Ciliary neurotrophic factor (CNTF) is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. It was initially identified as a trophic factor for embryonic chick ciliary parasympathetic neurons in culture. The protein is also a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. In addition, CNTF is useful for treatment of motor neuron disease and it could reduce food intake without causing hunger or stress. CNTF is structurally related to IL6, IL11, LIF, and OSM. All of these four helix bundle cytokines share gp130 as a signal-transducing subunit in their receptor complexes.

Ciliary neurotrophic factor (CNTF) is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. It was initially identified as a trophic factor for embryonic chick ciliary parasympathetic neurons in culture. The protein is also a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. In addition, CNTF is useful for treatment of motor neuron disease and it could reduce food intake without causing hunger or stress. CNTF is structurally related to IL6, IL11, LIF, and OSM. All of these four helix bundle cytokines share gp130 as a signal-transducing subunit in their receptor complexes.

Glial cell-derived neurotrophic factor (GDNF) is a small protein that promotes the survival of various neuronal subpopulations in both the central as well as the peripheral nervous systems at different stages of their development. GDNF is a founding member of the GDNF family of ligands (GFL) and has been shown to interact with GFRA2 and GDNF family receptor alpha 1. GDNF (monomer) contains seven conserved cysteine residues, one of which (Cys 101) is used for inter-chain disulfide bridging and the others are involved in intramolecular ring formation known as the cystine knot configuration.

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Glia maturation factor beta is an actin-binding protein that shows sequence similarity to the ADF/ cofilin family. It is expressed in the cytosol and on the cell surface of astrocytes and interacts with target receptors in a juxtacrine manner. GMFB is involved in the differentiation of glial cells and neurons. It stimulates axon regeneration and proliferation of astroblasts, and inhibits proliferation of tumors. It also reversibly inhibits proliferation of neuronal and non-neuronal neoplastic cells by arresting the cell cycle in the G0/G1 phase. It is suggested that GMFB acts an intracellular regulator of signal pathways.

Glia maturation factor beta is an actin-binding protein that shows sequence similarity to the ADF/ cofilin family. It is expressed in the cytosol and on the cell surface of astrocytes and interacts with target receptors in a juxtacrine manner. GMFB is involved in the differentiation of glial cells and neurons. It stimulates axon regeneration and proliferation of astroblasts, and inhibits proliferation of tumors. It also reversibly inhibits proliferation of neuronal and non-neuronal neoplastic cells by arresting the cell cycle in the G0/G1 phase. It is suggested that GMFB acts an intracellular regulator of signal pathways. Analysis of crystallography and NMR reveals structural differences between murine and human ADF-H domains.

MANF is a secreted neurotrophic factor that is expressed in brain, neuronal and certain non-neuronal tissues. It has been shown to promote survival, growth and function of dopamine specific neurons. MANF and its structural homolog CDNF each contain an N-terminal saposin-like lipid binding domain and a carboxyl-terminal domain, which is not homologous to previously characterized protein structures. MANF has been identified as a soluble ER stress protein induced by the unfolded protein response. MANF and CDNF can prevent 6-OHDA induced degeneration of dopaminergic neurons by triggering survival pathways, as shown in a rat experimental model of Parkinson disease.

Midkine (MDK) is a heparin-binding growth factor that is expressed in various cell types during embryo development and in a variety of carcinomas. It is induced by retinoic acid, as well as during oncogenesis, inflammation, and tissue repair. MDK is pleiotropic and promotes angiogenesis, neurogenesis, chondrogenesis, cell growth, cell migration, and tumorigenesis. It also inhibits apoptosis in some cells. MDK acts through several different receptors including PTP, ALK, PTP-zeta, and LRP. The amino acid sequence of human MDK is about 50% homologous to human pleiotrophin (PTN).

Midkine (MDK) is a heparin-binding growth factor that is expressed in various cell types during embryo development and in a variety of carcinomas. It is induced by retinoic acid, as well as during oncogenesis, inflammation, and tissue repair. MDK is pleiotropic and promotes angiogenesis, neurogenesis, chondrogenesis, cell growth, cell migration, and tumorigenesis. It also inhibits apoptosis in some cells. MDK acts through several different receptors including PTP, ALK, PTP-zeta, and LRP. MDK shows significant homology to pleiotrophin (PTN).

Midkine (MDK) is a heparin-binding growth factor that is expressed in various cell types during embryo development and in a variety of carcinomas. It is induced by retinoic acid, as well as during oncogenesis, inflammation, and tissue repair. MDK is pleiotropic and promotes angiogenesis, neurogenesis, chondrogenesis, cell growth, cell migration, and tumorigenesis. It also inhibits apoptosis in some cells. MDK acts through several different receptors including PTP, ALK, PTP-zeta, and LRP. MDK shows significant homology to pleiotrophin (PTN). The amino acid sequence of Rat MDK is 99% homologous to human MDK.

Neuregulin 1 belongs to a family of structurally related polypeptide growth factors and is produced in numerous isoforms by alternative splicing, which allows it to perform a wide variety of functions. These isoforms include heregulins (HRGs), glial growth factors (GGFs) and sensory and motor neuron-derived factor (SMDF). They all have the EGF-like domain, and can bind to ErbB3 and ErbB4 receptor tyrosine kinases. This binding induces ErbB3 and ErbB4 heterodimerization with ErbB2, stimulating intrinsic kinase activity. This product is the EGF-like domain of isoform 1. NRG1 isoforms induce the growth and differentiation of epithelial, neuronal, glial, and other types of cells. Isoform 1 induces differentiation of mammary tumor cells, including altered morphology and synthesis of milk components. NRG1 is necessary for cardiac development, structural maintenance, and functional integrity of the heart. It is also thought to play a role in synaptic plasticity. Dysregulation of NRG1 has been linked to various cancers and schizophrenia.

Neuritin (NRN1) is a GPI-anchored neurotrophic factor, which is expressed in response to induction of neuronal activity by GDNF, BDNF, NT3 and other neural stimulators. It promotes neurite outgrowth and especially branching of neuritic processes in primary hippocampal and cortical cells. NRN1 also promotes angiogenesis. During early brain development, NRN1 inhibits apoptosis of cortical progenitors by preventing activation of caspase 3. Recombinant human neuritin is a covalently disulfide-linked homodimer, consisting of two 9.7 kDa polypeptide monomers, each containing 88 amino acid residues.

Neurotrophin 4 (NTF4), also known as NT5, is a member of the NGF family of neuronal and epithelial growth factors. Neurotrophins have six conserved cysteine residues that are involved in the formation of three disulfide bonds. Human NT4 shares 48 - 52% amino acid sequence identity with human β-NGF, BDNF and NT3. It shares 91% and 95% amino acid sequence identity with mouse and rat NT4/5, respectively. The protein is secreted as a homodimer and can also form heterodimers with BDNF or NT3. NT4 binds and induces receptor dimerization and activation of TrkB and promotes the development and survival of selected peripheral and CNS neurons. NT4 induced TrkB signaling augments NMDA receptor activity and increases neuronal sensitivity to excitotoxic cell death. NT4 is secreted by activated T cells and granulocytes and contributes to tissue regeneration at inflammation sites.