Neurotrimin is a glycoprotein. It belongs to the immunoglobulin superfamily and IgLON family. Neurotrimin localizes to the cell membrane and contains three Ig-like C2-type domains. Neurotrimin acts as a glycosylphosphatidylinositol (GPI)-anchored neural cell adhesion molecule. Neurotrimin may promote neurite outgrowth and adhesion via homophilic and heterophilic interactions.
Neurotrophin-3 (NT-3) is a member of the NGF family of neurotrophic factors and is structurally related to β-NGF, BDNF and NT-4. The NT3 cDNA encodes a 257 amino acid residue precursor protein with a signal peptide and a proprotein that are cleaved to yield the 119 amino acid residue mature NT3.The amino acid sequences of mature human, murine and rat NT-3 are identical. NT-3 selectively promotes the differentiation and survival of specific neuronal subpopulations in both the central as well as the peripheral nervous systems.
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.
Neutrophil cytosol factor 1( NCF1) is a 47 kDa cytosolic subunit of neutrophil NADPH oxidase. This oxidase is characterized as a multicomponent enzyme which is activated to produce superoxide anion. NCF2, NCF1, and a membrane bound cytochrome b558 are required for the activation of the latent NADPH oxidase. The human NCF1 gene encodes a 390 amino acids protein without a signal peptide. The NCF1 gene interacts with other subunits of nicotinamide adenine dinucleotide phosphate-oxidase (NADPH) and plays an important role in innate immunity, producing reactive oxygen species and reducing the severity and duration of parasitic infection and autoimmune disease. NCF1 also has a role in T cell activation.
NFASC, also known as neurofascin, belongs to the immunoglobulin superfamily, L1/neurofascin/NgCAM family. It contains 5 fibronectin type-III domains and 6 Ig-like C2-type (immunoglobulin-like) domains. NFASC functions in neurite outgrowth, neurite fasciculation, and organization of the axon initial segment (AIS) and nodes of Ranvier on axons during early development. Both the AIS and nodes of Ranvier contain high densities of voltage-gated Na+ (Nav) channels which are clustered by interactions with cytoskeletal and scaffolding proteins including this protein, gliomedin, ankyrin 3 (ankyrin-G), and betaIV spectrin. NFASC links the AIS extracellular matrix to the intracellular cytoskeleton.
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