Peptidoglycan and lipopolysaccharide activate PLCγ2, leading to enhanced cytokine production in macrophages and dendritic cells
Open accessAbstract
In macrophages and monocytes, microbial components trigger the production of pro‐inflammatory cytokine through Toll‐like receptors (TLRs). Although major TLR signaling pathways are mediated by serine/threonine kinases, including TAK1, IKK and MAP kinases, tyrosine phosphorylation of intracellular proteins by TLR ligands has been suggested in a number of reports. Here, we demonstrated that peptidoglycan (PGN) of a Gram‐positive bacterial cell wall component, a TLR2 ligand and lipopoysaccharide (LPS) of a Gram‐positive bacterial component, a TLR4 ligand induced tyrosine phosphorylation of phospholipase Cγ‐2 (PLCγ2), leading to intracellular free Ca 2+ mobilization in bone marrow‐derived macrophages (BMMφ) and bone marrow‐derived dendritic cells (BMDC). PGN‐ and LPS‐induced Ca 2+ mobilization was not observed in BMDC from PLCγ2 knockout mice. Thus, PLCγ2 is essential for TLR2 and TLR4‐mediated Ca 2+ flux. In PLCγ2‐knockdown cells, PGN‐induced IκB‐α phosphorylation and p38 activation were reduced. Moreover, PLCγ2 was necessary for the full production of TNF‐α and IL‐6. These data indicate that the PLCγ2 pathway plays an important role in bacterial ligands‐induced activation of macrophages and dendritic cells.
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PLCγ2 is required after peptidoglycan/TLR2 and LPS/TLR4 stimulation to induce normal levels of TNF-α and IL-6 in bone marrow-derived macrophages and dendritic cells.
“The use of BM-derived macrophages and DCs from PLCγ2 KO mice showed that PLCγ2 was required after peptidoglycan/TLR2 and LPS/TLR4 stimulation to induce normal levels of TNF-α and IL-6 (84).”
From The role of PLCγ2 in immunological disorders, cancer, and neurodegeneration (2021) · cites this paper as [84]
The cytokine-production results section reports reduced TNF-α and IL-6 after PGN stimulation of PLCγ2-deficient bone marrow-derived macrophages, with a similar reduction after LPS stimulation. It suggests the requirement extends to dendritic cells, but the Introduction describes the knockout dendritic-cell finding as impaired calcium mobilization, not a direct cytokine-production measurement. The claim overstates what the knockout dendritic-cell experiments showed. (LLM, conf=0.85)
Experimental — accuracy not yet measuredPLCγ2 activation leads to an increase in cytoplasmic calcium, that supports the assembly of the NLRP3 inflammasome, and pro-inflammatory cytokine release in human blood monocytes, bone-marrow-derived macrophages and dendritic cells.
“PLCγ2 activation leads to an increase in cytoplasmic calcium, that supports the assembly of the pyrin (PYD)-domain-containing protein 3 (NLRP3) inflammasome, and pro-inflammatory cytokine release in human blood monocytes [31], bone-marrow-derived macrophages (BMDM) and dendritic cells [32].”
From TREM2/PLCγ2 signalling in immune cells: function, structural insight, and potential therapeutic modulation (2021) · cites this paper as [32]
The Discussion and results report that PLCγ2 contributes to intracellular calcium mobilization in bone-marrow-derived macrophages and dendritic cells, and that it is required for full pro-inflammatory cytokine production. The paper does not link this calcium response to NLRP3 inflammasome assembly. Human blood monocytes are attached to a different citation in the citing sentence, so they are not assessed here. (LLM, conf=0.88)
Experimental — accuracy not yet measuredPLCγ2 activation in microglia, monocyte/macrophages, dendritic and mast cells has been linked to increased cytokine production.
“PLCγ2 activation in microglia, monocyte/macrophages, dendritic and mast cells has been linked to increased cytokine production [32, 35]”
From TREM2/PLCγ2 signalling in immune cells: function, structural insight, and potential therapeutic modulation (2021) · cites this paper as [32]
The Introduction and the section on TLR2–PLCγ2 signaling link PLCγ2 to TNF-α and IL-6 production in macrophages and dendritic cells after bacterial-ligand stimulation (page numbers unavailable). Our copy does not establish the same PLCγ2–cytokine link in microglia, mast cells, or monocytes specifically. (LLM, conf=0.88)
Experimental — accuracy not yet measuredPLCG2 plays a critical role in transducing signals emanating from a number of immune receptors, acting as an intracellular hub for immune signaling.
