By Louis B. Justement (auth.), Louis B. Justement Ph.D., Professor Katherine A. Siminovitch M.D. (eds.)
Proper improvement and differentiation of B lymphocytes is es sential to make sure that an organism has the power to mount a good humoral immune reaction opposed to international antigens. The immune process needs to keep a stability among the deletion of destructive self-reactive B cells and the iteration of a various rep ertoire of B cells that has the facility to acknowledge a nearly un restricted array of overseas antigens. the necessity to delete self-reactive cells is tempered by means of the necessity to steer clear of the iteration of enormous practical holes within the repertoire of international antigen-specific B cells that patrol the outer edge. to complete this, the immune method needs to succeed in a compromise by way of casting off simply the main harmful autoreactive clones, whereas permitting much less destructive au toreactive B cells to exist within the outer edge the place they might com plement the organism's skill to mount a fast reaction opposed to invading micro-organisms. these autoreactive cells that do input the peripheral pool are topic to a few conditional re straints that successfully attenuate their skill to answer self antigens. Deleterious changes within the homeostasis among tolerance induction and recruitment of B cells into the practical repertoire could lead to elevated susceptibility to autoimmune ailment or an infection, respectively. consequently, delineation of the molecular strategies that continue immunological homeostasis within the B cellphone compartment is critical.
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Additional info for Signal Transduction and the Coordination of B Lymphocyte Development and Function I: Transduction of BCR Signals from the Cell Membrane to the Nucleus
1996). Due to the presence of these functional domains, it is possible that Vav regulates signaling via the BCR through one or more distinct processes. It has been shown that Yav is inducibly phosphorylated on tyrosine residues in response to BCR cross-linking (BUSTELO and BARBACID 1992; GULBINS et al. 1994). The yeast two-hybrid system has been used to demonstrate that Vav physically interacts with the PTK Syk (DECKERT et al. 1996). The association between these proteins requires the catalytic activity of Syk, the SH2 domain of Vav and specific tyrosine residues located in the linker domain of Syk.
In either instance, the loss of SHPI activity severely alters normal B-cell function due to dysregulation of BCRdependent signal transduction. 1 SHP-1 Negatively Regulates Signal Transduction via the BCR The abnormal expansion of CD5 + B cells in me and me v mice and the associated high levels of serum immunoglobulins, autoantibodies and B-cell lymphokines provided an initial indication that SHP-I function is associated with attenuation of B-cell activation, presumably through its ability to attenuate BCR-mediated signal transduction.
Cross-linking of the BCR mediates activation of Src family protein tyrosine kinases (PTKs), which in turn phosphorylate one or more inhibitory receptors that contain immunoreceptor tyrosine-based inhibition motifs (ITIMs) within their respective cytoplasmic domains. Tyrosine phosphorylation of the ITIMs promotes the recruitment and activation of SHP-l, which binds to the phosphorylated inhibitory molecule via its dual SH2 domains. This effectively targcts active SHP-l to the BCR complex under specific conditions, depending on the particular inhibitory receptor involved.