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Related Experiment Videos

The charge polymorphism of rat apoprotein E.

C A Reardon, D M Driscoll, R A Davis

    The Journal of Biological Chemistry
    |April 5, 1986
    PubMed
    Summary
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    Rat apolipoprotein E (apo-E) polymorphism arises from post-translational modifications in the endoplasmic reticulum and Golgi. Sialic acid residues contribute to apo-E isoform diversity, with apo-E-1 not being an N-linked glycoprotein.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Cell Biology

    Background:

    • Apolipoprotein E (apo-E) exhibits genetic polymorphism with four isoelectric forms (E-1 to E-4) in rat plasma.
    • Understanding the biogenesis of these apo-E isoforms is crucial for elucidating their functional roles.

    Purpose of the Study:

    • To investigate the post-translational modifications and cellular processes responsible for rat apolipoprotein E (apo-E) isoform generation.
    • To determine the contribution of sialic acid and glycosylation to apo-E polymorphism.

    Main Methods:

    • Analysis of intrahepatic apo-E precursors in intact rats and cultured rat hepatocytes using isoelectric focusing and molecular weight determination.
    • Radiolabeling studies ([3H]leucine and [3H]glucosamine) to track apo-E synthesis and modification.

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  • Treatment with tunicamycin to assess the role of N-linked glycosylation.

    • Main Results:

    • The primary translation product of apo-E mRNA yielded two basic isoproteins, distinct from plasma forms.
    • Microsomal processing generated isoproteins corresponding to plasma apo-E-4 and apo-E-3.
    • Intrahepatic apo-E isoforms E-2 and E-1 were sequentially detected in the rough endoplasmic reticulum (RER) and Golgi, with increasing molecular weight.
    • Only apo-E-1 was sensitive to neuraminidase, indicating partial contribution of sialic acid to polymorphism.
    • Tunicamycin did not affect apo-E synthesis, glycosylation, or secretion, confirming apo-E-1 is not N-linked glycosylated.

    Conclusions:

    • Post-translational modifications within the RER and Golgi are key contributors to rat apo-E polymorphism.
    • Sialic acid residues play a role in creating the observed apo-E isoform diversity.
    • Apo-E-1 isoform is not an N-linked glycoprotein, distinguishing it from other potential modifications.