“PLCG2 plays a critical role in transducing signals emanating from a number of immune receptors, acting as an intracellular hub for immune signaling.”
From PLCG2 modulates TREM2 expression and signaling in response to Alzheimer's disease pathology (2025) · cites this paper as [15]
PLCG2 mediates transduction of many other cell surface receptors in addition to TREM2.
“Likewise, PLCG2 mediates transduction of many other cell surface receptors in addition to TREM2. 13 , 15 , 16 , 17 , 18 , 19 , 20 , 21”
From PLCG2 modulates TREM2 expression and signaling in response to Alzheimer's disease pathology (2025) · cites this paper as [15]
TREM2 plays a key and enigmatic role in the progression of AD, acting to drive microglial phagocytosis, survival, lipid homeostasis, and metabolism.
“TREM2 plays a key and enigmatic role in the progression of AD, acting to drive microglial phagocytosis, survival, lipid homeostasis, and metabolism.”
From PLCG2 modulates TREM2 expression and signaling in response to Alzheimer's disease pathology (2025) · cites this paper as [15]
The Introduction and the passage headed Abstract (page not provided) discuss PLCγ2-dependent responses to bacterial ligands in macrophages and dendritic cells. Searches for TREM2 and for Alzheimer’s disease or microglia returned no passage addressing TREM2’s role in AD progression, phagocytosis, survival, lipid homeostasis, or metabolism. (LLM, conf=0.76)
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Cites
Pathogen Recognition and Innate Immunity
Akira, S., Uematsu, S., & Takeuchi, O. (2006) · Cell · doi:10.1016/j.cell.2006.02.015 · Cited by 11,974 · see citing works
Inositol trisphosphate and calcium signalling
Berridge, M. J. (1993) · Nature · doi:10.1038/361315a0 · Cited by 6,545 · see citing works
The family of five: TIR-domain-containing adaptors in Toll-like receptor signalling
O'Neill, L. A. J., & Bowie, A. G. (2007) · Nature Reviews Immunology · doi:10.1038/nri2079 · Cited by 2,667 · see citing works
Protein kinase C and lipid signaling for sustained cellular responses
Nishizuka, Y. (1995) · The FASEB Journal · doi:10.1096/fasebj.9.7.7737456 · Cited by 2,499 · see citing works
Akira, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.r300028200 · Cited by 1,486 · see citing works
Rogers, N. C., Slack, E. M. C., Edwards, A. D., Nolte, M. A., Schulz, O., Schweighoffer, E., Williams, D. L., Gordon, S., Tybulewicz, V. L. J., Brown, G. D., et al. (2005) · Immunity · doi:10.1016/j.immuni.2005.03.004 · Cited by 897 · see citing works
Sekiguchi, M. (1997) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(97)83119-2 · Cited by 668 · see citing works
Toll-like receptor 2–mediated NF-κB activation requires a Rac1-dependent pathway
Arbibe, L., Mira, J. P., Teusch, N. E., Kline, L., Guha, M., Mackman, N., Godowski, P. J., Ulevitch, R. J., & Knaus, U. G. (2000) · Nature Immunology · doi:10.1038/82797 · Cited by 664 · see citing works
Differential responses of mast cell Toll-like receptors 2 and 4 in allergy and innate immunity
Supajatura, V., Ushio, H., Nakao, A., Akira, S., Okumura, K., Ra, C., & Ogawa, H. (2002) · Journal of Clinical Investigation · doi:10.1172/jci14704 · Cited by 491 · see citing works
Differential responses of mast cell Toll-like receptors 2 and 4 in allergy and innate immunity
Supajatura, V., Ushio, H., Nakao, A., Akira, S., Okumura, K., Ra, C., & Ogawa, H. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0214704 · Cited by 404 · see citing works
