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Shiverer and normal peripheral myelin compared: basic protein localization, membrane interactions, and lipid

H Inouye, A L Ganser, D A Kirschner

    Journal of Neurochemistry
    |December 1, 1985
    PubMed
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    Shiverer myelin, lacking myelin basic protein, shows altered extracellular interactions due to lipid changes. P0 glycoprotein, not basic protein, stabilizes cytoplasmic membrane surfaces in peripheral myelin.

    Area of Science:

    • Neuroscience
    • Biochemistry
    • Cell Biology

    Background:

    • Myelin basic protein (MBP) is crucial for myelin structure and compaction.
    • The shiverer mutant mouse lacks MBP, providing a model to study its role.
    • Understanding myelin membrane interactions is key to nervous system function.

    Purpose of the Study:

    • To correlate shiverer sciatic nerve myelin structure and interactions with its biochemical composition.
    • To investigate the role of myelin basic protein and lipids in membrane apposition and swelling.
    • To identify the molecular basis for the stability of cytoplasmic membrane surfaces.

    Main Methods:

    • X-ray diffraction analysis of swollen shiverer and normal sciatic nerve myelin.
    • Biochemical analysis of myelin lipid composition.

    Related Experiment Videos

  • Comparative studies of membrane swelling under varying ionic strength and pH conditions.

    • Main Results:

    • Shiverer myelin exhibits an electron density deficit in the cytoplasmic half, correlating with the absence of MBP.
    • Shiverer myelin shows increased swelling in the extracellular space compared to normal myelin.
    • Lipid composition differences in shiverer myelin include higher sulfatides and lower sphingomyelin.
    • Cytoplasmic membrane surfaces remain apposed in shiverer myelin, independent of MBP.

    Conclusions:

    • MBP localizes to the cytoplasmic apposition in normal myelin, but its absence does not disrupt cytoplasmic membrane stability.
    • Altered lipid composition, particularly increased sulfatides, contributes to increased extracellular swelling in shiverer myelin.
    • P0 glycoprotein is proposed as the primary mediator of stable interactions at the cytoplasmic surfaces of peripheral myelin membranes.