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Related Experiment Videos

Polyamines stimulate endogenous protein phosphorylation in thyroid cytosol.

S Levasseur, T Poleck, G Burke

    Biochemical and Biophysical Research Communications
    |November 27, 1985
    PubMed
    Summary

    Spermine significantly enhances protein phosphorylation in rat thyroid cytosol, particularly a 107 kDa protein. This polyamine

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Endocrinology

    Background:

    • Polyamines are crucial for cellular processes.
    • Thyroid function involves protein phosphorylation.

    Purpose of the Study:

    • To investigate the effect of spermine on protein phosphorylation in rat thyroid cytosol.
    • To identify specific proteins affected by spermine.

    Main Methods:

    • Rat thyroid cytosol was incubated with spermine.
    • Protein phosphorylation was analyzed using SDS-PAGE and autoradiography.
    • Effects of different polyamines and heparin were assessed.

    Main Results:

    • Spermine increased 107 kDa protein phosphorylation 4-fold.
    • Spermine showed biphasic effects on 88 and 65 kDa protein phosphorylation.
    • Heparin inhibited spermine-stimulated phosphorylation.
    • Spermine also affected 107 kDa protein phosphorylation in mouse and beef thyroid.

    Conclusions:

    • Spermine is a potent stimulator of protein phosphorylation in thyroid cytosol.
    • The 107 kDa protein is a primary target of spermine in thyroid tissue.
    • Spermine's effects are specific and conserved across species.

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