Neurexophilin-1, or NXPH1 is a secreted glycoprotein, which belongs to the Neurexophilin family. The Neurexophilin family contain at least four genes and resembles a neuropeptide, suggesting a function as an endogenous ligand for alpha-neurexins. The mammalian brains contain four genes for neurexophilins the products of which share a common structure composed of five domains: an N-terminal signal peptide, a variable N-terminal domain, a highly conserved central domain that is N-glycosylated, a short linker region, and a conserved C-terminal domain that is cysteine-rich. Neurexophilin-1 constitutes a secreted cysteine-rich glycoprotein, forms a very tight complex with alpha neurexins, a group of proteins that promote adhesion between dendrites and axons. Neurexophilins 1 and 3 but not 4 (neurexophilin 2 is not expressed in rodents) bind to a single individual LNS domain, the second overall LNS domain in all three alpha-neurexins.
Neuroligin 1 (NLGN1) belongs to the type-B carboxylesterase/lipase family, is a synaptic cell-adhesion molecule that is enriched in postsynaptic densities where it may recruit receptors, channels, and signal-transduction molecules to synaptic sites of cell adhesion. Neuroligins consist of five members (NLGN1, NLGN2, NLGN3, NLGN4 and NLGN4Y), which interact with beta-neurexins and this interaction is involved in the formation of functional synapses. The extracellular domain of functional Neuroligin 1 associates as a dimer when analyzed by sedimentation equilibrium. Neuroligin 1 has a unique N-linked glycosylation pattern in the neuroligin family, and glycosylation and its processing modify neuroligin activity. Neuroligin 1 is a potent trigger for the de novo formation of synaptic connections, and it has recently been suggested that it is required for the maturation of functionally competent excitatory synapses. The persistent expression of Neuroligin 1 is required for the maintenance of NMDAR-mediated synaptic transmission, which enables normal development of synaptic plasticity and long-term memory in the amygdala of adult animals.
The TRK Family of Tyrosine Kinase Receptor consists of 3 members: TrkA, TrkB and TrkC. The three TRK family proteins have different ligand specificities. They connect to different neurotrophins, including NGF, BDNF, NT-3NT-4/5. TRKA binds NGF, TRKB binds BDNF and NT-3, TRKC binds NT-4/5. At the protein sequence level, human and rat TRKB have greater than 90% sequence identity and the proteins exbihit cross-species activity. TRKB is primarily expressed in the nervous system and it also expression in a wide variety of tissues with low levels.
Neurturin is a member of the GDNF family of ligands, which include glial cell-derived neurotrophic factor (GDNF), Neurturin, Persephin, and Artemin. Neurturin is expressed in both neuronal and nonneuronal tissues. Similarly to other TGFβ family proteins, Neurturin is synthesized as a precursor protein that is cleaved at the dibasic cleavage site (RXXR) to release the carboxyterminal domain. The carboxy terminal domain of Neurturin contains the characteristic seven conserved cysteine residues necessary for the formation of the cysteine-knot and the single interchain disulfide bond. Biologically active human Neurturin is a disulfide-linked homodimer of the carboxy-terminal 102 amino acid residues. Unlike other members of TGF-β family, bioactivities of all GDNF family ligands are mediated through a unique multicomponent receptor complex composed of high affinity ligand binding component (GFRα-1-GFRα-4) and a common signaling component (cRET receptor tyrosine kinase). Each member of the GDNF family ligands has its preferred binding protein. Neurturin preferentially binds to GFRα-2 but can also bind GFRα-1 at higher concentrations. It may play a role in regulating the development and maintenance of the central and peripheral nervous systems and as well as non neuronal systems.
Plays a role in the inducible expression of cytokine genes in T-cells, especially in the induction of the IL-2 or IL-4 gene transcription. Also controls gene expression in embryonic cardiac cells. Could regulate not only the activation and proliferation but also the differentiation and programmed death of T-lymphocytes as well as lymphoid and non-lymphoid cells.
Lipocalin-2 (LCN2), also known as neutrophil gelatinase-associated lipocalin (NGAL), is a 25 kDa protein belonging to the lipocalin superfamily. It was initially found in activated neutrophils, however, many other cells, like kidney tubular cells, may produce NGAL in response to various insults. This protein is released from injured tubular cells after various damaging stimuli, is already known by nephrologists as one of the most promising biomarkers of incoming Acute Kidney Injury (AKI). Recent evidence also suggests its role as a biomarker in a variety of other renal and non-renal conditions. Moreover, recent studies seem to suggest a potential involvement of this factor also in the genesis and progression of chronic kidney diseases. NGAL is the first known mammalian protein which specifically binds organic molecules called siderophores, which are high-affinity iron chelators. NGAL, first known as an antibacterial factor of natural immunity, and an acute phase protein, is currently one of the most interesting and enigmatic proteins involved in the process of tumor development. acting as an intracellular iron carrier and protecting MMP9 from proteolytic degradation, NGAL has a clear pro-tumoral effect. In thyroid carcinomas, NGAL is strongly induced by NF-kB, an important factor involved both in tumor growth and in the link between chronic inflammation and neoplastic development. Thus, Lipocalin-2 (LCN2/NGAL) has been implicated in a variety of processes including cell differentiation, proliferation, survival and morphogenesis.
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