Activation of Phospholipase C-γ by Phosphatidylinositol 3,4,5-Trisphosphate
Bae, Y. S., Cantley, L. G., Chen, C.-S., Kim, S.-R., Kwon, K.-S., & Rhee, S. G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.8.4465 · Cited by 330 · see citing works
Jefferies, C. A., Doyle, S., Brunner, C., Dunne, A., Brint, E. K., Wietek, C., Walch, E., Wirth, T., & O'Neill, L. A. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301484200 · Cited by 293 · see citing works
Phospholipase C-γ as a Signal-Transducing Element
Carpenter, G. F., & Ji, Q. (1999) · Experimental Cell Research · doi:10.1006/excr.1999.4671 · Cited by 246 · see citing works
Protein Kinase Cϵ Is Required for Macrophage Activation and Defense Against Bacterial Infection
Castrillo, A., Pennington, D. J., Otto, F., Parker, P. J., Owen, M. J., & Boscá, L. (2001) · The Journal of Experimental Medicine · doi:10.1084/jem.194.9.1231 · Cited by 246 · see citing works
Bruton’s Tyrosine Kinase Is Required for TLR2 and TLR4-Induced TNF, but Not IL-6, Production
Horwood, N. J., Page, T. H., McDaid, J., Palmer, C. D., Campbell, J., Mahon, T., Brennan, F. M., Webster, D., & Foxwell, B. M. J. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.6.3635 · Cited by 203 · see citing works
Lymphocyte calcium signaling from membrane to nucleus
Gallo, E. M., Canté-Barrett, K., & Crabtree, G. R. (2005) · Nature Immunology · doi:10.1038/ni1295 · Cited by 183 · see citing works
Cutting Edge: Essential Role of Phospholipase C-γ2 in B Cell Development and Function
Hashimoto, A., Takeda, K., Inaba, M., Sekimata, M., Kaisho, T., Ikehara, S., Homma, Y., Akira, S., & Kurosaki, T. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.4.1738 · Cited by 155 · see citing works
Self-citationZhou, X., Yang, W., & Li, J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m602739200 · Cited by 152 · see citing works
Chang, Y., Wu, M., Lin, J., & Chen, C. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.12.8242 · Cited by 149 · see citing works
Trif-related adapter molecule is phosphorylated by PKCε during Toll-like receptor 4 signaling
McGettrick, A. F., Brint, E. K., Pålsson‐McDermott, E. M., Rowe, D. C., Golenbock, D. T., Gay, N. J., Fitzgerald, K. A., & O'Neill, L. A. J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0600462103 · Cited by 137 · see citing works
Chen, T., Guo, J., Yang, M., Han, C., Zhang, M., Chen, W., Liu, Q., Wang, J., & Cao, X. (2003) · Blood · doi:10.1182/blood-2003-07-2412 · Cited by 131 · see citing works
Involvement of PKCα/β in TLR4 and TLR2 dependent activation of NF-κB
Asehnoune, K., Strassheim, D., Mitra, S., Kim, J. Y., & Abraham, E. H. (2004) · Cellular Signalling · doi:10.1016/j.cellsig.2004.08.005 · Cited by 126 · see citing works
Chen, C., Wang, J. K. T., & Lin, S. (1998) · PubMed · Cited by 121 · see citing works
Kimura, A., Kinjyo, I., Matsumura, Y., Mori, H., Mashima, R., Harada, M., Chien, K. R., Yasukawa, H., & Yoshimura, A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.c300496200 · Cited by 119 · see citing works
Self-citationMatsumura, Y., Kobayashi, T., Ichiyama, K., Yoshida, R., Hashimoto, M., Takimoto, T., Tanaka, K., Chinen, T., Shichita, T., Wyss‐Coray, T., et al. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.179.4.2170 · Cited by 107 · see citing works
Self-citationChen, C.-C., Wang, J.-K., & Lin, S.-B. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.161.11.6206 · Cited by 106 · see citing works
Valledor, A. F., Xaus, J., Comalada, M., Soler, C., & Celada, A. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.164.1.29 · Cited by 103 · see citing works
