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Multiple fibronectin subunits and their post-translational modifications.

J I Paul, R O Hynes

    The Journal of Biological Chemistry
    |November 10, 1984
    PubMed
    Summary
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    Fibronectin subunit heterogeneity arises from both primary sequence differences and post-translational modifications like glycosylation and tyrosine sulfation. These modifications create distinct subunits in plasma and cellular fibronectin, varying between species.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Proteomics

    Background:

    • Fibronectin is a crucial extracellular matrix protein involved in cell adhesion and migration.
    • Fibronectin exists in plasma and cellular forms, with known heterogeneity in its subunits.
    • Understanding fibronectin subunit diversity is key to elucidating its diverse biological functions.

    Purpose of the Study:

    • To analyze the subunit diversity of plasma and cellular fibronectins using high-resolution electrophoresis.
    • To investigate the roles of differential glycosylation and other post-translational modifications in fibronectin heterogeneity.
    • To compare fibronectin subunit patterns between plasma and cellular forms and across species.

    Main Methods:

    • High-resolution one- and two-dimensional gel electrophoresis were employed.

    Related Experiment Videos

  • Plasma and cellular fibronectins from rats and hamsters were analyzed.
  • Differential glycosylation, phosphorylation, and sulfation patterns were examined.

    • Main Results:

    • Fibronectin subunits exhibit significant heterogeneity, with distinct patterns for plasma and cellular forms within and between species.
    • Differential glycosylation accounts for some, but not all, subunit heterogeneity; nonglycosylated forms share common subunits.
    • Tyrosine sulfation occurs on specific subunits, potentially linked to alternative mRNA splicing and located in the C-terminal region.

    Conclusions:

    • Fibronectin subunit heterogeneity is a complex interplay of primary sequence variations and post-translational modifications.
    • Glycosylation and tyrosine sulfation contribute significantly to the distinct profiles of plasma and cellular fibronectins.
    • The findings provide insights into the molecular basis of fibronectin diversity and its functional implications.