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Structure and function of basement membrane proteoglycans.

M Paulsson, S Fujiwara, M Dziadek

    Ciba Foundation Symposium
    |January 1, 1986
    PubMed
    Summary
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    Basement membranes contain distinct proteoglycans, including large and small heparan sulfate proteoglycans. These molecules exhibit unique structures and varying affinities for antithrombin, suggesting specialized roles.

    Area of Science:

    • Biochemistry
    • Cell Biology
    • Extracellular Matrix Research

    Background:

    • Basement membranes are crucial extracellular matrix structures.
    • They contain diverse proteoglycans, including heparan sulfate proteoglycans (HSPGs) and chondroitin sulfate proteoglycans.
    • Understanding proteoglycan structure and function is key to comprehending basement membrane biology.

    Purpose of the Study:

    • To characterize the distinct proteoglycans within basement membranes.
    • To elucidate the structural organization of large and small HSPGs.
    • To investigate the antithrombin-binding properties of heparan sulfate chains.

    Main Methods:

    • Purification of heparan sulfate proteoglycans from mouse EHS tumor.
    • Structural analysis using electron microscopy and analytical ultracentrifugation.

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  • Isolation and characterization of heparan sulfate chains from EHS tumor and Reichert's membrane.

    • Main Results:

    • Identified three distinct basement membrane proteoglycans: one large and two smaller types.
    • Determined structural models for large (core protein with 3 long chains) and small (core protein with 4 short chains) HSPGs.
    • Heparan sulfate from Reichert's membrane binds antithrombin with high affinity, containing a unique 3-O-sulfated glucosamine residue.

    Conclusions:

    • Basement membrane proteoglycans represent a distinct family.
    • Structural variations in HSPGs suggest specialized functions.
    • The presence of specific sulfation patterns in heparan sulfate influences biological interactions, such as antithrombin binding.