The Molecular Adapter Carma1 Controls Entry of IκB Kinase into the Central Immune Synapse
Hara, H., Bakal, C., Wada, T., Bouchard, D., Rottapel, R. K., Saito, T., & Penninger, J. M. (2004) · The Journal of Experimental Medicine · doi:10.1084/jem.20032246 · Cited by 88 · see citing works
Kim, Y., Moon, J. S., Lee, K. S., Park, S. Y., Cheong, J., Kang, H. S., Lee, H. Y., & Kim, H. D. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.12.153 · Cited by 84 · see citing works
Chinen, T., Kobayashi, T., Ogata, H., Takaesu, G., Takaki, H., Hashimoto, M., Yagita∥, H., Nawata, H., & Yoshimura, A. (2006) · Gastroenterology · doi:10.1053/j.gastro.2005.10.051 · Cited by 82 · see citing works
Self-citationActivation of Ca2+-Dependent Signaling by TLR2
Chun, J., & Prince, A. S. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.2.1330 · Cited by 79 · see citing works
Akt Binds to and Phosphorylates Phospholipase C-γ1 in Response to Epidermal Growth Factor
Wang, Y., Wu, J., & Wang, Z. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-10-0918 · Cited by 64 · see citing works
Shapira, L., Sylvia, V. L., Halabi, A., Soskolne, W. A., Dyke, T. E. V., Dean, D. D., Boyan, B. D., & Schwartz, Z. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7717 · Cited by 52 · see citing works
Modulation of TLR signalling by the C‐terminal Src kinase (Csk) in macrophages
Aki, D., Mashima, R., Saeki, K., Minoda, Y., Yamauchi, M., & Yoshimura, A. (2005) · Genes to Cells · doi:10.1111/j.1365-2443.2005.00839.x · Cited by 36 · see citing works
Self-citationDuperrier, K., Farre, A., Bienvenu, J., Bleyzac, N., Bernaud, J., Gebuhrer, L., Rigal, D., & Eljaafari, A. (2002) · PubMed · Cited by 35 · see citing works
Duperrier, K., Farre, A., Bienvenu, J., Bleyzac, N., Bernaud, J., Gebuhrer, L., Rigal, D., & Eljaafari, A. (2002) · Journal of Leukocyte Biology · doi:10.1189/jlb.72.5.953 · Cited by 32 · see citing works
Shinji, H., Akagawa, K. S., Tsuji, M., Maeda, M., Yamada, R., Matsuura, K., Yamamoto, S., & Yoshida, T. (1997) · The Journal of Immunology · doi:10.4049/jimmunol.158.3.1370 · Cited by 21 · see citing works
Flagged first, then by citations
1 of the 38 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Vitamin D cell signalling in health and disease
Berridge, M. J. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.01.008 · Cited by 214 · see citing works
Sharbati, J., Lewin, A., Kutz-Lohroff, B., Kamal, E., Einspanier, R., & Sharbati, S. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020258 · Cited by 163 · see citing works
Racioppi, L., & Means, A. R. (2008) · Trends in Immunology · doi:10.1016/j.it.2008.08.005 · Cited by 146 · see citing works
Knowles, H. M., Heizer, J. W., Li, Y., Chapman, K., Ogden, C. A., Andreasen, K., Shapland, E. M., Kucera, G., Mogan, J., Humann, J., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1010678108 · Cited by 142 · see citing works
Chiang, C.-Y., Veckman, V., Limmer, K., & David, M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.c111.328559 · Cited by 120 · see citing works
The role of PLCγ2 in immunological disorders, cancer, and neurodegeneration
Jackson, J. T., Mulazzani, E., Nutt, S. L., & Masters, S. L. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100905 · Cited by 113 · see citing works
“The use of BM-derived macrophages and DCs from PLCγ2 KO mice showed that PLCγ2 was required after peptidoglycan/TLR2 and LPS/TLR4 stimulation to induce normal levels of TNF-α and IL-6 (84).”
