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Subaxolemmal cytoskeleton in squid giant axon. II. Morphological identification of microtubule- and microfilament-associated domains of axolemma.
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MedLine Citation:
PMID:  3700475     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
In the preceding paper (Kobayashi, T., S. Tsukita, S. Tsukita, Y. Yamamoto, and G. Matsumoto, 1986, J. Cell Biol., 102:1710-1725), we demonstrated biochemically that the subaxolemmal cytoskeleton of the squid giant axon was highly specialized and mainly composed of tubulin, actin, axolinin, and a 255-kD protein. In this paper, we analyzed morphologically the molecular organization of the subaxolemmal cytoskeleton in situ. For thin section electron microscopy, the subaxolemmal cytoskeleton was chemically fixed by the intraaxonal perfusion of the fixative containing tannic acid. With this fixation method, the ultrastructural integrity was well preserved. For freeze-etch replica electron microscopy, the intraaxonally perfused axon was opened and rapidly frozen by touching its inner surface against a cooled copper block (4 degrees K), thus permitting the direct stereoscopic observation of the cytoplasmic surface of the axolemma. Using these techniques, it became clear that the major constituents of the subaxolemmal cytoskeleton were microfilaments and microtubules. The microfilaments were observed to be associated with the axolemma through a specialized meshwork of thin strands, forming spot-like clusters just beneath the axolemma. These filaments were decorated with heavy meromyosin showing a characteristic arrowhead appearance. The microtubules were seen to run parallel to the axolemma and embedded in the fine three-dimensional meshwork of thin strands. In vitro observations of the aggregates of axolinin and immunoelectron microscopic analysis showed that this fine meshwork around microtubules mainly consisted of axolinin. Some microtubules grazed along the axolemma and associated laterally with it through slender strands. Therefore, we were led to conclude that the axolemma of the squid giant axon was specialized into two domains (microtubule- and microfilament-associated domains) by its underlying cytoskeletons.
Authors:
S Tsukita; S Tsukita; T Kobayashi; G Matsumoto
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Journal of cell biology     Volume:  102     ISSN:  0021-9525     ISO Abbreviation:  J. Cell Biol.     Publication Date:  1986 May 
Date Detail:
Created Date:  1986-06-12     Completed Date:  1986-06-12     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  0375356     Medline TA:  J Cell Biol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1710-25     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Animals
Axons / ultrastructure*
Cell Compartmentation
Cytoskeleton / ultrastructure*
Decapodiformes
Freeze Etching
Hydrolyzable Tannins / diagnostic use
Microfilaments / ultrastructure
Microscopy, Electron / methods
Microtubule-Associated Proteins / metabolism
Microtubules / ultrastructure
Nerve Tissue Proteins / metabolism
Neurilemma / ultrastructure*
Chemical
Reg. No./Substance:
0/Hydrolyzable Tannins; 0/Microtubule-Associated Proteins; 0/Nerve Tissue Proteins
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Full Text
Journal Information
Journal ID (nlm-ta): J Cell Biol
ISSN: 0021-9525
ISSN: 1540-8140
Publisher: The Rockefeller University Press
Article Information
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Print publication date: Day: 1 Month: 5 Year: 1986
Volume: 102 Issue: 5
First Page: 1710 Last Page: 1725
ID: 2114206
Publisher Id: 86196246
PubMed Id: 3700475

Subaxolemmal cytoskeleton in squid giant axon. II. Morphological identification of microtubule- and microfilament-associated domains of axolemma


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