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Sulphated glycoproteins in synaptosomes

C J Branford White

    Neuroscience Letters
    |March 1, 1980
    PubMed
    Summary

    Isolated nerve terminals (synaptosomes) from sheep brains can perform sulfation on glycoproteins. This process involves the incorporation of sulfate into proteins within these nerve terminals, as evidenced by the identification of numerous sulfated proteins.

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    Area of Science:

    • Neurochemistry
    • Molecular Neuroscience
    • Protein Biochemistry

    Background:

    • Synaptosomes are isolated nerve terminals crucial for studying neuronal function.
    • Post-translational modifications, such as sulfation, play vital roles in protein function and localization.
    • Understanding modifications within synaptosomes can elucidate synaptic processes.

    Purpose of the Study:

    • To investigate the potential for sulfation of proteins within isolated nerve terminals (synaptosomes).
    • To identify and characterize sulfated proteins in the synaptosomal fraction.
    • To determine if glycoproteins undergo sulfation in isolated nerve terminals.

    Main Methods:

    • Incubation of sheep brain synaptosomes with sodium sulfate (Na2(35)SO4) to label sulfated proteins.
    • Protein extraction and separation from both soluble and particulate synaptosomal fractions using SDS/urea.
    • Analysis of labeled proteins by molecular weight and isolation of a glycopeptide for further characterization.

    Main Results:

    • Identification of at least twelve 35S-labeled proteins in the soluble synaptosomal fraction (13,000–150,000 MW).
    • Detection of an additional eight 35S-labeled proteins in the particulate fraction (27,000–140,000 MW).
    • Isolation of a glycopeptide containing fucose, sialic acid, N-acetylglucosamine, and galactose, with over 50% of its hexosamine and neutral sugar residues labeled with 35S.

    Conclusions:

    • The results strongly suggest that sulfation of glycoproteins occurs in isolated nerve terminals.
    • This study provides evidence for the enzymatic machinery responsible for protein sulfation within synaptosomes.
    • The findings contribute to the understanding of molecular processes occurring at the synapse.

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