Low affinity immunoglobulin gamma Fc region receptor III-B; also known as Fc-gamma RIII-beta; FcR-10; IgG Fc receptor III-1; FCG3; FCGR3; CD16b and FCGR3B. FCGR3B is a GPI-anchor membrane protein and contains two Ig-like C2 type domains. FCGR3B can be expressed in orphonuclear leukocytes and stimulated eosinophils. FCGR3B can interact with INPP5D/SHIP1. FCGR3B localizes in the FCGR gene cluster is a CN polymorphic gene involved in the recruitment of polymorphonuclear neutrophils to sites of inflammation and their activation. FCGR3B may serve as a trap for immune complexes in the peripheral circulation which does not activate neutrophils.
The cluster of differentiation (CD) system is commonly used as cell markers in immunophynotyping. Different kinds of cells in the immune system can be identified through the surface CD molecules which associating with the immune function of the cell. There are more than 320 CD unique clusters and subclusters have been identified. Some of the CD molecules serve as receptors or ligands important to the cell through initiating a signal cascade which then alter the behavior of the cell. Some CD proteins do not take part in cell signal process but have other functions such as cell adhesion. Cluster of differentiation 24, also known as signal transducer CD24 or heat stable antigen CD24 (HSA), is a mucin-type glycosylphosphatidylinositol-linked glycoprotein expressed on the surface of B-cells, differentiating neuroblasts and many tumors. It is involved in molecular adhesion and metastatic tumor spread and serve as a normal receptor for P-selectin. The CD24 / P-selectin pathway could be important in dissimenating of tumor cells by facilitating the interaction with platelet and endothelial cells. It has also been considered as a tumor marker. High rate of CD24 expressions have been found in epithelial ovarian cancer, breast cancer, non-small cell lung cancer, prostate cancer and pancreatic cancer.
L1 cell adhesion molecule (L1CAM), also designated as CD171, is a cell adhesion receptor of the immunoglobulin superfamily, known for its roles in nerve cell function. While originally believed to be present only in brain cells, in recent years L1-CAM has been detected in other tissues, and in a variety of cancer cells, including some common types of human cancer. L1CAM interacts with a variety of ligands including axonin-1, CD9, neurocan and intergrins, and it has been revealed that the RGD motif in the sixth Ig domain of L1CAM is a binding site for integrins, thus important for nuclear signaling. Disruption of L1CAM function causes three X-linked neurological syndromes, i.e. hydrocephalus, MASA syndrome (mental retardation, aphasia, shuffling gait and adducted thumbs) and spastic paraplegia syndrome. Overexpression of L1CAM in normal and cancer cells increased motility, enhanced growth rate and promoted cell transformation and tumorigenicity. Recent work has identified L1CAM (CD171) as a novel marker for human carcinoma progression, and a candidate for anti-cancer therapy.
Signal Regulatory Protein α (SIRPα) is a monomeric approximately 90 kD type I transmembrane glycoprotein. The 504 amino acid human SIRPα contains two Ig-like C1-type domains and one Ig-like V-type domain. SIRPα can express in various tissues, mainly on brain and myeloid cells, including macrophages, neutrophils, dendritic and Langerhans cells. It also can detect in neurons, smooth muscle and endothelial cells. SIRPA is an immunoglobulin-like cell surface receptor for CD47. SIRPα acts as docking protein and induces translocation of PTPN6, PTPN11 and other binding partners from the cytosol to the plasma membrane. SIRPα shows adhesion of cerebellar neurons, neurite outgrowth and glial cell attachment. SIRPα engagement generally produces a negative regulatory signal; it may mediate negative regulation of phagocytosis, mast cell activation and dendritic cell activation
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