Electron microscopic study of intramembranous changes in protein-extracted peripheral nervous system myelin

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Abstract
Sciatic nerves from young mice were incubated for 2–8 hours in 0.5% Triton X‐100 in 0.5 M ammonium acetate, a solution which solubilizes the large and small basic proteins of the myelin sheath. As previously noted (Peterson and Gruener, 1978), myelin sheaths from treated nerves extensively split and unravelled along major dense lines. Small focal areas of compact myelin remained. In freeze‐fracture replicas, areas of myelin with lamellar splitting contained few intramembranous particles, while membrane areas with greater than normal densities of particles were associated with the patches of compact myelin membrane. Fixation for as short a time as 15 minutes stabilized the myelin membrane enough to prevent the Triton X‐100 effects, even when incubations were extended to 20 hours. Controls, both untreated and 0.5 M ammonium acetate‐treated nerves, had predominantly compact myelin sheaths; their leaflets were covered with numerous intramembranous particles. The data suggest that Triton X‐100 alters the compact structure of peripheral nervous system myelin. In areas where lamellae are split and separated, there is a loss of intramembranous particles. It appears that the loss of intramembranous particles is related to the removal of the basic proteins which are located in major dense line regions of compact myelin sheaths.