Document Detail


Oligosaccharides on living human neuroblastoma cells of dissimilar degrees of differentiation. A flow-cytometric study with sugar-specific lectins and glycosidases.
MedLine Citation:
PMID:  7895249     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The present study is an attempt to correlate cell-surface saccharide composition and/or disposition with malignant behavior and differentiation of two established human neuroblastoma sublines. The methodology applied was quantitative flow-cytometric evaluation of binding data for sugar-specific lectins in conjunction with cell-surface modification by specific glycosidases. The relevant parameters were both the number of binding sites and their apparent affinity constants for the respective lectins on native cells as well as the expected shift of those values after sequential treatment with specific glycosidases. The main conclusions from the findings may be summarized as follows: 1. There appears to exist a correlation between differentiation and/or maturation of neural cells and their cell-surface oligosaccharide patterns, as deduced indirectly by the biophysical approach of quantitative evaluation of lectin-binding data. More specifically, our findings support the hypothesis of a strong correlation between the degree of sialylation of terminal saccharide structures and the relative immaturity and/or lack of differentiation of the respective cells by morphological and biochemical criteria. 2. The combined application of specific lectins and glycosidases should be further exploited for similar purposes since it yields unequivocal information, provided that all biochemical and biophysical methods are scrutinized for their specificity. 3. Flow cytometry with fluorescence-labeled lectins is especially suited for the purposes mentioned since it allows quantitative binding studies to be conducted in a quick and uncomplicated manner. Most importantly, these data can be derived from intact living cells.
Authors:
B Pepperl; B Bohn; A Sauer; R Brossmer
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Cell biophysics     Volume:  23     ISSN:  0163-4992     ISO Abbreviation:  Cell Biophys.     Publication Date:    1993 Aug-Dec
Date Detail:
Created Date:  1995-04-21     Completed Date:  1995-04-21     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  8002185     Medline TA:  Cell Biophys     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  165-85     Citation Subset:  IM    
Affiliation:
Institut für Biochemie II (Med. Fak) der Universität Heidelberg, Germany.
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MeSH Terms
Descriptor/Qualifier:
Binding Sites
Cell Differentiation
Female
Flow Cytometry
Glycoside Hydrolases / metabolism*
Humans
Lectins / metabolism*
Membrane Glycoproteins / analysis
N-Acetylneuraminic Acid
Neuraminidase / metabolism
Neuroblastoma / chemistry*,  enzymology,  metabolism,  pathology*
Oligosaccharides / analysis*,  chemistry,  metabolism
Sialic Acids / analysis
Sialoglycoproteins / analysis
Tumor Cells, Cultured
Chemical
Reg. No./Substance:
0/Lectins; 0/Membrane Glycoproteins; 0/Oligosaccharides; 0/Sialic Acids; 0/Sialoglycoproteins; 131-48-6/N-Acetylneuraminic Acid; EC 3.2.1.-/Glycoside Hydrolases; EC 3.2.1.18/Neuraminidase

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


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