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Prenylated proteins from kidney.

E Bruenger, H C Rilling

    Biochemical and Biophysical Research Communications
    |August 29, 1986
    PubMed
    Summary

    Radioactive mevalonate is incorporated into kidney proteins in mice, forming an allylic ether linkage. This mevalonate derivative is similar to dolichol C95, suggesting a novel protein modification.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Renal Physiology

    Background:

    • Mevalonate is a key precursor in isoprenoid biosynthesis.
    • Isoprenoids play crucial roles in protein modification and cellular signaling.
    • The kidney's role in macromolecule metabolism is not fully understood.

    Purpose of the Study:

    • To investigate the incorporation and nature of mevalonate derivatives in kidney macromolecules.
    • To identify the chemical linkage and molecular characteristics of the incorporated mevalonate.

    Main Methods:

    • Injection of [5-3H]mevalonate into mice.
    • Biochemical assays including RNase/DNase and protease treatments.
    • Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE).
    • Acid/base hydrolysis and organic solvent extraction.
    • Chromatographic analysis.

    Main Results:

    • Mevalonate was incorporated into kidney macromolecules, resistant to nucleic acid degradation but sensitive to protease.
    • SDS-PAGE indicated a molecular weight of approximately 25,000 for the modified protein.
    • Hydrolysis and protease treatment released the mevalonate derivative, suggesting an allylic ether linkage to the protein.
    • Chromatographic properties matched dolichol C95.

    Conclusions:

    • Mevalonate is covalently attached to kidney proteins via an allylic ether bond.
    • The modified protein has a molecular weight of ~25 kDa.
    • The mevalonate derivative is structurally similar to dolichol C95, indicating a potential role in protein prenylation or related pathways within the kidney.

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