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Native heparin from rat peritoneal mast cells

R W Yurt, R W Leid, K F Austen

    The Journal of Biological Chemistry
    |January 25, 1977
    PubMed
    Summary
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    Mast cells produce unique heparin proteoglycans resistant to protein breakdown. This native heparin exhibits low anticoagulant activity and may be structurally distinct from other heparin forms.

    Area of Science:

    • Biochemistry
    • Cell Biology

    Background:

    • Mast cells are known to store heparin.
    • The biochemical nature and structure of mast cell heparin remain incompletely understood.

    Purpose of the Study:

    • To characterize the native heparin produced by rat peritoneal mast cells.
    • To investigate the potential proteoglycan nature and enzymatic resistance of mast cell heparin.

    Main Methods:

    • In vitro and in vivo radiolabeling of heparin using [35S]sulfate.
    • Isolation of native heparin using mild purification techniques.
    • Analysis of heparin size and composition using gel filtration and radiolabeling ([3H]serine).
    • Enzymatic and alkaline degradation studies.

    Main Results:

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    • Mast cell heparin was synthesized and isolated with low anticoagulant activity.
    • Heparin size varied with incubation time, ranging from Mr=200,000-400,000 to Mr=750,000.
    • [3H]serine co-chromatographed with [35S]heparin, suggesting a proteoglycan structure.
    • Heparin was resistant to proteolytic enzymes but degraded by alkali, with a portion of the serine label remaining associated.

    Conclusions:

    • Native mast cell heparin is likely an unusual proteoglycan.
    • This heparin exhibits significant resistance to proteolytic degradation.
    • Its unique structure may contribute to its low anticoagulant activity.