Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.5.1.52 (PNGase F)
 1,527 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The dopamine transporter from rat caudate-putamen was photolabeled with [125I]DEEP as previously described. Treatment of photolabeled membranes with neuraminidase and N-glycanase reduced the molecular weight of the [125I]DEEP photolabeled dopamine transporter complex, whereas treatment with alpha-mannosidase had no effect. The solubilized [125I]DEEP photolabeled dopamine transporter complex readily bound to wheat-germ agglutinin but not to concanavalin-A sepharose columns. These results suggest that the carbohydrate moiety of the dopamine transporter is N-linked and contains significant quantities of sialic acid but not high mannose residues. A DEEP binding protein was readily detectable in other brain regions including the nucleus accumbens and olfactory tubercle, but not in the prefrontal cortex, olfactory bulb or hypothalamus under similar conditions. The DEEP binding protein in the other brain regions was similar to that in the striatum.
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PMID:Dopamine transporter: deglycosylation with exo- and endoglycosidases. 205

Using affinity chromatography with the monoclonal antibody 271A6, which binds selectively to telencephalic regions of the rabbit brain, we have purified a telencephalon-specific antigen to apparent homogeneity and characterized it as a membrane glycoprotein. The telencephalon-specific membrane protein (named "telencephalin") has a molecular weight of about 500,000 and is composed of four subunits each of mol. wt 130,000. Its digestion with N-glycanase reduced the subunit mol. wt by 23,000, indicating that each subunit has several N-asparagine-linked oligosaccharide chains. Immunohistochemical analysis using polyclonal antibody against the purified telencephalin shows that expression of the entire protein is restricted to the telencephalon. In addition, segment-specific expression of telencephalin was observed in all mammalian species examined (mouse, rat, guinea-pig, rabbit, cat and monkey). The telencephalon is the most rostral segment of the brain, and comprises the cerebral neocortex, paleocortex, hippocampus, septum, striatum and olfactory bulb. The present results indicate that all regions of the mammalian telencephalon express the segment-specific membrane glycoprotein, telencephalin, and suggest that telecephalin is involved in functions specific to the surface membrane of telencephalic neurons.
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PMID:Mammalian telencephalic neurons express a segment-specific membrane glycoprotein, telencephalin. 235 99

The bovine herpesvirus 5 (BHV-5) gE ectodomain contains a glycine-rich epitope coding region (gE5 epitope), residues 204 to 218, that is significantly different from the corresponding gE region of BHV-1. Deletion of the gE epitope significantly reduced the neurovirulence of BHV-5 in rabbits. Pulse-chase analyses revealed that the epitope-deleted and wild-type gE were synthesized as N-glycosylated endoglycosidase H-sensitive precursors with approximate molecular masses of 85 kDa and 86 kDa, respectively. Like the wild-type gE, epitope-deleted gE complexed with gI and was readily transported from the endoplasmic reticulum. Concomitantly, the epitope-deleted and wild-type gE acquired posttranslational modifications in the Golgi leading to an increased apparent molecular mass of 93-kDa (epitope-deleted gE) and 94-kDa (wild-type gE). The kinetics of mutant and wild-type gE processing were similar, and both mature proteins were resistant to endoglycosidase H but sensitive to glycopeptidase F. The gE epitope-deleted BHV-5 formed wild-type-sized plaques in MDBK cells, and the epitope-deleted gE was expressed on the cell surface. However, rabbits infected intranasally with gE epitope-deleted BHV-5 did not develop seizures, and only 20% of the infected rabbits showed mild neurological signs. The epitope-deleted virus replicated efficiently in the olfactory epithelium. However, within the brains of these rabbits there was a 10- to 20-fold reduction in infected neurons compared with the number of infected neurons within the brains of rabbits infected with the gE5 epitope-reverted and wild-type BHV-5. In comparison, 70 to 80% of the rabbits exhibited severe neurological signs when infected with the gE5 epitope-reverted and wild-type BHV-5. These results indicated that anterograde transport of the gE epitope-deleted virus from the olfactory receptor neurons to the olfactory bulb is defective and that, within the central nervous system, the gE5 epitope-coding region was required for expression of the full virulence potential of BHV-5.
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PMID:A glycine-rich bovine herpesvirus 5 (BHV-5) gE-specific epitope within the ectodomain is important for BHV-5 neurovirulence. 1507 62