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• W2149505831 abstract "Abstract FcγRIIB functions as an inhibitory receptor to dampen B cell Ag receptor signals and immune responses. Accumulating evidence indicates that ex vivo B cells require the inositol 5-phosphatase, Src homology domain 2-containing inositol 5-phosphatase (SHIP), for FcγRIIB-mediated inhibitory signaling. However, we report here that LPS-activated primary B cells do not require SHIP and thus differ from resting B cells. SHIP-deficient B cell blasts display efficient FcγRIIB-dependent inhibition of calcium mobilization as well as Akt and extracellular signal-related protein kinase phosphorylation. Surprisingly, FcγRIIB-dependent degradation of phosphatidylinositol 3,4,5-trisphosphate and conversion into phosphatidylinositol 3,4-bisphosphate occur in SHIP-deficient B cell blasts, demonstrating the function of an additional inositol 5-phosphatase. Further analysis reveals that while resting cells express only SHIP, B cell blasts also express the recently described inositol 5-phosphatase, SHIP-2. Finally, data suggest that both SHIP-2 and SHIP can mediate downstream biologic consequences of FcγRIIB signaling, including inhibition of the proliferative response." @default.
• W2149505831 created "2016-06-24" @default.
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• W2149505831 date "2001-07-01" @default.
• W2149505831 modified "2023-10-14" @default.
• W2149505831 title "Partially Distinct Molecular Mechanisms Mediate Inhibitory FcγRIIB Signaling in Resting and Activated B Cells" @default.
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• W2149505831 doi "https://doi.org/10.4049/jimmunol.167.1.204" @default.
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