Phospholipase Cγ2 Provides Survival Signals via Bcl2 and A1 in Different Subpopulations of B Cells
Open accessAbstract
PLCgamma2 plays a critical role in B cell receptor (BCR) signaling and its targeted deletion results in defective B cell development and function. Here, we show that PLCgamma2 deficiency specifically blocks B cell maturation at the transitional type 2 (T2) to follicular (FO) B cell transition and the PLCgamma2 pathway regulates survival of B cells. BCR-induced apoptosis is dramatically enhanced in all subsets of splenic PLCgamma2-deficient B cells, especially in T2 and FO B cell subpopulations. We also find that all splenic PLCgamma2-deficient B cell subpopulations express abnormally low levels of Bcl-2 protein. In addition, PLCgamma2 deficiency disrupts BCR-mediated induction of A1 expression. Enforced expression of Bcl-2 prevents BCR-induced apoptosis in all splenic PLCgamma2-deficient B cell subpopulations and partially restores the numbers of PLCgamma2-deficient FO B cells. In contrast to Bcl-2, enforced expression of A1 preferentially prevents BCR-induced apoptosis in PLCgamma2-deficient FO B cells and partially restores the numbers of these B cells. Therefore, the PLCgamma2 pathway provides a survival signal via regulation of Bcl-2 in all splenic B cell subpopulations and via additional induction of A1 in mature FO B cells.
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PLCγ2−/− mice show a block in B cell maturation from transitional 2 to follicular B cells, with increased BCR-induced apoptosis.
“The first PLCγ2−/− mouse studies showed a block in B cell maturation from transitional 2 to follicular B cells, with these cells also exhibiting increased levels of BCR-induced apoptosis (28, 32).”
From The role of PLCγ2 in immunological disorders, cancer, and neurodegeneration (2021) · cites this paper as [32]
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“24 h with anti-IgM F(ab)2 fragments and/or anti-CD40 crosslinking antibodies, stimuli reported to induce A1 mRNA.(17,19,32) Western analysis revealed that A1 was expressed at low levels in freshly isolated B220 B cells.”
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Phospholipase Cγ2 Contributes to Light-Chain Gene Activation and Receptor Editing
Bai, L., Chen, Y., He, Y., Dai, X., Lin, X., Wen, R., & Wang, D. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02273-06 · Cited by 22 · see citing works
“Although PLC 2 is known to be involved in the survival and proliferation of transitional and mature B cells (68, 70), our analysis of apoptosis and proliferation rates in Ig and Ig B-cell populations derived from wild-type and PLC 2 / mice demonstrates that PLC 2 deficiency does not specifically increase apoptosis or…”
BackgroundSelf-citationComplement Factor H Modulates Splenic B Cell Development and Limits Autoantibody Production
Kiss, M. G., Ozsvár-Kozma, M., Porsch, F., Göderle, L., Papac-Miličević, N., Gritti, B. B., Tsiantoulas, D., Pickering, M. C., & Binder, C. J. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01607 · Cited by 19 · see citing works
Mitochondria, Cell Death, and B Cell Tolerance
Deming, P. B., & Rathmell, J. C. (2005) · KARGER eBooks · doi:10.1159/000090774 · Cited by 19 · see citing works
Modulation and function of caspase pathways in B lymphocytes
Graves, J. D., Craxton, A., & Clark, E. A. (2004) · Immunological Reviews · doi:10.1111/j.0105-2896.2004.0110.x · Cited by 16 · see citing works
“After BCR ligation of PLCg2 B cells, unlike in wildtype cells, Bcl-2 expression is decreased and A1 expression is not induced (139).”
