyte receptors that are coupled to activation of tyrosine kinases. The B cell antigen receptor was found to transduce a Ca(2+)-mobilizing signal only if cells expressed CD45. Also, both membrane immunoglobulin M (mIgM) and CD45 were lost from the surface of cells treated with antibody to CD45, suggesting a physical interaction between these proteins. Finally, CD45 dephosphorylated a complex of mIg-associated proteins that appears to function in signal transduction by the antigen receptor. These data indicate that CD45 occurs as a component of a complex of proteins associated with the antigen receptor, and that CD45 may regulate signal transduction by modulating the phosphorylation state of the antigen receptor subunits.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Justement, L B -- Campbell, K S -- Chien, N C -- Cambier, J C -- AI20519/AI/NIAID NIH HHS/ -- AI21768/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1991 Jun 28;252(5014):1839-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, National Jewish Center for Immunology and Respiratory Medicine, Denver, CO.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1648262" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD45 ; Antigens, Differentiation/genetics/*physiology ; B-Lymphocytes/*immunology ; Calcium/physiology ; Cell Line ; Cell Membrane/physiology ; Cells, Cultured ; Clone Cells ; Histocompatibility Antigens/genetics/*physiology ; Immunoglobulin M/physiology ; Membrane Glycoproteins/*physiology ; Mice ; Phosphoprotein Phosphatases/metabolism ; Phosphorylation ; Plasmacytoma ; Protein Tyrosine Phosphatases ; RNA, Messenger/genetics ; Receptors, Antigen, B-Cell/*physiology ; *Signal Transduction ; Spleen/immunology ; Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Promotion of B cell immune responses via an alum-induced myeloid cell population (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-06-19
    Description: Exposure of naive B cells to the cytokine interleukin-4 (IL-4) and/or antigen leads to a state of "priming," in which subsequent aggregation of major histocompatibility complex class II molecules induces the mobilization of calcium ions and cell proliferation. However, it is not clear how critical this priming is for immune responses or how it is normally induced in vivo. Injection of mice with the commonly used adjuvant alum led to priming of splenic B cells and to the accumulation in the spleen of a previously unknown population of IL-4-producing, Gr1+ cells. These cells and IL-4 were both required for in vivo priming and expansion of antigen-specific B cells, as well as for optimal production of antibody. These studies reveal a key role for a previously unknown accessory myeloid cell population in the generation of humoral immune responses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jordan, Michael B -- Mills, David M -- Kappler, John -- Marrack, Philippa -- Cambier, John C -- AI-17134/AI/NIAID NIH HHS/ -- AI-18785/AI/NIAID NIH HHS/ -- AI-20519/AI/NIAID NIH HHS/ -- AI-22295/AI/NIAID NIH HHS/ -- AI-50802/AI/NIAID NIH HHS/ -- AI-52225/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2004 Jun 18;304(5678):1808-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Integrated Department of Immunology, National Jewish Medical and Research Center, University of Colorado Health Sciences Center, 1400 Jackson Street, Denver, CO 80206, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15205534" target="_blank"〉PubMed〈/a〉
    Keywords: *Adjuvants, Immunologic ; Adoptive Transfer ; *Alum Compounds/administration & dosage ; Animals ; B-Lymphocytes/*immunology ; Calcium/metabolism ; Cell Separation ; Cells, Cultured ; Coculture Techniques ; Eosinophils/cytology/immunology ; Freund's Adjuvant ; Granulocyte-Macrophage Colony-Stimulating Factor/pharmacology ; Histocompatibility Antigens Class II/immunology ; Immunization ; Interleukin-4/immunology/metabolism ; Lymphocyte Activation ; Mice ; Mice, Inbred C57BL ; Myeloid Cells/*immunology ; Nitrophenols/immunology ; Serum Albumin, Bovine/immunology ; Signal Transduction ; Spleen/cytology/immunology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Recruitment and activation of PTP1C in negative regulation of antigen receptor signaling by Fc gamma RIIB1 (1995)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1995-04-14
    Description: Coligation of the Fc receptor on B cells, Fc gamma RIIB1, with the B cell antigen receptor (BCR) leads to abortive BCR signaling. Here it was shown that the Fc gamma RIIB1 recruits the phosphotyrosine phosphatase PTP1C after BCR coligation. This association is mediated by the binding of a 13-amino acid tyrosine-phosphorylated sequence to the carboxyl-terminal Src homology 2 domain of PTP1C and activates PTP1C. Inhibitory signaling and PTP1C recruitment are dependent on the presence of the tyrosine within the 13-amino acid sequence. Inhibitory signaling mediated by Fc gamma RIIB1 is deficient in motheaten mice which do not express functional PTP1C. Thus, PTP1C is an effector of BCR-Fc gamma RIIB1 negative signal cooperativity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉D'Ambrosio, D -- Hippen, K L -- Minskoff, S A -- Mellman, I -- Pani, G -- Siminovitch, K A -- Cambier, J C -- New York, N.Y. -- Science. 1995 Apr 14;268(5208):293-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, National Jewish Center for Immunology and Respiratory Medicine, Denver, CO 80206, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7716523" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibody Formation ; *Antigens, CD ; B-Lymphocytes/*immunology/metabolism ; Binding Sites ; Calcium/metabolism ; Intracellular Signaling Peptides and Proteins ; Mice ; Mice, Mutant Strains ; Molecular Sequence Data ; Phosphorylation ; Protein Tyrosine Phosphatase, Non-Receptor Type 11 ; Protein Tyrosine Phosphatase, Non-Receptor Type 6 ; Protein Tyrosine Phosphatases/*metabolism ; Receptors, Antigen, B-Cell/*metabolism ; Receptors, IgG/*metabolism ; *Signal Transduction ; Tumor Cells, Cultured
