Programmed death-1 ligand-1 (PD-L1, CD274, B7-H1) has been identified as the ligand for the immunoinhibitory receptor programmed death-1(PD1/PDCD1) and has been demonstrated to play a role in the regulation of immune responses and peripheral tolerance. PD-L1/B7-H1 is a member of the growing B7 family of immune molecules and this protein contains one V-like and one C-like Ig domain within the extracellular domain, and together with PD-L2, are two ligands for PD1 which belongs to the CD28/CTLA4 family expressed on activated lymphoid cells. By binding to PD1 on activated T-cells and B-cells, PD-L1 may inhibit ongoing T-cell responses by inducing apoptosis and arresting cell-cycle progression. Accordingly, it leads to growth of immunogenic tumor growth by increasing apoptosis of antigen specific T cells and may contribute to immune evasion by cancers. PD-L1 thus is regarded as promising therapeutic target for human autoimmune disease and malignant cancers.
Programmed Cell Death 1 Ligand 2 (PDCD1LG2) is a member of the BTN/MOG family. PDCD1LG2 contains one Ig-like C2-type domain and one Ig-like V-type domain. PDCD1LG2 is highly expressed in the heart; placenta; pancreas; lung and liver; it is weakly expressed in the spleen; lymph nodes; and thymus. PDCD1LG2 is involved in the costimulatory signal; essential for T-cell proliferation and IFNG production in a PDCD1-independent manner. PDCD1LG2 interaction with PDCD1 inhibits T-cell proliferation by blocking cell cycle progression and cytokine production.
Programmed Cell Death 1 Ligand 2 (PDCD1LG2) is a member of the BTN/MOG family. PDCD1LG2 contains one Ig-like C2-type domain and one Ig-like V-type domain. PDCD1LG2 is highly expressed in the heart, placenta, pancreas, lung and liver, it is weakly expressed in the spleen, lymph nodes, and thymus. PDCD1LG2 is involved in the costimulatory signal, essential for T-cell proliferation and IFNG production in a PDCD1-independent manner. PDCD1LG2 interaction with PDCD1 inhibits T-cell proliferation by blocking cell cycle progression and cytokine production.
PDZ domain-containing protein 11, also known as AIPP1a, PISP, PDZD11 and PDZK11, is a cytosolic protein which contains onePDZ (DHR) domain. PDZD11 bears resemblance to members of the MALS / VELIS family of proteins. It contains but one PDZ domain that apparently interacts with the C-terminus of partner proteins. PDZD11 is ubiquitously expressed, and appears to target calcium and copper ATPases to basolateral cell membranes. PDZD11 is a transiently interacting partner of the PMCA b-splice forms that may play a role in their sorting to or from the plasma membrane. Full-length human PDZD11 shares 97% amino acids (aa) identity with mouse PDZD11.
CD31, also known as platelet endothelial cell adhesion molecule-1 (PECAM-1), is a 130 kDa heavily glycosylated transmembrane protein belonging to the immunoglobulin (Ig) superfamily of cell adhesion molecules. CD31 is highly expressed on endothelial cells and at a lower level on platelets, granulocytes, macrophages, dendritic cells, T and B cells, and natural killer (NK) cells. It is involved in cell adhesion and is required for transepithelial migration of leukocytes (TEM). CD31 is composed of an extracellular domain (ECD) of 574 amino acids containing six Ig-like domains, a transmembrane domain, and a 118 aa cytoplasmic domain. The latter undergoes alternative splicing which generates multiple isoforms showing altered adhesive properties compared to full length CD31. The human CD31 ECD shares 63% and 61% aa sequence identity with mouse and rat CD31, respectively. CD31 acts as a homophilic receptor through its extracellular domain and is involved in downstream signaling via its cytoplasmic domain. This domain contains highly conserved ITIM motifs which, once tyrosine phosphorylated, recruit and activate the signaling molecules Src and SHP-2. The resulting inhibition of TCR signaling increases the activation threshold of T cells, thus reinforcing peripheral tolerance and preventing development of autoimmunity. CD31 additionally regulates immune responses by acting as a key inhibitory receptor in dendritic cell development. Besides its role in TEM, CD31 appears to regulate T cell trafficking through a complex coordination of endothelial cell junctions and T cell extravasation.
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