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Related Experiment Videos

Electron microscopy of trypsin-digested peripheral nerve myelin.

R G Peterson

    Journal of Neurocytology
    |February 1, 1975
    PubMed
    Summary

    Trypsin digestion fragmented Schwann cell basement membranes and altered myelin structure in mouse sciatic nerves. This indicates trypsin-digestible proteins are present in peripheral nervous system myelin.

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    Area of Science:

    • Neuroscience
    • Biochemistry
    • Cell Biology

    Background:

    • Peripheral nervous system (PNS) myelin provides insulation for nerve axons.
    • Understanding the molecular composition of myelin is crucial for studying nerve health and disease.

    Purpose of the Study:

    • To investigate the effects of trypsin on the structural integrity of mouse sciatic nerve myelin.
    • To identify the presence of trypsin-digestible proteins within PNS myelin sheaths.

    Main Methods:

    • Mouse sciatic nerves were incubated with trypsin (Sigma Type III) in phosphate-buffered saline (PBS) at varying temperatures and durations.
    • Nerve tissues were prepared for electron microscopy using standard fixation and embedding techniques.
    • Ultrastructural changes in myelin and Schwann cell basement membranes were analyzed.

    Main Results:

    • Trypsin digestion led to fragmentation and detachment of Schwann cell basement membranes.
    • Myelin intraperiod bands lost density, and main period bands showed splitting after prolonged incubation.
    • Myelin structures transformed into vesicles, suggesting membrane detachment.

    Conclusions:

    • Trypsin effectively digests components of the Schwann cell basement membrane.
    • The study provides evidence for trypsin-digestible proteins within both the intraperiod and main period bands of PNS myelin.

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