Disease relevance of Nyx

• Nyx expression was found during all stages of postnatal retinal development and was confined to cells of the inner nuclear layer and the ganglion cell layer in adult mouse and rat retinas [1].
• PURPOSE: The available evidence indicates that the naturally occurring mouse mutant nob (no b-wave) provides an animal model for the complete form of human X-linked congenital stationary night blindness (CSNB1) [2].

High impact information on Nyx

• Transgenic rescue of the mutated protein (nyctalopin) within nob retinal interneurons, without rescuing expression in either retinal projection neurons or their postsynaptic targets in the dLGN, restores spontaneous retinal activity patterns and prevents desegregation [3].
• Failure to Maintain Eye-Specific Segregation in nob, a Mutant with Abnormally Patterned Retinal Activity [3].
• METHODS: Nyx was isolated by conventional DNA library screening and polymerase chain reaction (PCR)-based approaches [1].
• Deletion of the ER signal sequence in Nyx delocalized the intracellular V5-Nyx protein and caused its dispersion in the cytosol [4].
• This model will be useful in defining the role of nyctalopin in signal transmission between photoreceptors and retinal bipolar cells [2].

Biological context of Nyx

• Identification of the gene and the mutation responsible for the mouse nob phenotype [2].
• The inheritance pattern for nob was defined by breeding nob animals with normal mice [5].
• NYX (nyctalopin on chromosome X), the gene mutated in congenital stationary night blindness, encodes a cell surface protein [4].
• Our findings support a role for nyctalopin in synaptic transmission and/or synapse formation at ribbon synapses in the retina [6].
• Localization of the mouse nob (no b-wave) gene to the centromeric region of the X chromosome [7].

Anatomical context of Nyx

• PURPOSE: To describe a naturally occurring X-linked recessive mutation, no b-wave (nob), that compromises visual transmission between photoreceptors and second-order neurons in mice [5].

Associations of Nyx with chemical compounds

• The nyctalopin protein contains 11 leucine-rich repeats and is flanked by cysteine rich regions, which identifies it as a member of the small leucine rich proteoglycan family [2].

Other interactions of Nyx

• The amplitude of slow PIII, revealed by the nob genetic background, was reduced in Kir4.1+/- mice [8].
• The nob mutation does not protect against light-induced retinal degeneration [9].

Analytical, diagnostic and therapeutic context of Nyx

• Subsequently, the expression pattern of Nyx and its gene product in mouse and rat retinas was investigated by RNA in situ hybridization and immunohistochemistry with Nyx-specific antibodies [1].

References