Murofushi, Y., Villena, J., Morie, K., Kanmani, P., Tohno, M., Shimazu, T., Aso, H., Suda, Y., Hashiguchi, K., Saito, T., et al. (2014) · Molecular Immunology · doi:10.1016/j.molimm.2014.10.027 · Cited by 99 · see citing works
Morishita, M., Horita, M., Higuchi, A., Marui, M., Katsumi, H., & Yamamoto, A. (2021) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.0c01011 · Cited by 93 · see citing works
Qiu, C., Shi, W., Wu, H., Zou, S., Li, J., Wang, D., Liu, G., Song, Z., Xu, X., Hu, J., et al. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.769685 · Cited by 91 · see citing works
Wachi, S., Kanmani, P., Tomosada, Y., Kobayashi, H., Yuri, T., Egusa, S., Shimazu, T., Suda, Y., Aso, H., Sugawara, M., et al. (2014) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201400218 · Cited by 87 · see citing works
Ca2+ signaling in the regulation of dendritic cell functions
Shumilina, E. V., Huber, S. M., & Lang, F. J. W. (2011) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00039.2011 · Cited by 86 · see citing works
CD8+ T Cells Regulate Bone Tumor Burden Independent of Osteoclast Resorption
Zhang, K., Kim, S., Cremasco, V., Hirbe, A. C., Novack, D. V., Weilbaecher, K. N., & Faccio, R. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-3922 · Cited by 82 · see citing works
The Role of Phospholipase C Signaling in Macrophage-Mediated Inflammatory Response
Zhu, L., Jones, C., & Zhang, G. (2018) · Journal of Immunology Research · doi:10.1155/2018/5201759 · Cited by 74 · see citing works
PLC-γ2 is essential for formation and maintenance of memory B cells
Hikida, M., Casola, S., Takahashi, N., Kaji, T., Takemori, T., Rajewsky, K., & Kurosaki, T. (2009) · Journal of Experimental Medicine · doi:10.1084/jem.20082100 · Cited by 73 · see citing works
Self-citationImmunomodulatory effects of sulfated polysaccharides of pine pollen on mouse macrophages
Geng, Y., Li, X., Sun, M., & Su, F. (2016) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2016.06.021 · Cited by 72 · see citing works
Magno, L., Bunney, T. D., Mead, E., Svensson, F., & Bictash, M. N. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00436-5 · Cited by 64 · see citing works
Ryu, S., Han, H. M., Song, P. I., Armstrong, C. A., & Park, Y. (2015) · PLoS ONE · doi:10.1371/journal.pone.0132619 · Cited by 53 · see citing works
Langlet, C., Springael, C., Johnson, J., Thomas, S., Flamand, V., Leitges, M., Goldman, M., Aksoy, E., & Willems, F. (2009) · European Journal of Immunology · doi:10.1002/eji.200939391 · Cited by 52 · see citing works
Velmurugan, G. V., Huang, H., Sun, H., Candela, J., Jaiswal, M. K., Beaman, K. D., Yamashita, M., Prakriya, M., & White, C. (2015) · Science Signaling · doi:10.1126/scisignal.aac7135 · Cited by 48 · see citing works
Abe, K., Fuchs, H., Boersma, A., Hans, W., Yu, P., Kalaydjiev, S., Klaften, M., Adler, T., Calzada‐Wack, J., Mossbrugger, I., et al. (2011) · Arthritis & Rheumatism · doi:10.1002/art.30280 · Cited by 46 · see citing works
Tassi, I., Cella, M., Castro, I., Gilfillan, S., Khan, W. N., & Colonna, M. (2009) · European Journal of Immunology · doi:10.1002/eji.200839313 · Cited by 46 · see citing works
Cremasco, V., Benasciutti, E., Cella, M., Kisseleva, M. V., Croke, M., & Faccio, R. (2010) · PLoS ONE · doi:10.1371/journal.pone.0008909 · Cited by 39 · see citing works
Zhou, X., Ye, Y., Sun, Y., Li, X., Wang, W., Privratsky, B., Tan, S., Zhou, Z., Huang, C., Wei, Y.-Q., et al. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00256-15 · Cited by 38 · see citing works
Effect of Bacterial Lipopolysaccharide on Na+/H+ Exchanger Activity in Dendritic Cells
Rotte, A., Pasham, V., Eichenmüller, M., Mahmud, H., Xuân, N. T., Shumilina, E. V., Götz, F., & Lang, F. J. W. (2010) · Cellular Physiology and Biochemistry · doi:10.1159/000322323 · Cited by 33 · see citing works
