Ptx3, also known as tumor necrosis factor-stimulated gene sequence-14 (TSG14), is a secreted pattern-recognition receptor that has a non-redundant role in resistance to selected microbial agents. Ptx3 belongs to the family of “long pentraxins”, which have C-terminal pentraxin domains and novel amino-terminal domains. Ptx3 binds selected pathogens, including Aspergillus fumigatus, Pseudomonas aeruginosa and Salmonella typhimurium. It is synthesized in IgA glomerulonephritis and activates mesangial cells.
Essential mediator of p53/TP53-dependent and p53/TP53-independent apoptosis . Functions by promoting partial unfolding of BCL2L1 and dissociation of BCL2L1 from p53/TP53. Regulates ER stress-induced neuronal apoptosis.
RGMa, also known as RGM domain family, member A, belongs to the RGM (repulsive guidance molecule) family whose members are membrane-associated glycoprotein. RGMa is a glycosylphosphatidylinositol-anchored glycoprotein that functions as an axon guidance protein in the developing and adult central nervous system. It helps guide Retinal Ganglion Cell (RGC) axons to the tectum in the midbrain. RGMa has been implicated to play an important role in the developing brain and in the scar tissue that forms after a brain injury. This protein may also function as a tumor suppressor in some cancers.
Human PVRIG (poliovirus receptor related immunoglobulin domain-containing protein), also known as CD112 receptor (CD112R), is an approximately 34 kDa single transmembrane protein in the poliovirus receptor-like protein (PVR) family. The extracellular domain sequence of human and mouse PVRIG have approximately 65% similarity. PVRIG functions as a cell surface receptor for Nectin-2/CD112, a cell surface protein that is widely expressed on antigen-presenting cells and tumor cells. Disrupting the PVRIG/Nectin-2 interaction enhances human T cell response, suggesting PVRIG is a novel checkpoint for human T cells. PVRIG may act as a coinhibitory receptor that suppresses T-cell receptor-mediated signals.
Nectin-1 is a type I transmembrane glycoprotein belonging to the Ig superfamily. Nectin-1 promotes cell-cell contacts by forming homophilic or heterophilic trans-dimers. Heterophilic interactions have been detected between Nectin-1 and Nectin-3 and between Nectin-1 and Nectin-4. Nectin ECDs contain three Ig like domains: an N terminal V type that mediates ligand binding, and two C2 type. Nectin-1 binds viral Glycoprotein D to mediate Herpesvirus (but not Poxvirus) entry into vaginal mucosa, sensory neurons and fibroblasts. In forming adherens junctions and synapses, Nectin-1 and Nectin-3 initiate cell-cell interactions, recruiting αvβ3 integrin extracellularly and cadherins intracellularly through afadin and other junctional proteins. These interactions organize the cytoskeleton, strengthen attachment to basement membrane and promote further cell-cell connections. Nectin-1 and Nectin-3 have been found to localize assymetrically along the chemical synapse, with Nectin-1 primarily on the axonal side and Nectin-3 on the dendritic side. Deficiency of Nectin-1 can result in cleft lip/palate ectodermal dysplasia. Nectin-1 downregulation in epithelial cancers is mediated in part by ectodomain shedding, but it may contribute to invasiveness.
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