Role of B Cell Antigen Receptor in Regulation of V(D)J Recombination and Cell Survival

2000 ◽  
Vol 21 (2-3) ◽  
pp. 259-264 ◽  
Author(s):  
David Nemazee
Keyword(s):  
B Cell ◽  
Cell Survival ◽  
Antigen Receptor ◽  
B Cell Antigen Receptor ◽  
Cell Antigen Receptor ◽  
Cell Antigen

Role of the extracellular and transmembrane domain of Ig-α/β in assembly of the B cell antigen receptor (BCR)

2007 ◽  
Vol 112 (1) ◽  
pp. 47-57 ◽  
Author(s):  
Janis Dylke ◽  
Jared Lopes ◽  
May Dang-Lawson ◽  
Steve Machtaler ◽  
Linda Matsuuchi
Keyword(s):  
B Cell ◽  
Transmembrane Domain ◽  
Antigen Receptor ◽  
B Cell Antigen Receptor ◽  
Cell Antigen Receptor ◽  
Cell Antigen

The role of Ig-α/β in B cell antigen receptor internalization

2010 ◽  
Vol 134 (1) ◽  
pp. 75-82 ◽  
Author(s):  
Caren Jang ◽  
Steven Machtaler ◽  
Linda Matsuuchi
Keyword(s):  
B Cell ◽  
Antigen Receptor ◽  
Receptor Internalization ◽  
B Cell Antigen Receptor ◽  
Cell Antigen Receptor ◽  
Cell Antigen

scholarly journals Role of B-cell antigen receptor-associated molecules and lipid rafts in CD5-induced apoptosis of B CLL cells

Leukemia ◽  
2004 ◽  
Vol 19 (2) ◽  
pp. 223-229 ◽  
Author(s):  
Y Renaudineau ◽  
S Nédellec ◽  
C Berthou ◽  
P M Lydyard ◽  
P Youinou ◽  
...  
Keyword(s):  
B Cell ◽  
Lipid Rafts ◽  
Antigen Receptor ◽  
B Cell Antigen Receptor ◽  
Cell Antigen Receptor ◽  
Cell Antigen ◽  
Induced Apoptosis

scholarly journals The B Lymphocyte Adaptor Molecule of 32 kD (Bam32) Regulates B Cell Antigen Receptor Signaling and Cell Survival

2002 ◽  
Vol 195 (1) ◽  
pp. 143-149 ◽  
Author(s):  
Hiroaki Niiro ◽  
Akito Maeda ◽  
Tomohiro Kurosaki ◽  
Edward A. Clark
Keyword(s):  
B Cells ◽  
B Cell ◽  
Cell Survival ◽  
Phospholipase C ◽  
B Lymphocyte ◽  
Antigen Receptor ◽  
B Cell Antigen Receptor ◽  
Nuclear Factor ◽  
Cell Antigen Receptor ◽  
Cell Antigen

The B lymphocyte–associated adaptor protein 32 kD in size (Bam32) is expressed at high levels in germinal center (GC) B cells. It has an NH2-terminal src homology 2 (SH2) domain which binds phospholipase C (PLC)γ2, and a COOH-terminal pleckstrin homology (PH) domain. Thus, Bam32 may function to integrate protein tyrosine kinase (PTK) and phosphatidylinositol 3-kinase (PI3K) signaling pathways in B cells. To further define the role Bam32 plays in B cells, we generated Bam32-deficient DT40 cells. These Bam32−/− cells exhibited lower levels of B cell antigen receptor (BCR)-induced calcium mobilization with modest decreases in tyrosine phosphorylation of phospholipase C (PLC)γ2. Moreover, BCR-induced activation of extracellular signal-regulated kinase (ERK), c-jun NH2-terminal kinase (JNK), and p38 mitogen-activated protein kinase (MAPK) pathways was impaired in Bam32−/− cells but not the activation of Akt-related pathways. Activation of downstream transcription factors such as nuclear factor of activated T cells (NF-AT) and nuclear factor of κ binding (NF-κB) was also impaired in Bam32−/− cells. Furthermore, Bam32−/− cells were more susceptible to BCR-induced death. Taken together, these findings suggest that Bam32 functions to regulate BCR-induced signaling and cell survival most likely in germinal centers.

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