Glycoprotein biosynthesis in the developing rat brain. 3. Are glycoprotein glycosyl transferases present in synaptosomes?

@article{Raghupathy1972GlycoproteinBI,
  title={Glycoprotein biosynthesis in the developing rat brain. 3. Are glycoprotein glycosyl transferases present in synaptosomes?},
  author={E. Raghupathy and Gyi. Ko Ko and Neal A. Peterson},
  journal={Biochimica et biophysica acta},
  year={1972},
  volume={286 2},
  pages={
          339-49
        }
}

Rat brain glycosyltransferase activities during postnatal development

Glycoprotein galactosyltransferase activity in synaptic junctional complexes isolated from rat forebrain

A synaptosomal plasma membrane fraction and its junctional and nonjunctional subfractions were isolated and analyzed for glycoprotein galactosyltransferase activity, suggesting an enrichment of enzyme in this fraction.

Distribution and metabolism of glycoproteins and glycosaminoglycans in subcellular fractions of brain.

Data indicate that sialic acid may be added locally to synaptosomal soluble glycoproteins before there is significant labeling of nerve ending glycopriteins by axoplasmic transport, as indicated by the 80-155% higher specific activity of hexosamine and siali acid 1 day after labeling with [3H]glucosamine in vivo.

Biosynthesis of Glycoproteins

Since membrane glycoproteins have been implicated in many neurobiological processes and functions (see Chapters 7, 8, and 11), the mechanisms and regulation of biosynthesis of the oligosaccharide

SIALYLTRANSFERASES IN RAT BRAIN: INTRACELLULAR LOCALIZATION AND SOME MEMBRANE PROPERTIES

  • S. NgJ. Dain
  • Biology, Chemistry
    Journal of neurochemistry
  • 1977
Abstract— Total rat cerebral homogenate, with nuclei removed, yielded sialyltransferase activity peaks that were distinct from the protein distribution profile in a continuous sucrose density

The biosynthesis of brain gangliosides--evidence for a "transient pool" and an "end product pool" of gangliosides.

The pathway of synthesis found for GTlb (Arce et al, 1971) was recently confirmed by using exogenous acceptors (Mestrallet et al., 1974) and the pathway of completion of GDlb was also confirmed.

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Properties of some glycosyltransferases in embryonic chicken brain.

Isolation of plasma membranes from rat brain.

PARTICULATE AND SOLUBILIZED FUCOSYL TRANSFERASES FROM MOUSE BRAIN

  • M. ZatzS. H. Barondes
  • Biology, Chemistry
    Journal of neurochemistry
  • 1971
The transferase of brain was more active than the transferases from all other organs tested, with the exception of kidney, and activity was limited to fractions containing microsomal membranes, whereas synaptosomal and other fractions were virtually inactive.

SYNTHESIS OF GLYCOPROTEINS IN BRAIN: IDENTIFICATION, PURIFICATION AND PROPERTIES OF GLYCOSYL TRANSFERASES FROM PURIFIED SYNAPTOSOMES OF GUINEA PIG CEREBRAL CORTEX

  • H. Bosmann
  • Biology, Chemistry
    Journal of neurochemistry
  • 1972
Four glycoprotein:glycosyl transferases were purified 34‐, 45‐, 37‐ and 47‐fold, respectively, from synaptosomes prepared from guinea pig cerebral cortex by centrifugation and column chromatography, and were highly specific for specific macromolecular acceptors.

DISTRIBUTION OF POLYSOMES IN MOUSE BRAIN TISSUE

Sucrose gradient analysis of the material in the post‐mitochondrial supernatant fraction indicated that 80 per cent of the ribosomes were present in polysomes and that little, if any, of the pellet fraction was present.

SYNAPTOSOMAL PROTEIN SYNTHESIS IN A CELL‐FREE SYSTEM *

The protein‐synthesizing system was not stimulated by the addition of either ATP or an ATP‐generating system, and ATP at all concentrations was inhibitory.

PROTEIN SYNTHESIS IN SYNAPTOSOMAL FRACTIONS : Ultrastructural Radioautographic Study

The findings indicate that protein synthesis takes place in vitro in presynaptic terminals although to a significantly lesser degree than that occurring in ribosome-containing processes, which are at the present time unavoidable contaminants of synaptosomal fractions.