Ca2+-dependent Functions in Peptidoglycan-stimulated Mouse Dendritic Cells
Xuân, N. T., Shumilina, E. V., Matzner, N., Zemtsova, I. M., Biedermann, T., Goetz, F., & Lang, F. J. W. (2009) · Cellular Physiology and Biochemistry · doi:10.1159/000233243 · Cited by 35 · see citing works
Frequent Calcium Oscillations Lead to NFAT Activation in Human Immature Dendritic Cells
Vukcevic, M., Zorzato, F., Spagnoli, G. C., & Treves, S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.066704 · Cited by 34 · see citing works
The gut microbiota and cardiovascular health benefits: A focus on wholegrain oats
Kristek, A., Schär, M. Y., Soycan, G., Alsharif, S. N. M., Kuhnle, G., Walton, G., & Spencer, J. P. E. (2018) · Nutrition Bulletin · doi:10.1111/nbu.12354 · Cited by 31 · see citing works
Activation of the Endoplasmic Reticulum Stress Response Impacts the NOD1 Signaling Pathway
Mendez, J. M., Kolora, L. D., Lemon, J. S., Dupree, S. L., & Keestra, A. M. (2019) · Infection and Immunity · doi:10.1128/iai.00826-18 · Cited by 31 · see citing works
Halabi, S., Sekine, E., Verstak, B., Gay, N. J., & Moncrieffe, M. C. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.761528 · Cited by 30 · see citing works
Immune regulation of the tumor/bone vicious cycle
Faccio, R. (2011) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2011.06244.x · Cited by 30 · see citing works
Regulation of calcium signaling in dendritic cells by 1,25‐dihydroxyvitamin D 3
Shumilina, E. V., Xuân, N. T., Matzner, N., Bhandaru, M., Zemtsova, I. M., & Lang, F. J. W. (2010) · The FASEB Journal · doi:10.1096/fj.09-142265 · Cited by 30 · see citing works
Matsumura, T., Oyama, M., Kozuka‐Hata, H., Ishikawa, K., Inoue, T., Muta, T., Semba, K., & Inoue, J. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.08.055 · Cited by 29 · see citing works
Influence of Dexamethasone on Na+/H+ Exchanger Activity in Dendritic Cells
Rotte, A., Pasham, V., Eichenmüller, M., Yang, W., Bhandaru, M., & Lang, F. J. W. (2011) · Cellular Physiology and Biochemistry · doi:10.1159/000331746 · Cited by 28 · see citing works
Membrane androgen receptor sensitive Na+/H+ exchanger activity in prostate cancer cells
Chatterjee, S., Schmidt, S., Pouli, S., Honisch, S., Alkahtani, S. H., Stournaras, C., & Lang, F. J. W. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.02.040 · Cited by 27 · see citing works
Effect of dexamethasone on Na+/Ca2+ exchanger in dendritic cells
Heise, N., Shumilina, E. V., Nurbaeva, M. K., Schmid, E., Szteyn, K., Yang, W., Xuân, N. T., Wang, K., Zemtsova, I. M., Duszenko, M., et al. (2011) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00396.2010 · Cited by 25 · see citing works
Park, K. S., Kim, S. H., Das, A., Yang, S.-N., Jung, K. H., Kim, M. K., Berggren, P., Lee, Y., Chai, J. C., Kim, H. J., et al. (2016) · Scientific Reports · doi:10.1038/srep23103 · Cited by 24 · see citing works
Effect of Thymoquinone on Cytosolic pH and Na+/H+ Exchanger Activity in Mouse Dendritic Cells
Yang, W., Bhandaru, M., Pasham, V., Bobbala, D., Zelenak, C., Jilani, K., Rotte, A., & Lang, F. J. W. (2012) · Cellular Physiology and Biochemistry · doi:10.1159/000337583 · Cited by 23 · see citing works
Rapamycin Sensitive ROS Formation and Na+/H+Exchanger Activity in Dendritic Cells
Rotte, A., Pasham, V., Bhandaru, M., Bobbala, D., Zelenak, C., & Lang, F. J. W. (2012) · Cellular Physiology and Biochemistry · doi:10.1159/000338508 · Cited by 23 · see citing works
Casas, J., Meana, C., López‐López, J. R., Balsinde, J., & Balboa, M. A. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03999-0 · Cited by 22 · see citing works