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    Activation of phosphatidylinositol-3' kinase by Src-family kinase SH3 binding to the p85 subunit (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-03-18
    Description: Engagement of antigen receptor complexes induces rapid activation of Src-family kinases and association with phosphatidylinositol-3' kinase (PI-3 kinase). Here it was found that the Src homology 3 (SH3) domain of Lyn and Fyn bound to a proline-rich region (residues 84 to 99) within the 85-kilodalton subunit (p85) of PI-3 kinase. The binding of SH3 to the purified kinase led to a five- to sevenfold increase in the specific activity of PI-3 kinase. Ligand-induced receptor stimulation activated PI-3 kinase, and this activation was blocked by a peptide containing residues 84 to 99 of p85. These data demonstrate a mechanism for PI-3 kinase activation and show that binding of SH3 domains to proline-rich target sequences can regulate enzymatic activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pleiman, C M -- Hertz, W M -- Cambier, J C -- A120519/PHS HHS/ -- A121768/PHS HHS/ -- A129903/PHS HHS/ -- New York, N.Y. -- Science. 1994 Mar 18;263(5153):1609-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, National Jewish Center for Immunology and Respiratory Medicine, Denver, CO 80206.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8128248" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; B-Lymphocytes/*enzymology ; Enzyme Activation ; Lymphocyte Activation ; Mice ; Molecular Sequence Data ; Peptide Fragments/pharmacology ; Phosphatidylinositol 3-Kinases ; Phosphotransferases (Alcohol Group Acceptor)/chemistry/*metabolism ; Proline/chemistry ; Protein-Tyrosine Kinases/chemistry/*metabolism ; Proto-Oncogene Proteins/chemistry/*metabolism ; Proto-Oncogene Proteins c-fyn ; *src-Family Kinases
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    B cell receptor signal transduction in the GC is short-circuited by high phosphatase activity (2012)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2012-05-05
    Description: Germinal centers (GCs) generate memory B and plasma cells, which are essential for long-lived humoral immunity. GC B cells with high-affinity B cell receptors (BCRs) are selectively expanded. To enable this selection, BCRs of such cells are thought to signal differently from those with lower affinity. We show that, surprisingly, most proliferating GC B cells did not demonstrate active BCR signaling. Rather, spontaneous and induced signaling was limited by increased phosphatase activity. Accordingly, both SH2 domain-containing phosphatase-1 (SHP-1) and SH2 domain-containing inositol 5 phosphatase were hyperphosphorylated in GC cells and remained colocalized with BCRs after ligation. Furthermore, SHP-1 was required for GC maintenance. Intriguingly, GC B cells in the cell-cycle G(2) period regained responsiveness to BCR stimulation. These data have implications for how higher-affinity B cells are selected in the GC.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3777391/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3777391/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Khalil, Ashraf M -- Cambier, John C -- Shlomchik, Mark J -- AI43603/AI/NIAID NIH HHS/ -- AR44077/AR/NIAMS NIH HHS/ -- R01 AI043603/AI/NIAID NIH HHS/ -- R01 AR044077/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 2012 Jun 1;336(6085):1178-81. doi: 10.1126/science.1213368. Epub 2012 May 3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Laboratory Medicine, Yale University School of Medicine, New Haven, CT 06520, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22555432" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibody Affinity ; Antigen Presentation ; Antigens/immunology ; Antigens, CD79/metabolism ; B-Lymphocytes/enzymology/*immunology/metabolism ; Calcium/metabolism ; Cell Cycle ; Down-Regulation ; Germinal Center/cytology/*immunology ; Intracellular Signaling Peptides and Proteins/metabolism ; Lymphocyte Activation ; Mice ; Mice, Inbred BALB C ; Mice, Transgenic ; Models, Immunological ; Phosphoric Monoester Hydrolases/metabolism ; Phosphorylation ; Protein Tyrosine Phosphatase, Non-Receptor Type 6/*metabolism ; Protein-Tyrosine Kinases/metabolism ; Receptors, Antigen, B-Cell/*immunology/*metabolism ; Signal Transduction
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
    Electronic Resource
    Electronic Resource
    Signal Transduction by the B Cell Antigen Receptor and its Coreceptors (1994)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Immunology 12 (1994), S. 457-486 
    Details
    ISSN: 0732-0582
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.iy.12.040194.002325
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  • 10
    Electronic Resource
    Electronic Resource
    Molecular Mechanisms of Transmembrane Signaling in B Lymphocytes (1987)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Immunology 5 (1987), S. 175-199 
    Details
    ISSN: 0732-0582
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.iy.05.040187.001135
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