Tumor necrosis factor receptor superfamily member 9(TNFRSF9); also known as CD137 and 4-1BB; is an inducible T cell surface protein belonging to the tumor necrosis factor receptor superfamily. It is a single-pass type I membrane protein which contains 4 TNFR-Cys repeats. The human and mouse proteins share 60% amino acid sequence identity. CD137 is expressed by mesenchymal cells; including endothelial cells; chondrocytes; and cells of the central nervous system. CD137 is also broadly expressed by cells of the human immune system; is broadly expressed by cells of the human immune system; including activated CD8+ and CD4+ T cells; activated natural killer (NK) cells; follicular dendritic cells (FDCs) and monocytes. CD137 has diverse roles in the immune response; the one key function is to promote the survival of both T cells and dendritic cells by binding the cognate ligand CD137L (4-1BBL).
Tumor necrosis factor receptor superfamily member 9(TNFRSF9) is an inducible T cell surface protein belonging to the TNF receptor superfamily. It is a single-pass type I membrane protein which contains 4 TNFR-Cys repeats. The human and mouse proteins share 60% amino acid sequence identity. It is absent from naive T cells; but upregulated and continually expressed following T cell activation. It is a receptor for TNFSF9/4-1BBL; and possibly active during T cell activation.
Eukaryotic Translation Initiation Factor 4E-Binding Protein 1 (4EBP1) is a number of the eIF4E-binding protein family. 4EBP1 regulates eIF4E activity by preventing its assembly into the eIF4F complex. 4EBP1 mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways. Non-phosphorylated 4EBP1 competes with EIF4G1/EIF4G3 to interact with EIF4E. 4EBP1 is phosphorylated in response to various signals including insulin signaling, resulting in its dissociation from eIF4E and activation of mRNA translation. 4EBP1 has a role in progression of breast neoplasms through cell signaling.
CD73 is a glycosyl phosphatidylinositol (GPI) anchored membrane protein that belongs to the 5'-nucleotidase family. CD73 is an ecto 5'Nucleotidase expressed by most cell types. CD73 hydrolyzes extracellular nucleotides into membrane permeable nucleosides. CD73 is one of several enzymes responsible for the production of extracellular adenosine, a signaling molecule that is involved in responses to inflammation and tissue injury. CD73 is a lymphocyte maturation marker that has functions independent of its catalytic activity. CD73 is also a regulator of leukocyte extravasation, a function that requires its 5'Nucleotidase activity. Defects in NT5E are the cause of calcification of joints and arteries (CAJA). The recombinant CD73 lacking GPI anchor is secreted as a monomer.
Alpha-1B-glycoprotein (A1BG) is an approximately 80 kDa molecule that circulates in the serum. Mature human A1BG consists of five tandem Ig like domains and shares 44% amino acid sequence identity with mouse and rat A1BG. Alternative splicing generates an isoform that lacks the signal peptide and the first Ig like domain. A1BG binds with high affinity to the cysteine rich protein CRISP-3. In pancreatic carcinoma, it is elevated in pancreatic juice as well as in the serum relative to normal patients. A1BG is abnormally excreted into the urine during idiopathic nephrotic syndrome (INS). Multiple breakdown fragments of A1BG are also present in INS urine, including one of 14 kDa that is found in steroid resistant but not steroid sensitive cases. A1BG is also elevated in the urine of patients with interstitial cystitis/painful bladder syndrome (IC/PBS).
alpha-2-macroglobulin, also known as α2-macroglobulin (α2M and A2M), is an abundant protein of the plasma of vertebrates and members of several invertebrate phyla and functions as a broad-spectrum protease-binding protein. alpha-2-macroglobulin is produced by the liver, and is a major component of the alpha-2 band in protein electrophoresis. alpha-2-macroglobulin is a large plasma glycoprotein that has long been known as an irreversible inhibitor of a variety of proteinases. More recently, it has been reported that numerous growth factors, cytokines and hormones bind to alpha 2M through diverse mechanisms. A2M is also produced in the brain where it binds multiple extracellular ligands and is internalized by neurons and astrocytes. In the brain of Alzheimer's disease (AD) patients, A2M has been localized to diffuse amyloid plaques. A2M also binds soluble beta-amyloid, of which it mediates degradation. Protease-conjugated alpha2-macroglobulin is selectively bound by cells contacting the body fluids and alpha2-macroglobulin and its protease cargo are then internalized and degraded in secondary lysosomes of those cells. In addition to this function as an agent for protease clearance, alpha2-macroglobulin binds a variety of other ligands, including several peptide growth factors and modulates the activity of a lectin-dependent cytolytic pathway in arthropods.
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