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.
Tumor Necrosis Factor Receptor Superfamily Member 1B (TNFRSF1B) is a member of the Tumor Necrosis Factor Receptor Superfamily. TNFRSF1B contains four TNFR-Cys repeats. TNFRSF1B can be cleaved into the following 2 chains: Tumor necrosis factor receptor superfamily member 1b and membrane form and Tumor necrosis factor-binding protein 2. TNFRSF1B is a receptor with high affinity for TNFSF2/TNF-α and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-α. TNFRSF1B mediates most of the metabolic effects of TNF-α. TNF-α-induced apoptosis suggests that it regulates TNF-α function by antagonizing its biological activity.
Tumor associated calcium signal transducer 2 (TACSTD2, TROP-2) is a type I cell surface glycoprotein that is highly expressed on human carcinomas. It was originally identified as an antigen present on human gastrointestinal tumors and is the second of two members of this family. Human and mouse TROP-2 share 87% amino acid (aa) similarity. TROP-2 is capable of transducing an intracellular calcium signal and may play a role in tumor growth. It also has adhesive functions.
IGF I, also known as Mechano Growth Factor, somatomedin-C, IGF-I, and IGF1, is a secreted protein that belongs to the insulin family. The insulin family, comprised of insulin, relaxin, insulin-like growth factors I and II ( IGF-I and IGF-II ), and possibly the beta-subunit of 7S nerve growth factor, represents a group of structurally related polypeptides whose biological functions have diverged. The IGFs, or somatomedins, constitute a class of polypeptides that have a key role in pre-adolescent mammalian growth. IGF-I expression is regulated by GH and mediates postnatal growth, while IGF-II appears to be induced by placental lactogen during prenatal development. IGF1 / IGF-I may be a physiological regulator of [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblasts. IGF1 / IGF-I stimulates glucose transport in rat bone-derived osteoblastic (PyMS) cells and is effective at much lower concentrations than insulin, not only regarding glycogen and DNA synthesis but also about enhancing glucose uptake. Defects in IGF1 / IGF-I are the cause of insulin-like growth factor I deficiency (IGF1 deficiency) which is an autosomal recessive disorder characterized by growth retardation, sensorineural deafness, and mental retardation.
This gene encodes a member of the Rho family of small GTPases, which cycle between inactive GDP-bound and active GTP-bound states and function as molecular switches in signal transduction cascades. Rho proteins promote reorganization of the actin cytoskeleton and regulate cell shape, attachment, and motility. Overexpression of this gene is associated with tumor cell proliferation and metastasis. Multiple alternatively spliced variants have been identified.
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