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Human plasma actin-depolymerizing factor. Purification, biological activity and localization in leukocytes and

C Chaponnier, P Patebex, G Gabbiani

    European Journal of Biochemistry
    |January 15, 1985
    PubMed
    Summary
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    Human actin-depolymerizing factor (ADF) is a 90 kDa protein that depolymerizes actin filaments. This purified protein, ADF, may play a role in actin organization and solubilization in cells and plasma.

    Area of Science:

    • Biochemistry
    • Cell Biology
    • Molecular Biology

    Background:

    • Plasma and serum from humans and animals exhibit actin-depolymerizing activity.
    • Actin is a crucial protein involved in cellular structure and function.

    Purpose of the Study:

    • To purify and characterize the human actin-depolymerizing factor (ADF).
    • To investigate the mechanism and biological role of human ADF.

    Main Methods:

    • Ammonium sulfate fractionation, DEAE-cellulose, and blue-Sepharose chromatography for protein purification.
    • Electron microscopy, differential ultracentrifugation, and DNase I inhibition assay to study actin filament depolymerization.
    • Immunofluorescence and immunoblotting to detect ADF in human cells.

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    Main Results:

    • Human ADF was purified as a 90 kDa heat and trypsin-sensitive polypeptide.
    • ADF was shown to fragment and depolymerize actin filaments, leading to actin extraction.
    • A 90 kDa protein reacting with ADF antibody was found in human white blood cells and platelets, primarily in the soluble cytoplasmic fraction.

    Conclusions:

    • Human ADF is a potent actin-depolymerizing agent.
    • ADF may be involved in the solubilization of plasma actin and intracellular actin organization.
    • ADF could be a valuable tool for assessing cytoplasmic actin filament stability in various conditions.