Pro-Neuropeptide Y (NPY) is a member of the NPY family. NPY is a secreted protein and is one of the most abundant peptides in the nervous system. It also can be found in some chromaffin cells of the adrenal medulla. NPY can be cleaved into Neuropeptide Y and C-flanking peptide of NPY chain, which regulates energy usage, and it is involved in learning, memory processing, and epilepsy. NPY is implicated in the control of feeding and in secretion of gonadotrophin-release hormone. In addition, NPY increases the proportion of energy stored as fat and blocks nociceptive signals to the brain.
NPY (Neuropeptide Y) is a Protein Coding gene. This gene encodes a neuropeptide that is widely expressed in the central nervous system and influences many physiological processes, including cortical excitability, stress response, food intake, circadian rhythms, and cardiovascular function. NPY is a neuromodulator that is widely expressed throughout the central nervous system (CNS) and is consecrated with classic neurotransmitters including GABA and glutamate. NPY/Agouti-related protein (AgRP) neurons in the arcuate nucleus of the hypothalamus are part of a neuroendocrine feedback loop that regulates feeding behavior and glucose homeostasis. NPY/AgRP neurons sense peripheral signals (including the hormones leptin, insulin, and ghrelin) and integrate those signals with inputs from other brain regions.
NQO1 gene is a member of the NAD(P)H dehydrogenase (quinone) family and encodes a cytoplasmic 2-electron reductase. NQO1 forms homodimers and reduces quinones to hydroquinones. NQO1's enzymatic activity prevents the one electron reduction of quinones that results in the production of radical species. Mutations in NQO1 gene have been associated with tardive dyskinesia (TD), an increased risk of hematotoxicity after exposure to benzene, and susceptibility to various forms of cancer. Altered expression of NQO1 has been seen in many tumors and is also associated with Alzheimer's disease (AD). Alternate transcriptional splice variants, encoding different isoforms, have been characterized. Recent pharmacological research suggests feasibility of genotype-directed redox chemotherapeutic intervention targeting NQO1 breast cancer, a common missense genotype encoding a functionally impaired NQO1 protein.
NRAS was discovered by researchers at the Institute of Cancer Research, funded by the Cancer Research Campaign (now Cancer Research UK). NRAS gene is a member of the Ras gene family. It is mapped on chromosome 1, and it is activated in HL60, a promyelocytic leukemia line. The mammalian ras gene family consists of the harvey and kirsten ras genes (HRAS and KRAS), an inactive pseudogene of each (c-Hras2 and c-Kras1) and the N-ras gene. They differ significantly only in the C-terminal 40 amino acids. These ras genes have GTP/GDP binding and GTPase activity, and their normal function may be as G-like regulatory proteins involved in the normal control of cell growth. The NRAS gene specifies two main transcripts of 2Kb and 4.3Kb. The difference between the two transcripts is a simple extension through the termination site of the 2Kb transcript. The NRAS gene consists of seven exons (-I, I, II, III, IV, V, VI).
Neuronal cell adhesion molecule(NRCAM) is a single-pass type I membrane protein ,containing 5 fibronectin type-III domains and 6 Ig-like C2-type (immunoglobulin-like) domains.It belongs to the immunoglobulin superfamily. NrCAM is engaged in such biological processes as axonal fasciculation, cell-cell adhesion, central nervous system development, clustering of voltage-gated sodium channels, neuron migration, positive regulation of neuron differentiation, regulation of axon extension, and synaptogenesis. It also may play a role in the molecular assembly of the nodes of Ranvier. NrCAM effects are also linked with different recognition processes and signal transduction pathways regulating cell differentiation, proliferation, or migration.
Neuritin-like protein belongs to the neuritin family. Neuritin is a GPI-anchored protein that promotes neurite outgrowth and branching of neuritic processes in primary hippocampal and cortical cells. Neuritin expression also enhances the development of motor neuron axon arbors by promoting neuromuscular synaptogenesis and by stimulating the addition of new axon branches. Neuritin is induced by neuronal activity and by the neurotrophins, BDNF and NT3. NRN1L contains a consensus cleavage signal found in glycosylphoshatidylinositol (GPI)-anchored proteins.
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