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Macrophage component gp160, a major trypsin-sensitive surface glycoprotein

E Remold-O'Donnell

    The Journal of Experimental Medicine
    |December 1, 1980
    PubMed
    Summary

    Macrophages have surface proteases, and mild trypsin treatment cleaves a 160,000 mol wt glycoprotein (gp160). This glycoprotein is exposed on the cell surface, with its carbohydrate moiety on an 85,000 mol wt fragment.

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    Area of Science:

    • Cell Biology
    • Proteomics
    • Immunology

    Background:

    • Macrophages secrete proteases, indicating cell surface exposure to proteolytic conditions.
    • Cell surface glycoproteins play crucial roles in cellular functions and interactions.

    Purpose of the Study:

    • To identify and characterize the primary surface protein cleaved by mild trypsin treatment on macrophages.
    • To investigate the structure and surface accessibility of the cleaved glycoprotein.

    Main Methods:

    • Iodination (125I) and carbohydrate labeling (3H) of guinea pig peritoneal macrophages.
    • Mild trypsin digestion and subsequent protein purification using lectin affinity and ion-exchange chromatography.
    • Non-reducing and reducing SDS-polyacrylamide gel electrophoresis (SDS-PAGE) to analyze protein fragments and molecular weights.

    Main Results:

    • Mild trypsin treatment preferentially cleaved a single surface glycoprotein (gp160) of 160,000 mol wt.
    • gp160 remained assembled as a multichain disulfide-bonded molecule in the membrane after trypsinization.
    • Reducing SDS-PAGE of purified gp160 yielded two fragments (85,000 and 71,000 mol wt), both accessible to the cell surface.
    • The 85,000 mol wt fragment contained the carbohydrate label, indicating its surface exposure.

    Conclusions:

    • Macrophages possess a major surface glycoprotein (gp160) susceptible to mild trypsin cleavage.
    • gp160 is exposed on the cell surface, with its carbohydrate moiety located on the larger fragment.
    • This study provides insights into macrophage surface protein structure and proteolytic susceptibility.

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