CD27 antigen, also known as CD27L receptor, T-cell activation antigen CD27, T14, S152, Tp55, TNFRSF7 and Tumor necrosis factor receptor for superfamily member 7,belongs to the TNF-receptor superfamily. CD27 is a single-pass type I membrane protein and exists as a homodimer form, containing three TNFR-Cys repeats. CD27 transduces signals that lead to the activation of NF-KappaB and MAPK8/JNK. CD27 is involved in regulating B-cell activation and immunoglobulin synthesis, binding to the ligand CD70. TRAF2 and TRAF5 have been shown to mediate the signaling process of CD27. CD27-binding protein (SIVA), which is a proapoptotic protein, can bind to CD27 and is thought to play a key role in the apoptosis. CD27 is required for generation and long-term maintenance of T cell immunity.
CD47, also known as Integrin-Associated Protein (IAP) and OA3, is a glycosylated atypical member of the immunoglobulin superfamily. Mouse CD47 is an integral membrane protein that consists of a extracellular domain (ECD) with a single Ig like domain, five membrane-spanning regions with short intervening loops, and C-terminal cytoplasmic tail. CD47 has a role in both cell adhesion by acting as an adhesion receptor for THBS1 on platelets, and in the modulation of integrins. It plays an important role in memory formation and synaptic plasticity in the hippocampus. As a receptor for SIRPA, it binding to which prevents maturation of immature dendritic cells and inhibits cytokine production by mature dendritic cells. Interaction with SIRPG mediates cellcell adhesion, it enhances superantigen-dependent T-cell-mediated proliferation and costimulates T-cell activation. It may play a role in membrane transport and/or integrin dependent signal transduction. It also prevents premature elimination of red blood cells.
CD47(Integrin-Associated Protein,IAP) is a 40-60 kDa variably glycosylated atypical member of the immunoglobulin superfamily. The ubiquitously expressed CD47 binds to SIRP family members on macrophages, neutrophils, and T cells. CD47 is involved in the increase in intracellular calcium concentration that occurs upon cell adhesion to extracellular matrix. The protein is also a receptor for the C-terminal cell-binding domain of thrombospondin, and it may play a role in membrane transport and signal transduction. This protein has broad tissue distribution, and is reduced in expression on Rh erythrocytes.
CD79B is a single-pass type I membrane protein. CD79B contains one Ig-like V-type domain and one ITAM domain. CD79B is required in cooperation with CD79A for initiation of the signal transduction cascade activated by the B-cell antigen receptor complex (BCR), which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. CD79B enhances phosphorylation of CD79A, possibly by recruiting kinases that phosphorylate CD79A or by recruiting proteins that bind to CD79A and protect it from dephosphorylation.
Glypican-3/GPC3 is a member of the glypican family. It belongs to the glypican family and is highly expressed in lung, liver, and kidney. It is a heparan sulfate proteoglycan, which is overexpressed in various neoplasms such as hepatocellular carcinoma, malignant melanoma, and testicular yolk sac tumor, and plays an important role in cell growth and differentiation. GPC3 function is tissue dependent. In some tissues, GPC3 acts as a tumor suppressor gene, whereas in others, it acts as an oncofetal protein. GPC3 is a reliable marker for hepatocellular carcinoma. The sensitivity and specificity exceeds both alpha-fetoprotein and hepatocyte-paraffin1. GPC3 immunohistochemistry can aid in the differentiation of testicular germ cell tumors, being expressed in all yolk sac tumors but not in seminomas. GPC3 expression has also been identified in some squamous cell carcinomas of the lung and clear cell carcinomas of the ovary. Glypican-3 is currently regarded as a tumor marker and potential target for immunotherapy.
Herpesvirus entry mediator (HVEM) is a type I membrane protein in the TNF receptor superfamily, and it can both promote and inhibit T cell activity. HVEM is highly expressed on naïve CD4+ T cells, CD8+ T memory cells, regulatory T cells, dendritic cells, monocytes, and neutrophils. It functions as a receptor for BTLA, CD160, LIGHT/TNFSF14, and Lymphotoxin-alpha. Ligation of HVEM by LIGHT triggers T cell, monocyte, and neutrophil activation and contributes to Th1 inflammation and cardiac allograft rejection. In contrast, HVEM binding to CD160 or BTLA suppresses T cell and dendritic cell activation and dampens intestinal inflammation. HVEM enhances the development of CD8+ T cell memory and Treg function. It is additionally expressed on intestinal epithelial cells, where its binding by intraepithelial lymphocyte (IEL) expressed CD160 promotes epitheilal integrity and host defense. The herpesvirus envelope glycoprotein gD, which binds HVEM to initiate membrane fusion, can antagonize both BTLA and LIGHT binding.
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