Document Detail

Mannose dependent tightening of the rat ependymal cell barrier. In vivo and in vitro study using neoglycoproteins.
MedLine Citation:
PMID:  8130735     Owner:  NLM     Status:  MEDLINE    
The possible role of carbohydrate binding proteins (lectins) and glycoconjugates in the formation of junctions ensuring tightening between ependymal cells was studied using synthetic glycoconjugates, the neoglycoproteins. These compounds are prepared by substituting bovine serum albumin with sugar residues and additional labelling (or not) with fluorescein or biotin. Injections of these components into the cerebral ventricles of adult rats resulted in a binding pattern which could be related to their carbohydrate composition. Mannose-containing neoglycoproteins were bound to ependymal cell cilia and penetrated rapidly the brain tissue. Such phenomenon was not seen with glucose- or galactose-containing neoglycoprotein molecules. In contrast, mannose-, galactose- and glucose-containing neoglycoproteins bound strongly to some endothelial cells around blood vessels. Fluorescent unglycosylated serum albumin did not bind to any brain structures. In contrast, co-injection of mannose-containing non-fluorescent neoglycoproteins with the other fluorescent compounds (including fluorescent sugar-free BSA) resulted in the penetration of the fluorescent compounds into the brain tissue. This internalization into brain was attributed to disaggregation of junctions between ependymal cells. Cultured ependymal cells behaved likewise. In short term experiments (5 min-1 h), only the mannose-containing neoglycoproteins bound strongly to the ependymal cells, particularly to the cilia. In long term experiments (1-9 days), mannose-containing neoglycoproteins specifically induced the disappearance of junctions between the cultured cells. These results emphasize the importance of mannose-dependent recognition system in the maintenance of junctions between ependymal cells, where a mannose-binding lectin has been previously detected.
S Kuchler; M N Graff; S Gobaille; G Vincendon; A C Roche; J P Delaunoy; M Monsigny; J P Zanetta
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Neurochemistry international     Volume:  24     ISSN:  0197-0186     ISO Abbreviation:  Neurochem. Int.     Publication Date:  1994 Jan 
Date Detail:
Created Date:  1994-04-21     Completed Date:  1994-04-21     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  8006959     Medline TA:  Neurochem Int     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  43-55     Citation Subset:  IM    
Laboratoire de Neurobiologie Moléculaire des Interactions Cellulaires, Centre de Neurochimie du CNRS, Strasbourg, France.
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MeSH Terms
Cells, Cultured
Endothelium, Vascular / metabolism
Ependyma / cytology*,  drug effects,  metabolism
Fluorescein-5-isothiocyanate / analogs & derivatives,  metabolism
Fluorescent Dyes
Galactose / metabolism
Glucose / metabolism
Glycoproteins / metabolism,  pharmacology*
Intercellular Junctions / drug effects
Mannose / metabolism,  pharmacology*
Microscopy, Fluorescence
Rats, Wistar
Serum Albumin, Bovine / metabolism
Reg. No./Substance:
0/Fluorescent Dyes; 0/Glycoproteins; 0/Serum Albumin, Bovine; 0/fluorescein isothiocyanate bovine serum albumin; 26566-61-0/Galactose; 31103-86-3/Mannose; 3326-32-7/Fluorescein-5-isothiocyanate; 50-99-7/Glucose

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