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Vitamin D-binding protein (Gc-globulin) binds actin.

H Van Baelen, R Bouillon, P De Moor

    The Journal of Biological Chemistry
    |March 25, 1980
    PubMed
    Summary

    Serum vitamin D-binding protein (DBP) binds tightly with intracellular actin. This interaction, observed across species, influences actin

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    Molecular endocrinology (Baltimore, Md.)·1997

    Area of Science:

    • Biochemistry
    • Cell Biology
    • Molecular Interactions

    Background:

    • Actin is a highly conserved intracellular protein essential for cellular structure and function.
    • Serum vitamin D-binding protein (DBP) is known for its role in vitamin D transport.
    • A 5-6 S protein complex, involving DBP, is found in tissue supernatants and binds 25-hydroxycholecalciferol.

    Purpose of the Study:

    • To investigate the interaction between actin and serum vitamin D-binding protein (DBP).
    • To characterize the binding properties and potential biological significance of the actin-DBP complex.

    Main Methods:

    • In vitro complex formation assays between purified actin and DBP.
    • Observation of F-actin depolymerization upon incubation with DBP.
    • Assessment of DBP binding to actin complexed with deoxyribonuclease I.
    • Analysis of DBP binding to actin isolated from erythrocyte ghosts.

    Main Results:

    • Actin and DBP form stable 1:1 molar complexes in vitro, independent of species.
    • DBP binding to filamentous actin (F-actin) induces depolymerization of F-actin.
    • Actin retains its DBP-binding capacity even when complexed with deoxyribonuclease I.
    • Actin isolated from red blood cell membranes also binds DBP.

    Conclusions:

    • A novel, conserved interaction exists between intracellular actin and serum vitamin D-binding protein (DBP).
    • This interaction may explain the presence of the 5-6 S DBP-binding protein in cellular supernatants.
    • The biological implications of the actin-DBP interaction require further investigation.

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