Rac-mediated stimulation of phospholipase Cγ2 amplifies B cell receptor-induced calcium signaling
Walliser, C., Tron, K., Clauss, K., Gutman, O., Kobitski, A. Y., Retlich, M., Schade, A., Röcker, C., Henis, Y. I., Nienhaus, G. U., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.645739 · Cited by 21 · see citing works
Altered regulation of cytosolic Ca2+ concentration in dendritic cells from klotho hypomorphic mice
Shumilina, E. V., Nurbaeva, M. K., Yang, W., Schmid, E., Szteyn, K., Russo, A., Heise, N., Leibrock, C. B., Xuân, N. T., Faggio, C., et al. (2013) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00355.2012 · Cited by 21 · see citing works
Raimo, T. D., Leopizzi, M., Mangino, G., Rocca, C. D., Businaro, R., Longo, L., & Vasco, V. R. L. (2016) · Journal of Cell Communication and Signaling · doi:10.1007/s12079-016-0335-9 · Cited by 21 · see citing works
Kukita, A., Ichigi, Y., Takigawa, I., Watanabe, T., Kukita, T., & Miyamoto, H. (2012) · PLoS ONE · doi:10.1371/journal.pone.0038500 · Cited by 24 · see citing works
PLCG2 as a potential indicator of tumor microenvironment remodeling in soft tissue sarcoma
Li, Z., Zhao, R., Yang, W., Li, C., Huang, J., Wen, Z., Du, G., & Jiang, L. (2021) · Medicine · doi:10.1097/md.0000000000025008 · Cited by 21 · see citing works
Leucine‐rich repeat kinase 2‐sensitive Na + /Ca 2+ exchanger activity in dendritic cells
Yan, J., Ahnilaji, A., Schmid, E., Elvira, B., Shimshek, D. R., van der Putten, H., Wagner, C. A., Shumilina, E. V., & Lang, F. J. W. (2015) · The FASEB Journal · doi:10.1096/fj.14-264028 · Cited by 20 · see citing works
Kudo, K., Uchida, T., Sawada, M., Nakamura, Y., Yoneda, A., & Fukami, K. (2015) · Advances in Biological Regulation · doi:10.1016/j.jbior.2015.11.004 · Cited by 18 · see citing works
Li, R. H. L., Nguyen, N. H., & Tablin, F. (2019) · BMC Veterinary Research · doi:10.1186/s12917-019-1997-3 · Cited by 17 · see citing works
PLCG2 modulates TREM2 expression and signaling in response to Alzheimer's disease pathology
Messenger, E. J., Baar, S. A., Bedford, L. M., Tsai, A. P., Lin, P. B., Ferguson, C. A., Xu, G., Wallace, A., Landreth, G. E., Lamb, B. T., et al. (2025) · Alzheimer's & Dementia · doi:10.1002/alz.70231 · Cited by 16 · see citing works
Phosphoinositide 3-kinase-dependent regulation of Na+/H+ exchanger in dendritic cells
Rotte, A., Pasham, V., Yang, W., Eichenmüller, M., Bhandaru, M., Shumilina, E. V., & Lang, F. J. W. (2010) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-010-0879-0 · Cited by 16 · see citing works
Effect of Azathioprine on Na+/H+Exchanger Activity in Dendritic Cells
Bhandaru, M., Pasham, V., Yang, W., Bobbala, D., Rotte, A., & Lang, F. J. W. (2012) · Cellular Physiology and Biochemistry · doi:10.1159/000338507 · Cited by 16 · see citing works
Li, Y., Efferson, C. L., Ramesh, R., Peoples, G. E., Hwu, P., & Ioannides, C. G. (2010) · Cancer Immunology Immunotherapy · doi:10.1007/s00262-010-0959-1 · Cited by 13 · see citing works
Regulation of Na+/H+ Exchanger in Dendritic Cells by Akt1
Zhou, Y., Pasham, V., Chatterjee, S., Rotte, A., Yang, W., Bhandaru, M., Singh, Y., & Lang, F. J. W. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000430293 · Cited by 13 · see citing works
Son, A., Shin, D. M., & Hong, J. H. (2015) · Korean Journal of Physiology and Pharmacology · doi:10.4196/kjpp.2015.19.1.51 · Cited by 11 · see citing works
Regulation of Na+/H+ exchanger in dendritic cells by Akt2
Bhandaru, M., Yang, W., Rotte, A., Pasham, V., & Lang, F. J. W. (2011) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-011-1015-5 · Cited by 11 · see citing works
Slomiany, B. L., & Slomiany, A. (2015) · Inflammopharmacology · doi:10.1007/s10787-015-0231-6 · Cited by 10 · see citing works
