Introduction
B lymphocytes can directly participate in humoral immune responses as immune effector cells, and can also be used as antigen-presenting cells to capture antigens and present them to T lymphocytes. B cells mediate foreign antigen signals and complex biological effects, including B cell activation, proliferation, and differentiation, through their surface B cell receptors (BCR). This process involves a series of downstream signal transduction pathways that interweave to form a very complex B cell receptor signal transduction regulatory network. Many non-Hodgkin's lymphomas (NHL) originate from B lymphocytes. B cell receptor (BCR) complexes and their related protein kinases play important roles in the development, proliferation and survival of normal and malignant B cells. After the concept of antigen stimulation to induce lymphoma production, the BCR receptor signaling pathway has become an important pathway for lymphoma growth and survival. Therefore, various kinases in BCR and its signaling pathways can be new targets for lymphoma therapy.
BCR structure and function BCR is a heterologous oligomeric complex composed of membrane immunoglobulin (mIg) and Igα (CD79A)/Igβ (CD79B), which is one of the characteristic markers of B cells. mIg recognizes and binds antigens. The intracellular regions of Igα and Igβ have an immunoreceptor tyrosine-based activation motif (ITAM), which is involved in the transduction of antigenic stimulation signals after phosphorylation.
BCR signal transduction pathway
PLC-γ2 mediated signaling pathway BCR/Igα/Igβ complex enters the lipid raft on the B cell surface after BCR is stimulated by antigen. Activation of Lyn (SRC family kinases) phosphorylates ITAM in the cytoplasmic region of Igα/Igβ. Then Syk (spleen tyrosine kinase) is recruited to the lipid raft and then be phosphorylated. Activated Syk can phosphorylate B cell linker protein (BLNK) and CIN85 (Cbl-interacting protein of 85 ku), and then bind to phospholipase C-γ2 (phospholipase C-γ2, PLC-γ2) with Btk (Bruton tyrosine kinase). Activated PLC-γ2 hydrolyzes the membrane substrate PIP2 to generate a second messenger IP3 and DAG. Binding of IP3 to the IP3 receptor on the endoplasmic reticulum membrane opens the membrane Ca2++ channel and intracellular calcium stores, resulting in an increase in intracytoplasmic Ca2++ concentration. The calcineurin is then activated to dephosphorylate the transcription factor NFAT (phosphorylated factor NFAT) to activate and mediate the NFAT pathway. DAG can bind protein kinase Cβ (PKCβ) to the inner side of the cell membrane.
BCR structure and function BCR is a heterologous oligomeric complex composed of membrane immunoglobulin (mIg) and Igα (CD79A)/Igβ (CD79B), which is one of the characteristic markers of B cells. mIg recognizes and binds antigens. The intracellular regions of Igα and Igβ have an immunoreceptor tyrosine-based activation motif (ITAM), which is involved in the transduction of antigenic stimulation signals after phosphorylation.
BCR signal transduction pathway
PLC-γ2 mediated signaling pathway BCR/Igα/Igβ complex enters the lipid raft on the B cell surface after BCR is stimulated by antigen. Activation of Lyn (SRC family kinases) phosphorylates ITAM in the cytoplasmic region of Igα/Igβ. Then Syk (spleen tyrosine kinase) is recruited to the lipid raft and then be phosphorylated. Activated Syk can phosphorylate B cell linker protein (BLNK) and CIN85 (Cbl-interacting protein of 85 ku), and then bind to phospholipase C-γ2 (phospholipase C-γ2, PLC-γ2) with Btk (Bruton tyrosine kinase). Activated PLC-γ2 hydrolyzes the membrane substrate PIP2 to generate a second messenger IP3 and DAG. Binding of IP3 to the IP3 receptor on the endoplasmic reticulum membrane opens the membrane Ca2++ channel and intracellular calcium stores, resulting in an increase in intracytoplasmic Ca2++ concentration. The calcineurin is then activated to dephosphorylate the transcription factor NFAT (phosphorylated factor NFAT) to activate and mediate the NFAT pathway. DAG can bind protein kinase Cβ (PKCβ) to the inner side of the cell membrane.
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