scholarly journals Stimulation of the B Cell Receptor, CD86 (B7-2), and the β2-Adrenergic Receptor Intrinsically Modulates the Level of IgG1 and IgE Produced per B Cell

2000 ◽  
Vol 165 (2) ◽  
pp. 680-690 ◽  
Author(s):  
Deborah J. Kasprowicz ◽  
Adam P. Kohm ◽  
Michael T. Berton ◽  
Andrezj J. Chruscinski ◽  
Arlene Sharpe ◽  
...  
Keyword(s):  
B Cell ◽  
Adrenergic Receptor ◽  
Cell Receptor ◽  
B Cell Receptor ◽  
Β2 Adrenergic Receptor ◽  
Stimulation Of

scholarly journals B Cell Receptor- and β2-Adrenergic Receptor-Induced Regulation of B7-2 (CD86) Expression in B Cells

2002 ◽  
Vol 168 (12) ◽  
pp. 6314-6322 ◽  
Author(s):  
Adam P. Kohm ◽  
Afsaneh Mozaffarian ◽  
Virginia M. Sanders
Keyword(s):  
B Cells ◽  
B Cell ◽  
Adrenergic Receptor ◽  
Cell Receptor ◽  
B Cell Receptor ◽  
Β2 Adrenergic Receptor

scholarly journals Stimulation of the B-cell receptor activates the JAK2/STAT3 signaling pathway in chronic lymphocytic leukemia cells

Blood ◽  
2014 ◽  
Vol 123 (24) ◽  
pp. 3797-3802 ◽  
Author(s):  
Uri Rozovski ◽  
Ji Yuan Wu ◽  
David M. Harris ◽  
Zhiming Liu ◽  
Ping Li ◽  
...  
Keyword(s):  
Chronic Lymphocytic Leukemia ◽  
B Cell ◽  
Cell Receptor ◽  
B Cell Receptor ◽  
Lymphocytic Leukemia ◽  
Leukemia Cells ◽  
Stat3 Signaling ◽  
Stat3 Signaling Pathway ◽  
Key Points ◽  
Stimulation Of

Key Points Stimulation of the BCR activates JAK2 and STAT3 in CLL cells. The JAK1/2 inhibitor ruxolitinib induces apoptosis of CLL cells.

scholarly journals B cell activator PAX5 promotes lymphomagenesis through stimulation of B cell receptor signaling

2007 ◽  
Vol 117 (9) ◽  
pp. 2602-2610 ◽  
Author(s):  
Diana Cozma ◽  
Duonan Yu ◽  
Suchita Hodawadekar ◽  
Anna Azvolinsky ◽  
Shannon Grande ◽  
...  
Keyword(s):  
B Cell ◽  
Cell Receptor ◽  
B Cell Receptor ◽  
Receptor Signaling ◽  
B Cell Receptor Signaling ◽  
Cell Activator ◽  
Cell Receptor Signaling ◽  
Stimulation Of

CD24 and IgM Stimulation of B Cells Triggers Transfer of Functional B Cell Receptor to B Cell Recipients Via Extracellular Vesicles

2021 ◽  
pp. ji2100025
Author(s):  
Hong-Dien Phan ◽  
Modeline N. Longjohn ◽  
Delania J. B. Gormley ◽  
Reilly H. Smith ◽  
May Dang-Lawson ◽  
...  
Keyword(s):  
B Cells ◽  
B Cell ◽  
Extracellular Vesicles ◽  
Cell Receptor ◽  
B Cell Receptor ◽  
Stimulation Of

scholarly journals Mechanism of B-Cell Receptor-Induced Phosphorylation and Activation of Phospholipase C-γ2

2004 ◽  
Vol 24 (22) ◽  
pp. 9986-9999 ◽  
Author(s):  
Yeun Ju Kim ◽  
Fujio Sekiya ◽  
Benoit Poulin ◽  
Yun Soo Bae ◽  
Sue Goo Rhee
Keyword(s):  
B Cell ◽  
Phospholipase C ◽  
Lipase Activity ◽  
Cell Receptor ◽  
B Cell Receptor ◽  
Phosphorylation Sites ◽  
Jurkat T Cells ◽  
Tyrosine Residues ◽  
B Cell Signaling ◽  
Stimulation Of

ABSTRACT Phospholipase C-γ2 (PLC-γ2) plays an important role in B-cell signaling. Phosphorylation of various tyrosine residues of PLC-γ2 has been implicated in regulation of its lipase activity. With the use of antibodies specific for each of the putative phosphorylation sites, we have now shown that PLC-γ2 is phosphorylated on Y753, Y759, and Y1217 in response to engagement of the B-cell receptor in Ramos cells, as well as in murine splenic B cells. In cells stimulated maximally via this receptor, the extent of phosphorylation of Y1217 was three times that of Y753 or of Y759. Stimulation of Jurkat T cells or platelets via their immunoreceptors also elicited phosphorylation of Y753 and Y759 but not that of Y1217. A basal level of phosphorylation of Y753 was apparent in unstimulated lymphocytes. The extent of phosphorylation of Y753 and Y759, but not that of Y1217, correlated with the lipase activity of PLC-γ2. Examination of the effects of various pharmacological inhibitors and of RNA interference in Ramos cells suggested that Btk is largely, but not completely, responsible for phosphorylation of Y753 and Y759, whereas phosphorylation of Y1217 is independent of Btk. Finally, phosphorylation of Y1217 and that of Y753 and Y759 occurred on different PLC-γ2 molecules.