Slomiany, B. L., & Slomiany, A. (2014) · Inflammopharmacology · doi:10.1007/s10787-014-0220-1 · Cited by 8 · see citing works
Sakalauskienė, J., Giedrimienė, D., Gleiznys, D., Gleiznys, A., Gleiznienė, R., & Vitkauskienė, A. (2016) · Medical Science Monitor · doi:10.12659/msm.898422 · Cited by 8 · see citing works
Lv, Y., Jin, Y., Zhou, Z., Liao, J.-B., Zhang, Z.-Q., Tang, L.-Y., Xie, X., Wang, S., Jin, M.-X., & Liu, H. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1725349 · Cited by 7 · see citing works
Phospholipase C-γ as a Potential Therapeutic Target for Graves’ Orbitopathy
Roh, T. H., Chae, M. K., Ko, J., Kikkawa, D. O., Jang, S. Y., & Yoon, J. S. (2023) · Endocrinology and Metabolism · doi:10.3803/enm.2023.1780 · Cited by 7 · see citing works
Son, G.-Y., Shin, D. M., & Hong, J. H. (2015) · Korean Journal of Physiology and Pharmacology · doi:10.4196/kjpp.2015.19.3.291 · Cited by 5 · see citing works
Kim, M. J., Rah, S., An, J.-H., Kurokawa, K., Kim, U., & Lee, B. L. (2015) · BMB Reports · doi:10.5483/bmbrep.2015.48.1.080 · Cited by 4 · see citing works
Bull, D., Matte, J. C., Navarron, C. M., McIntyre, R., Whiting, P., Katan, M., Ducotterd, F., & Magno, L. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2023.166978 · Cited by 3 · see citing works
Regulation of Murine Dendritic Cell Functions by Calcium Channels
Sumoza‐Toledo, A. (2014) · SOJ Immunology · doi:10.15226/soji/2/2/00113 · Cited by 3 · see citing works
Function and Regulation of Na + / H + Exchanger in Dendritic Cells
Pasham, V. (2012)
Studies on the Regulation of Leukotriene Biosynthesis in Antigen Presenting Cells
Bieren, J. E. (2011) · Figshare
Golds, G. B. (2010) · cIRcle (University of British Columbia) · doi:10.14288/1.0071024
dendritic cells from klotho hypomorphic mice concentration in 2+ Altered regulation of cytosolic Ca
Kuro‐o, M., Lang, F. J. W., Russo, A., Heise, N., Leibrock, C. B., Xuân, N. T., Faggio, C., Shumilina, E. V., Nurbaeva, M. K., Yang, W., et al. (2016)
- Authors
- Aki, D., Minoda, Y., Yoshida, H., Watanabe, S., Yoshida, R., Takaesu, G., Chinen, T., Inaba, T., Hikida, M., Kurosaki, T., Saeki, K., & Yoshimura, A.
- Affiliations
- Hiroshima University (JP)
- Kyushu University (JP)
- RIKEN (JP)
- Corresponding author
- Yoshimura, Akihiko
- Venue
- Genes to Cells
- Publisher
- Wiley
- Published
- 2008-01-30
- Volume
- 13
- Issue
- 2
- Pages
- 199-208
- ISSN
- 1356-9597 (ISSN-L)
- 1365-2443
- OpenAlex
- W2143395804
- Cited by
- 68
- References
- 38
- Citations by year
- 2026: 1 · 2025: 1 · 2023: 2 · 2021: 6 · 2019: 2 · 2018: 2 · 2016: 6 · 2015: 12 · 2014: 5 · 2013: 1 · 2012: 5
- FWCI
- 3.47
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes to Cells (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Takeda Science Foundation
- National Institute of Biomedical Innovation
- Kanae Foundation for the Promotion of Medical Science
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Immunology and Microbiology › Immunology › Immunotherapy and Immune Responses
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Keywords
- peptidoglycan, lipopolysaccharide, PLCγ2, TLR2, TLR4, tyrosine phosphorylation, calcium mobilization, macrophages, dendritic cells, TNF-α, interleukin-6, IκBα phosphorylation, p38 MAPK, Toll-like receptor signaling
- MeSH terms
- Animals, Base Sequence, Cell Line, Dendritic Cells, Enzyme Activation, Humans, Ligands, Lipopolysaccharides, Macrophages, Mice, Mutant Strains, Mice, Transgenic, Peptidoglycan, Transfection, Tumor Necrosis Factor-alpha, Signal Transduction, Interleukin-6, Cytokines, Calcium Signaling, RNA, Small Interfering, Toll-Like Receptor 2, Toll-Like Receptor 4, Mice, Phospholipase C gamma
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