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Membrane‐Associated Cytoskeletal Proteins in Squid Giant Axons
Author(s) -
Baumgold Jesse,
Terakawa Susumu,
Iwasa Kunihiko,
Gainer Harold
Publication year - 1981
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1981.tb01653.x
Subject(s) - axolemma , cytoskeleton , squid giant axon , neurofilament , intermediate filament , microbiology and biotechnology , tubulin , axon , axoplasm , biology , actin , biophysics , microtubule , chemistry , neuroscience , biochemistry , cell , central nervous system , immunology , myelin , immunohistochemistry
Abstract: Cytoskeletal proteins (e.g., tubulin, actin, and neurofilament proteins) in the squid giant axon are separable into KF‐soluble and ‐insoluble forms. The KF‐insoluble cytoskeletal components appear to constitute the major proteins in the subaxolemmal fibrous network on the inner surface of the axon. These cytoskeletal proteins and the subaxolemmal network are both highly soluble in KI solutions. Whereas giant axons tolerate prolonged perfusions in KF solutions with no loss of excitable properties, a relatively short perfusion with KI solution completely eliminates the excitability of the axon. The loss of this excitability correlates with the simultaneous dissolution of the subaxolemmal network of cytoskeletal proteins and the release of its proteins into the perfusate. These data support the hypothesis that cytoskeletal proteins associated with the inner surface of the axolemma are involved in the regulation of axonal excitability.