Effect of tunicamycin on the glycosylation of rhodopsin.

@article{Plantner1980EffectOT,
  title={Effect of tunicamycin on the glycosylation of rhodopsin.},
  author={James J. Plantner and Louis Poncz and Edward L. Kean},
  journal={Archives of biochemistry and biophysics},
  year={1980},
  volume={201 2},
  pages={
          527-32
        }
}
Abstract The incorporation of [3H]glucosamine, [3H]mannose, and [35S]methionine into rhodopsin was investigated in retinas which had been incubated in the presence and absence of the antibiotic, tunicamycin. In its presence, the incorporation of glucosamine was inhibited 70% and mannose, 96% compared to controls. In the presence of tunicamycin the attachment of glucosamine to core-region sites was virtually eliminated. The formation of unglycosylated rhodopsin was also indicated by sodium… Expand
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In vitro galactosylation of rhodopsin and opsin: kinetics, properties and characterization.
TLDR
Characteristics of the galactosyltransferases of the retina are examined in the hope of shedding light on the capacity ofThe retina to carry out this reaction. Expand
The dolichol pathway in the retina: oligosaccharide-lipid biosynthesis.
TLDR
The formation of the oligosaccharide-lipid intermediates of the dolichol pathway by the bovine retina was investigated and experiments carried out in the presence of castanospermine and bromoconduritol indicated that alpha- glucosidase activity in the retina may have resulted in the accumulation of the unglucosylated oligo-lipids. Expand
Effects of glycosylation inhibitors on the frog retina
TLDR
The possibility that specific oligosaccharide processing reactions may not be required for the insertion of rhodopsin and subsequent assembly of disc membranes in frog photoreceptors is suggested. Expand
Effect of enzymatic deglycosylation on the regenerability of bovine rhodopsin.
TLDR
After photobleaching, deglycosylated rhodopsin reacted with 11-cis retinaldehyde in a manner similar to the native material, restoring the spectral properties lost after light-exposure. Expand
Influence of metal ions on the biosynthesis of N-acetylglucosaminyl polyprenols by the retina.
  • E. L. Kean
  • Chemistry, Medicine
  • Biochimica et biophysica acta
  • 1983
TLDR
The influence of metal ions, in addition to the stimulation by dolichol phosphate mannose, on GlcNAc-lipid synthesis may be aspects of metabolic regulation of the dolICHol pathway. Expand
Tunicamycin does not inhibit transport of phosphatidylinositol toXenopus rod outer segments
TLDR
Results indicate that despite the morphological disruption and inhibition of glycoprotein transport to outer segments after tunicamycin treatment, transport of labelled phosphatidylinositol occurs normally, adding to a growing body of evidence separating the lipid and protein transport pathways to the outer segment. Expand
The incorporation of 3H-fucose and 3H-mannose into the photopigment of the crayfish Procambarus clarkii
TLDR
Determination of the distribution of radioactivity in the gels indicated that both fucose and mannose labeled the photopigment and other glycoproteins, which provides the first reported data on the partial composition of the carbohydrate moiety of an invertebrate photopIGment. Expand
Photoreceptor-specific degeneration caused by tunicamycin
TLDR
It is reported that intraocular injection of tunicamycin produces a photoreceptor-specific degeneration characterized by progressive shortening of rod outer segment, decreased electroretinogram amplitudes, cessation of rods outer segment membrane assembly, and eventual photorecept cell death. Expand
Glycoprotein synthesis in the human retina: localization of the lipid intermediate pathway.
TLDR
The results suggest that the lipid intermediate pathway of glycoprotein synthesis is localized preferentially to the photoreceptor layer of the retina, and may subserve the biosynthesis of rod cell glycoproteins (e.g. opsin). Expand
The enzymatic cleavage of rhodopsin by the retinal pigment epithelium. I. Enzyme preparation, properties and kinetics: characterization of the glycopeptide product.
TLDR
An enzyme system has been detected in the bovine retinal pigmented epithelium (RPE) which carries out the degradation of rhodopsin and may be one of the means whereby the RPE participates in maintaining the physiological concentration of r Rhodopsin which is synthesized in the retina and catabolized inThe RPE. Expand
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