Document Detail

Arginine-rich proteins in spherical inclusions of human locus coeruleus neurons demonstrated by benzil modification.
MedLine Citation:
PMID:  6208239     Owner:  NLM     Status:  MEDLINE    
Previous studies have shown that aminergic neurons in the normal human brain contain acidophilic cytoplasmic inclusions--called protein bodies (PBs)--that are reduced or absent in parkinsonism and disrupted in depression. The purpose of the present study was to elucidate the constitution of PBs in five formalin-fixed normal human brains using histochemical methods specific for histones, protamines, and the amino acid arginine. PBs were revealed with alkaline fast green and bromphenol blue, exhibiting a high content in histones and in protamines. They developed blue metachromasia with phosphotungstic acid-hematoxylin and green fluorescence with phenanthrenequinone, which established the presence of arginyl residues. Using benzil, which selectively modifies the guanido group of arginine, staining was blocked for each of the above two methods. The application of Mallory's trichrome procedure after benzil differentiated the PBs into an unstained core and a still fuchsinophilic rim. Since the fuchsinophilia of the rim was shown to persist after acetylation as well, we suggest that this rim probably contains acidic macromolecules that attach to the basic charges of the amphoteric acid fuchsin. We conclude that the PB are complex structures consisting of a core segregating arginine-rich proteins and a rim which probably contains macromolecules of an acidic nature.
M T Panayotacopoulou; M R Issidorides
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society     Volume:  32     ISSN:  0022-1554     ISO Abbreviation:  J. Histochem. Cytochem.     Publication Date:  1984 Nov 
Date Detail:
Created Date:  1984-12-05     Completed Date:  1984-12-05     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9815334     Medline TA:  J Histochem Cytochem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1192-6     Citation Subset:  IM    
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MeSH Terms
Aldehydes / diagnostic use*
Arginine / metabolism*
Histological Techniques*
Inclusion Bodies / metabolism*
Locus Coeruleus / metabolism*
Nerve Tissue Proteins / metabolism*
Neurons / metabolism
Phenylglyoxal / analogs & derivatives,  diagnostic use*
Staining and Labeling
Reg. No./Substance:
0/Aldehydes; 0/Nerve Tissue Proteins; 1074-12-0/Phenylglyoxal; 134-81-6/benzil; 74-79-3/Arginine

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

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