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• W2057900906 abstract "Apoptosis of B cells upon ligation of the B cell antigen receptor (BCR) plays a role in elimination of self-reactive B cells. Previously, BCR ligation was shown to induce expression of the molecules involved in the unfolded protein response (UPR). However, the role of the UPR in BCR-mediated apoptosis is poorly understood. Here, we demonstrate that activation of various UPR molecules are induced when BCR ligation induces apoptosis in the B cell line WEHI-231 and mouse spleen B cells. BCR ligation-induced UPR is attenuated by survival signaling through CD40 in these cells. When overexpression of BiP suppresses the UPR in WEHI-231 cells, activation of p38 MAPK is blocked and apoptosis is reduced. Moreover, the p38 MAPK inhibitor SB203580 reduces BCR ligation-induced apoptosis. These results suggest that the UPR is involved in BCR ligation-induced apoptosis and that p38 MAPK is crucial for apoptosis during the UPR in B cells." @default.
• W2057900906 created "2016-06-24" @default.
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• W2057900906 date "2008-01-01" @default.
• W2057900906 modified "2023-10-18" @default.
• W2057900906 title "ER stress is involved in B cell antigen receptor ligation-induced apoptosis" @default.
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• W2057900906 doi "https://doi.org/10.1016/j.bbrc.2007.10.137" @default.
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