Sustained NF-Kappa B Activity In Chronic Lymphocytic Leukemia Is Independent of Genetic and Epigenetic Modifications of the Tumor Suppressor Genes CYLD and A20

Blood ◽  
2010 ◽  
Vol 116 (21) ◽  
pp. 3597-3597
Author(s):  
Lukas P. Frenzel ◽  
Janine Schwamb ◽  
Rainer Claus ◽  
Julia Claasen ◽  
Reinhild Brinker ◽  
...  
Keyword(s):  
B Cells ◽  
B Cell ◽  
Cell Receptor ◽  
B Cell Receptor ◽  
Lymphocytic Leukemia ◽  
B Cell Malignancies ◽  
Healthy Donors ◽  
B Cell Receptor Signaling ◽  
Cell Receptor Signaling ◽  
Stimulation Of

Abstract Abstract 3597 Introduction: The microenvironment and especially the antigenic stimulation of the B-cell receptor on the surface of the malignant cell play a crucial role in the pathogenesis of chronic lymphocytic leukemia (CLL). Aberrant Nuclear Factor kappa B (NFκB) activity is another major hallmark of B-cell malignancies as well as of CLL. NFκB-dependent genes are involved in anti-apoptotic regulation, cell proliferation and metastasis and are responsible for survival and proliferation of tumors. However, the mechanisms of NFκB over-expression in CLL still remain to be elucidated. Prior studies revealed that cylindromatosis (CYLD) function might be of special interest in CLL since it inhibits signaling via TRAF2 and c-IAP1/2, which are known to be over-expressed in CLL. CYLD inactivation might therefore result in sustained NFκB signaling. The enzyme CYLD, a tumor suppressor that functions as a deubiquitinase, plays a role in other physiological aspects such as cell cycle response, inflammatory and immune processes. Moreover, it could be shown that impaired CYLD activity leads to increased NFκB activity in multiple myeloma cells demonstrating the negative regulatory function of CYLD regarding NFκB. Aside from CYLD, which is constitutively active preventing uncontrolled transcription factor activation, the enzyme A20, a key player in negative feedback loop regulation of NFκB, operates via induction, supposing that both enzymes might proceed at different phases of NFκB signaling. A20, also known as tumor necrosis factor alpha-induced protein 3 (TNFAIP3), acts as an ubiquitin-editing enzyme. Its inactivation is involved in immunopathologies (e.g. Crohn's disease, rheumatoid arthritis, systemic lupus erythematodes, psoriasis and type 1 diabetes mellitus) and in tumorigenesis. Frequent mutations in the A20 locus – leading to sustained NFκB activity – could be shown to play a dominant role in development of different B-cell malignancies. Experimental design and results: Based on genome-wide gene expression profiling analysis of CLL samples (n=8) compared to healthy donor B-cells (n=5), CYLD is expressed and its expression was reduced following B-cell receptor cross-linking (24 hours) (p=0,0036) contrary to A20 that could be induced after receptor stimulation (p=0,044). These results underline the role of B-cell receptor signaling in survival regulation of CLL cells and also its in-direct influence on NFκB activity. Recently, our report revealed by methylation analysis and additional sequence analysis that the A20 region neither contains any methylation (64 CLL patients versus 10 healthy donors) nor mutation (55 CLL patients with sequence analysis of exons 2–9 of the tnfaip3 gene) contrary to reports from other B-cell malignancies. Moreover, A20 expression could be confirmed by immunoblotting showing comparable results to healthy B-cells. In order to check if such alterations in the enzyme CYLD might occur in CLL leading to sustained activity of NFκB similar to other B-cell entities, we performed analysis of the methylation status of the promoter region of CYLD in 64 CLL patients compared to 10 DNAs of CD19-selected B-cells from healthy donors. Epigenetic alterations of the CYLD promoter could not be identified. Conclusions: Here we present the first report of epigenetic and mRNA expression analysis concerning the deubiquitinase CYLD in CLL. We identified that CYLD as well as A20 are regulated by B-cell receptor signaling. The opposed expression of CYLD and A20 after stimulation of the receptor might contribute to an almost balanced and well-adjusted NFκB activity. Our results of lacking epigenetic alteration in both proteins (A20 and CYLD) and absence of mutations in A20 indicate that malignant development in CLL differs from most of other B-cell malignancies, which show frequent inactivation of either CYLD or A20. Disclosures: No relevant conflicts of interest to declare.

Stimulation of the B-Cell Receptor (BCR) Induces Tyrosine Phosphorylation of STAT3 via NF-κB Dependent Mechanism

2016 ◽  
Vol 16 ◽  
pp. S40-S41
Author(s):  
Uri Rozovski ◽  
David Harris ◽  
Ping Li ◽  
Zhiming Liu ◽  
Alessandra Ferrajoli ◽  
...  
Keyword(s):  
B Cell ◽  
Tyrosine Phosphorylation ◽  
Cell Receptor ◽  
B Cell Receptor ◽  
Dependent Mechanism ◽  
Stimulation Of

scholarly journals Rac-mediated Stimulation of Phospholipase Cγ2Amplifies B Cell Receptor-induced Calcium Signaling

2015 ◽  
Vol 290 (28) ◽  
pp. 17056-17072 ◽  
Author(s):  
Claudia Walliser ◽  
Kyrylo Tron ◽  
Karen Clauss ◽  
Orit Gutman ◽  
Andrei Yu. Kobitski ◽  
...  
Keyword(s):  
Calcium Signaling ◽  
B Cell ◽  
Cell Receptor ◽  
B Cell Receptor ◽  
Stimulation Of
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