Natural Cytotoxicity Triggering Receptor 3 (NCR3) along with NKp44 and NKp46 constitute a group of receptors termed “Natural Cytotoxicity Receptors”. They play a major role in triggering NK-mediated killing of most tumor cells lines. NKp30 is a type I transmembrane protein having a single extracellular V-like immunoglobulin domain. NKp30 is selectively expressed both in resting and activated human NK cells. In addition; NKp30 is also involved in NK-mediated induction of dendritic cell (DC) maturation. It has been demonstrated that NK cell activation signaling specifically induces lytic activity against several tumor cell types and synthesis of new NF-κB dependent proteins during the initiation of cytotoxicity.
Protein NDRG1 is a member of the N-Myc Downregulated Gene family, which is part of the α/β Hydrolase superfamily. Protein NDRG1 is a cytoplasmic protein that is involved in stress responses, hormone responses, cell growth and differentiation. Protein NDRG1 is necessary for p53-mediated caspase activation and apoptosis. Protein NDRG1 mutuations are reported to be the cause for hereditary motor and sensory neuropathy-Lom. Decreased NDRG1 expression in glioma is linked to tumor progression; overexpression of NDRG1 is connected to malignant status of esophageal cancer.
NECAP2 belongs to the NECAP family. The WXXF motifs mediate binding of accessory proteins to the ear-domain of AP-1, GGAs and AP-2 through hydrophobic interactions. Adaptin ear-binding coat-associated protein 2 can interacts with AP1G1 and AP2A1 components of the adapter protein complex AP-1 and AP-2. It also interacts with the GAE domain proteins GGA1, GGA2 and GGA3.
CD112 is a type I transmembrane glycoprotein belonging to the Immunoglobulin superfamily. It comprises one Ig-like V-type domain and two Ig-like C2-type domains in the extracellular region. The V domain is believed to mediate nectin binding to its ligands. Nectin2 is known to bind the pseudorabies virus, and herpes simplex virus2 (HSV2), involving in cell to cell spreading of these viruses. It does not bind poliovirus. As a homophilic adhesion molecule, CD112 is found concentrated in adherens junctions, and exists on neurons, endothelial cells,epithelial cells and fibroblasts. CD112 has been identified as the ligand for DNAM-1 (CD226), and the interaction of CD226/CD112 mediates cytotoxicity and cytokine secretion by T and NK cells. The costimulatory responses may be a critical component in allergic reactions and may therefore become targets for anti-allergic therapy.
Poliovirus receptor-related 3 (PVRL3), also known as Nectin-3 and CD113, is a member of the nectin family. PVRL3/Nectin-3 is an 83 kDa, type I transmembrane glycoprotein. Its precursor is 549 amino acids (aa) in length and contains an extended signal sequence of 57 aa, an extracellular domain (ECD) of 347 aa, a transmembrane segment of 21 aa, and a cytoplasmic region of 124 aa. Nectin-3 has three splicing variants, nectin-3alpha (biggest), -3beta (middle), and -3gamma (smallest). It is predominantly expressed in testis and placenta as well as in various cell lines, including epithelial cell lines. PVRL3/Nectin-3 plays a role in cell-cell adhesion through heterophilic trans-interactions with nectin-like proteins or nectins, such as trans-interaction with PVRL2/Nectin-2 at Sertoli-spermatid junctions. PVRL3/Nectin-3 is thus involved in the formation of cell-cell junctions, including adherens junctions and synapses. It has been shown to induce endocytosis-mediated down-regulation of PVR from the cell surface, resulting in reduction of cell movement and proliferation.
Nectin-3 is a type I transmembrane glycoprotein that belongs to the nectin family. Its precursor is 549 amino acids in length and contains an extended signal sequence of 57 amino acids, an extracellular domain (ECD) of 347 amino acids, a transmembrane segment of 21 amino acids, and a cytoplasmic region of 124 amino acids. It is predominantly expressed in testis and placenta as well as in various cell lines, including epithelial cell lines. Nectin-3 plays a role in cell-cell adhesion through heterophilic trans-interactions with nectin-like proteins or nectins, such as trans-interaction with PVRL2/Nectin-2 at Sertoli-spermatid junctions. Nectin-3 is also involved in the formation of cell-cell junctions, including adherens junctions and synapses.
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