Document Detail

Supramolecular aggregation and organization in peripheral nerve myelin.
MedLine Citation:
PMID:  6197534     Owner:  NLM     Status:  MEDLINE    
Under certain preparative conditions the lipid bilayers of glutaraldehyde-fixed, PNS myelin demonstrate a marked compartmentalization, which can be augmented by lipid extraction following sectioning. The results are interpreted as indicating a supramolecular domain pattern of arrangement centered upon the transmembrane protein (P0) molecules. The latter are thought to be surrounded by annuli of substantially immobilized phospholipids. In the lamellar planes particular lipids are considered to have a nonrandom distribution. The visualization of bilayer compartmentalization was seen only in negatively stained sections obtained from unembedded or glutaraldehyde-urea-embedded myelin. Lipids were unextracted in the basic preparations except in so far as some unfixed, amphipathic molecules escaped at the trough-fluid interface at the time of sectioning, an observed phenomenon which probably aided in the visualization of the compartmentalization. Visualization was also augmented by surface tension expanding section fragments as they floated on the trough fluid. All stages of transition between well-ordered myelin and dispersed globular units were commonly to be found. Deliberately delipidated myelin exposed more sharply defined and smaller globular units in bilayer regions, but even these are regarded as being supramolecular aggregates including residual lipid annuli around the transmembrane proteins. The addition of cadmium ions as a "fixative" for lecithin seemed to improve the preservation of glutaraldehyde-urea-embedded myelin but was not strictly necessary to reveal its domain structure. A secondary tannic acid fixation was required to process unembedded myelin so as to reveal the fundamental compartmentalization of its lipid bilayers.
D C Pease
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of ultrastructure research     Volume:  84     ISSN:  0022-5320     ISO Abbreviation:  J. Ultrastruct. Res.     Publication Date:  1983 Sep 
Date Detail:
Created Date:  1984-02-14     Completed Date:  1984-02-14     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0376344     Medline TA:  J Ultrastruct Res     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  275-88     Citation Subset:  IM    
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MeSH Terms
Cauda Equina / ultrastructure*
Hydrolyzable Tannins
Lipid Bilayers*
Macromolecular Substances
Membrane Lipids
Membrane Proteins
Microscopy, Electron
Myelin Sheath / ultrastructure*
Staining and Labeling
Grant Support
Reg. No./Substance:
0/Fixatives; 0/Hydrolyzable Tannins; 0/Lipid Bilayers; 0/Macromolecular Substances; 0/Membrane Lipids; 0/Membrane Proteins; 111-30-8/Glutaral; 57-13-6/Urea

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

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