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  • Title: Distribution of (Na+ + K+)ATPase and sodium channels in skeletal muscle and electroplax.
    Author: Ariyasu RG, Deerinck TJ, Levinson SR, Ellisman MH.
    Journal: J Neurocytol; 1987 Aug; 16(4):511-22. PubMed ID: 2445928.
    Abstract:
    The distributions of (Na+ + K+)ATPase and sodium channels in skeletal muscle fibres and electrocytes were determined by immunofluorescent and immunoelectron microscopic techniques using antibodies against rat and eel (Na+ + K+)ATPase and the eel electric organ sodium channel. The extrajunctional sarcolemma of skeletal muscle was uniformly stained by polyclonal antibodies against (Na+ + K+)ATPase and the sodium channel. The T-tubule system of skeletal muscle was also labelled heavily for both (Na+ + K+)ATPase and the sodium channel. The terminal cisternae of the sarcoplasmic reticulum was stained for (Na+ + K+)ATPase but not sodium channels. At the motor endplate, (Na+ + K+)ATPase-like immunoreactivity was present along the plasmalemma of motor nerve terminals but not along the postsynaptic junctional sarcolemma. Paradoxically, a monoclonal antibody that binds to the alpha form of the catalytic subunit of (Na+ + K+)ATPase from rat hepatocytes and renal tubule cells did not label the enzyme in rat skeletal muscle. In electrocytes, (Na+ + K+)ATPase-like immunoreactivity was concentrated primarily along the plasmalemma and calveolae of the non-innervated face. In contrast, sodium channel-like immunoreactivity was concentrated along the plasmalemma of the innervated face except in the clefts of the postsynaptic membrane. Thus, we conclude that at endplates both the (Na+ + K+)ATPase of rat skeletal muscle and sodium channels of eel electrocytes are not concentrated in the juxtaneuronal postsynaptic membrane. We also interpret the failure of the monoclonal anti-alpha (Na+ + K+)ATPase antibodies to bind to the enzyme in muscle to indicate that the catalytic subunit of skeletal muscle (Na+ + K+)ATPase displays different epitopes than does the alpha subunit of kidney and liver.
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