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Biosynthesis and processing of proteodermatan sulphate.

H Kresse, J Glössl, W Hoppe

    Ciba Foundation Symposium
    |January 1, 1986
    PubMed
    Summary
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    The study reveals proteodermatan sulphate (PDS) biosynthesis occurs in pre-Golgi compartments, with phosphorylation in the endoplasmic reticulum. PDS secretion and core protein structure are independent of glycosylation, but glycosaminoglycan chain composition varies between cell types.

    Area of Science:

    • Biochemistry
    • Cell Biology
    • Glycobiology

    Background:

    • Proteodermatan sulphate (PDS) is a key component of the extracellular matrix.
    • Understanding PDS biosynthesis and processing is crucial for comprehending its biological roles.

    Purpose of the Study:

    • To investigate the biosynthesis and processing of proteodermatan sulphate (PDS) in human skin fibroblasts and arterial smooth muscle cells (SMC).
    • To elucidate the intracellular compartments involved in PDS synthesis and modification.
    • To determine the role of glycosylation and intracellular transport in PDS secretion and structure.

    Main Methods:

    • Utilized core-directed antibodies and inhibitors of protein synthesis, intracellular transport, and glycosylation.
    • Investigated phosphorylation sites and sulphation patterns.

    Related Experiment Videos

  • Analyzed PDS composition, core protein structure, and peptide maps.

    • Main Results:

    • Linkage region attachment to the core protein occurs in a pre-Golgi compartment.
    • Phosphorylation of PDS precursors primarily happens in the endoplasmic reticulum.
    • Monensin blockade affects uronic acid epimerization and 4-sulphation, but not 6-sulphation.
    • PDS secretion and core protein structure are independent of N-linked oligosaccharides or glycosaminoglycan chains.
    • Significant differences in glycosaminoglycan chain composition were observed between fibroblast and SMC-derived PDS.
    • Core protein structure, analyzed by isoelectric focusing and limited proteolysis, showed no significant differences between cell types.

    Conclusions:

    • PDS biosynthesis involves early intracellular compartments and specific phosphorylation events.
    • Glycosaminoglycan chain composition is cell-type specific, while the core protein structure is conserved.
    • These findings provide insights into the complex regulation of PDS synthesis and its structural basis.