Aim - to study upstream and downstream events in CD150-mediated Akt signaling pathway in normal human B cells, EBVtransformed lymphoblastoid (LCL) and malignant Hodgkin's lymphoma (HL) B cell lines. Methods: to access protein-protein interaction we applied immunoprecipitation, Western blot analysis and surface plasmon resonance (SPR) technique. A novel modification of SPR technique using reduced glutathione bound to golden surface was proposed. Immunostaining and isolation of cytoplasmic fractions and nuclear extracts were performed to detect proteins' localization in cells. Western blot analysis was performed to follow up the phosphorylation of proteins on specific sites and proteins' expression level. It was shown that CD150 ligation induced Akt activation in normal tonsillar B cells (TBC), SH2D1A positive LCL and HL B cell lines. The p85alpha subunit of PI3K co-precipitated with CD150 cytoplasmic tail. This direct association depends on tyrosine phosphorylation and is mediated by N terminal SH2 domain of p85alpha. CD150 initiated phosphorylation of FoxO1 transcription factor in normal B cells as well as in LCL MP-1 and HL cell line L1236. At the same time, CD150 ligation triggered GSK-3beta kinase phosphorylation only in immortalized LCL MP-1 and HL cell line L1236. Conclusions: we have demonstrated that CD150 receptor could trigger PI3K-mediated Akt signaling pathway in normal, EBV-transformed and malignant B cells. CD150-mediated phosphorylation of Akt downstream targets GSK-3beta and FoxO1 in EBV-transformed and HL cells could be one of the mechanisms to avoid apoptosis and support survival program in these immortalized B cells.

• Шлапацька Лариса Миколаївна (біологічні науки)
• Кашуба Олена Віталіївна (медичні науки)
• Снопок Борис Анатолійович (1965–) (фізико-математичні науки)
• Сидоренко Світлана Павлівна (1953–2018) (медичні науки)

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