Document Detail


CD23 molecule acts as a galactose-binding lectin in the cell aggregation of EBV-transformed human B-cell lines.
MedLine Citation:
PMID:  7579799     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Epstein-Barr virus (EBV)-transformed human B-cell lines, L-KT9 and DH3 cells express CD23 antigen, and grow in a mixture of single and aggregated cells. The CD23 molecule has high amino acid sequence homology with C-type lectin and recently we have shown that the solubilized CD23 molecule can really interact with galactose residues on glycoproteins. In this study, therefore, we tested whether CD23 antigen on the cell surface really acts as a galactose-binding lectin in the aggregation of these cells. The EBV-transformed cells (L-KT9) were separated into an aggregated-cell-rich fraction and a single-cell-rich fraction. Aggregated cells disaggregated after removal of galactose by beta-galactosidase treatment, whereas single cells made large aggregation on sialidase treatment, and this aggregation was inhibited in the presence of asialo-fetuin. On the other hand, naturally aggregated cells become single cells with anti-CD23 monoclonal antibody (mAB) as well as the soluble form of CD23, but not with anti-CD21 mAB. In addition, L-KT9 and DH3 cells bound to asialo-fetuin-coupled Sepharose (ASF-Sepharose) and this binding was significantly inhibited by pre-treatment of cells with anti-CD23, but not with anti-CD21 or other anti-adhesion molecules. From these results, we conclude that the naturally aggregated state of EBV-transformed cells occurs mainly through the interaction of CD23 as a lectin molecule and galactose residues as its ligand.
Authors:
S Kijimoto-Ochiai; T Uede
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Glycobiology     Volume:  5     ISSN:  0959-6658     ISO Abbreviation:  Glycobiology     Publication Date:  1995 Jun 
Date Detail:
Created Date:  1995-12-07     Completed Date:  1995-12-07     Revised Date:  2012-06-06    
Medline Journal Info:
Nlm Unique ID:  9104124     Medline TA:  Glycobiology     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  443-8     Citation Subset:  IM    
Affiliation:
Section of Immunopathogenesis, Hokkaido University, Sapporo, Japan.
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MeSH Terms
Descriptor/Qualifier:
Antibodies, Monoclonal / pharmacology
Asialoglycoproteins / metabolism
B-Lymphocytes / immunology,  pathology*
Cell Aggregation* / drug effects
Cell Line, Transformed
Fetuins
Flow Cytometry
Galactose / metabolism*
Glycoproteins / metabolism
Herpesvirus 4, Human*
Humans
Lymphoma, B-Cell / immunology,  pathology*
Neuraminidase / pharmacology
Receptors, IgE / immunology,  metabolism*
Sepharose / metabolism
Tumor Cells, Cultured
alpha-Fetoproteins / metabolism
beta-Galactosidase / pharmacology
Chemical
Reg. No./Substance:
0/Antibodies, Monoclonal; 0/Asialoglycoproteins; 0/Fetuins; 0/Glycoproteins; 0/Receptors, IgE; 0/alpha-Fetoproteins; 0/asialofetuin; 26566-61-0/Galactose; 9012-36-6/Sepharose; EC 3.2.1.18/Neuraminidase; EC 3.2.1.23/beta-Galactosidase
Comments/Corrections
Erratum In:
Glycobiology. 2012 Jun;22(6):876

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


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