BackgroundIglesias, M., Augustín, J. J., Álvarez, P., Santiuste, I., Postigo, J., Merino, J., & Merino, R. (2016) · PLoS ONE · doi:10.1371/journal.pone.0159714 · Cited by 15 · see citing works
“Whereas the inhibition of B-cell apoptosis, observed in old BIM deficient mice or after the B-cell overexpression doi:10.1371/journal.pone.0159714.g004 PLOS ONE | DOI:10.1371/journal.pone.0159714 July 19, 2016 9 / 16 of BCL2, causes SLE in predisposed animals [3–5], the dysregulation of this pathway in T cells blocks…”
BackgroundInfluentialMontes, C. L., Maletto, B. A., Rodríguez, E. V. A., Gruppi, A., & Pistoresi-Palencia, M. C. (2005) · Clinical & Experimental Immunology · doi:10.1111/j.1365-2249.2005.02969.x · Cited by 14 · see citing works
Dai, X., Chen, Y., Schuman, J., Hua, Z., Adamson, J. W., Wen, R., & Wang, D. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.1.88-99.2006 · Cited by 13 · see citing works
“Specifically, we found in the present and previous (18, 65) studies that even though PI3K and PLC 2 deficiency weakened BCR-induced Ca(2) flux to the same extent, deficiency of the p85 -p55 -p50 regulatory subunits of PI3K impaired FO, MZ, and B1 B-cell development, whereas we showed in previous studies (71, 74) that…”
ResultSelf-citationPhospholipase Cγ2 Dosage Is Critical for B Cell Development in the Absence of Adaptor Protein BLNK
Xu, S., Huo, J., Chew, W.-K., Hikida, M., Kurosaki, T., & Lam, K.-P. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.8.4690 · Cited by 12 · see citing works
“As it was shown previously that BLNK and PLC 2 were both involved in transducing tonic survival signals to B cells (19, 20, 34), we next examined whether B cell survival would be affected by the gene dosage of plc 2 in the absence of BLNK.”
BackgroundChen, L., Oleksyn, D. W., Pulvino, M. J., Sanz, I., Ryan, D. H., Ryan, C., Lin, C., Poligone, B., Pentland, A. P., Ritchlin, C. T., et al. (2016) · Immunology Letters · doi:10.1016/j.imlet.2016.02.015 · Cited by 7 · see citing works
PKK deficiency in B cells prevents lupus development in Sle lupus mice
Oleksyn, D. W., Zhao, J., Vosoughi, A., Zhao, J. C., Misra, R. S., Pentland, A. P., Ryan, D. H., Anolik, J. H., Ritchlin, C. T., Looney, R. J., et al. (2017) · Immunology Letters · doi:10.1016/j.imlet.2017.03.002 · Cited by 5 · see citing works
Defects in B Cell Survival and Activation
Yong, P. F. K., Dziadzio, M., & Grimbacher, B. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-374279-7.18014-2 · Cited by 4 · see citing works
Antony, P., Hoek, K. L., Sarmah, B., & Khan, W. N. (2007) · PubMed Central · doi:10.1251/bpo135 · Cited by 3 · see citing works
Eipper-Mains, M. A. (2004) · DSpace@MIT (Massachusetts Institute of Technology)
Marginal Zone B Cell Development
Demissie, E., Rosenberg, I. M., & Pillai, S. S. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-374279-7.01014-6
Marginal Zone B Cell Development
Pillai, S. S. (2025) · Elsevier eBooks · doi:10.1016/b978-0-12-824465-4.00255-6
Defects in B Cell Survival and Activation
Akhoon, C., & Yong, P. F. K. (2025) · Elsevier eBooks · doi:10.1016/b978-0-12-824465-4.00196-4
- Authors
- Wen, R., Chen, Y., Xue, L., Schuman, J., Yang, S., Morris, S. W., & Wang, D.
- Affiliations
- Model Animal Research Center (CN)
- St. Jude Children's Research Hospital (US)
- Medical College of Wisconsin (US)
- Corresponding author
- Wang, Demin
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-10
- Volume
- 278
- Issue
- 44
- Pages
- 43654-43662
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2169916201
- Cited by
- 41
- References
- 63
- Citations by year
- 2025: 2 · 2021: 1 · 2019: 1 · 2017: 4 · 2016: 4 · 2015: 1 · 2013: 1 · 2012: 3
- FWCI
- 1.51
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Heart, Lung, and Blood Institute (HL073284, R01HL073284)
- National Cancer Institute (R01CA087064, CA87064)
- National Institute of Allergy and Infectious Diseases (R01AI052327, AI52327)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Health Sciences › Medicine › Pathology and Forensic Medicine › Lymphoma Diagnosis and Treatment
- Keywords
- PLCγ2, B cell receptor signaling, B cell survival, apoptosis, Bcl-2, A1, B cell maturation, follicular B cells, splenic B cells
- MeSH terms
- Animals, B-Lymphocytes, Cell Separation, Cell Survival, Cells, Cultured, DNA-Binding Proteins, Flow Cytometry, Humans, Type C Phospholipases, Retroviridae, Spleen, Time Factors, Blotting, Western, Signal Transduction, Bone Marrow Transplantation, Apoptosis, Proto-Oncogene Proteins c-bcl-2, Reverse Transcriptase Polymerase Chain Reaction, In Situ Nick-End Labeling, Mice, Rats, Replication Protein C, Phospholipase C gamma
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