Bruton's tyrosine kinase (or BTK) is a type of kinase protein expressed in B lymphocytes and T cells. BTK contains a PH domain which binds phosphatidylinositol(3,4,5)-trisphosphate (PIP3). After binding to PIP3, BTK is induced to phosphorylate phospholipase C, which in turn hydrolyzes PIP2 into two second messagers, IP3 and DAG, which then modulate the activity of downstream proteins during B-cell signaling. Btk is also found implicated in the primary immunodeficiency disease X-linked agammaglobulinemia(Bruton's agammaglobulinemia). BTK played a key role in B-cell maturation as well as mast cell activation through the high-affinity IgE receptor. Patients with X-linked agammaglobulinemia have normal pre-B cell populations in their bone marrow but these B-cells can not mature and enter the circulation.
B- and T-Lymphocyte Attenuator (BTLA) is a single-pass type I membrane protein containing 1 Ig-like V-type (immunoglobulin-like) domain. BTLA expression is induced during activation of T cells, and BTLA remains expressed on Th1 cells but not Th2 cells. Like PD1 and CTLA4, BTLA interacts with a B7 homolog, B7H4. However, unlike PD-1 and CTLA-4, BTLA displays T-Cell inhibition via interaction with tumor necrosis family receptors (TNF-R), not just the B7 family of cell surface receptors. BTLA is a lymphocyte inhibitory receptor that inhibits lymphocytes during immune response. BTLA also is a ligand for tumor necrosis factor (receptor) superfamily, member 14 (TNFRSF14), also known as herpes virus entry mediator (HVEM). BTLA-HVEM complexes negatively regulate T-cell immune responses.
Butyrophilin 2A1 (BTN2A1) is an approximately widely expressed and variably glycosylated type I transmembrane glycoprotein. Mature human Butyrophilin 2A1 consisits of a 220 amino acid (aa) extracellular domain with two immunoglobulin-like domains, a 21 aa transmembrane segment, and a 258 aa cytoplasmic domain. Alternative splicing generates additional isoforms of human Butyrophilin 2A1 that lack the first Ig like domain or transmembrane segment as well as isoforms with substitutions and deletions in the cytoplasmic region. BTN2A1 is widely expressed including on colonic epithelial cells, on immune cells, and in milk fat globules. It binds to the C-type lectin DCSIGN on monocytederived dendritic cells, and this interaction can be blocked by soluble gp130 from HIV. The polymorphism of BTN2A1 has been associated with metabolic syndrome, type II diabetes mellitus, chronic kidney disease, and hypertension.
Butyrophilin 2A2 (BTN2A2) is a widely expressed type I transmembrane glycoprotein that functions as a negative regulator of immune responses. Mature human Butyrophilin 2A2 consisits of a 233 amino acid (aa) extracellular domain with two immunoglobulin-like domains, a 21 aa transmembrane segment, and a 237 aa cytoplasmic domain. Alternative splicing generates additional isoforms of human Butyrophilin 2A2 that lack the first, second, or both Iglike domains as well as isoforms with substitutions and deletions in the cytoplasmic region. Within the immune system, Butyrophilin 2A2 is expressed on thymic epithelial cells, naive B cells, splenic NK cells, dendritic cells, and peritoneal macrophages and is up-regulated with cell activation. Butyrophilin 2A2 inhibits T cell proliferation and activation and enhances the development of FoxP3+ regulatory T cells. Its up-regulation in the hippocampus is associated with schizophrenia.
Butyrophilin Subfamily 3 Member A1 (BTN3A1/CD277) is a type I transmembrane glycoprotein member of the Ig superfamily. It is expressed on a wide variety of immune cells. Similar to BTN3A2 and BTN3A3, BTN3A1 is composed of an extracellular N-terminal IgV and a membraneproximal IgC domain followed by a transmembrane domain and a cytoplasmic tail. These Ig domains are also found in B7 family costimulatory molecules, suggesting structural and functional similarities between the two protein families. BTN3A1 acts as a critical protein for the activation of Vγ9Vδ2 T cells following detection of distressed cells. The anti-tumor responses of Vγ9Vδ2 T cells may be enhanced with agonistic anti-BTNA3 antibodies.
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