关于IL-18BP:
Interleukin-18-binding protein, also known as Tadekinig-alfa and IL18BP, contains 1 Ig-like C2-type domain. IL18BP is constitutively expressed and secreted in mononuclear cells. IL18BP functions as an IL18 inhibitor. IL18BP binds to IL18, prevents the binding of IL18 to its receptor, and thus inhibits IL18-induced IFN-gamma production. It has been shown that IL18BP may be a promising molecular approach to inhibit neointimal hyperplasia and arteriosclerosis progression following coronary and peripheral angioplasty.
关于THSD1:
Thrombospondin Type-1 Domain-Containing Protein 1 (THSD1) is a single-pass type I membrane protein. THSD1 contains a signal peptide and one TSP type-1 domain that is found in thrombospondin. THSD1 is a good novel candidate for TSG as it has been mapped to 13q14. Alternatively spliced transcript variants encoding distinct isoforms have been observed. THSD1 may be involved in the complement pathway.
关于SLAMF7/CD319:
SLAMF7 is a single-pass type I membrane protein and contains 1 Ig-like C2-type (immunoglobulin-like) domain. SLAMF7 is expressed in NK cells, activated B-cells, NK-cell line but not in promyelocytic, B-cell lines, or T-cell lines. Although the cytoplasmic domain of CS1 contains immunoreceptor tyrosine-based switch motifs (ITSM), which enables to recruite signaling lymphocyte activation molecule (SLAM)-associated protein (SAP/SH2D1A), it activates NK cells in the absence of a functional SAP. SLAMF7 positively regulated natural killer cell functions by a mechanism dependent on the adaptor EAT-2 but not the related adaptor SAP. However, in the absence of EAT-2, CRACC potently inhibited natural killer cell function. It was also inhibitory in T cells, which are typically devoid of EAT-2. Thus, SLAMF7 can exert activating or inhibitory influences on cells of the immune system depending on cellular context and the availability of effector proteins.