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Structure-function studies of a colony stimulating factor (CSF-1)

S K Das, E R Stanley

    The Journal of Biological Chemistry
    |November 25, 1982
    PubMed
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    Colony-stimulating factor 1 (CSF-1) is a glycoprotein essential for mononuclear phagocyte development. This study reveals CSF-1

    Area of Science:

    • Biochemistry
    • Cell Biology
    • Immunology

    Background:

    • Colony-stimulating factor 1 (CSF-1) is a crucial glycoprotein growth factor for mononuclear phagocyte lineage cells.
    • Understanding CSF-1's structure, particularly its glycosylation, is key to its function and biological activity.

    Purpose of the Study:

    • To investigate the glycosylation of purified CSF-1.
    • To determine the role of the carbohydrate moiety in CSF-1's biological and antibody-binding activities.

    Main Methods:

    • Radiolabeling and purification of murine and human CSF-1.
    • Molecular weight analysis using SDS-PAGE before and after reduction/alkylation.
    • Enzymatic deglycosylation using endo-beta-N-acetylglucosaminidase D and H, and endo-alpha-N-acetyl-D-galactosaminidase.

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  • Concanavalin A binding assays to assess glycosylation.

    • Main Results:

    • CSF-1 exists as a dimer with subunits of similar molecular weight, varying between 47,000-76,000 Da.
    • Enzymatic analysis indicated Asn-linked "complex-type" carbohydrate units.
    • Deglycosylation did not affect antibody binding, receptor binding, or biological activity, suggesting carbohydrate is not essential for these functions.

    Conclusions:

    • CSF-1 is an Asn-linked glycoprotein with complex-type oligosaccharides.
    • The carbohydrate moiety of CSF-1 is not essential for its biological activity, antibody binding, or receptor binding.