Document Detail


Neuroglycan C is a novel midkine receptor involved in process elongation of oligodendroglial precursor-like cells.
MedLine Citation:
PMID:  16901907     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Midkine is a heparin-binding growth factor that promotes cell attachment and process extension in undifferentiated bipolar CG-4 cells, an oligodendroglial precursor cell line. We found that CG-4 cells expressed a non-proteoglycan form of neuroglycan C, known as a part-time transmembrane proteoglycan. We demonstrated that neuroglycan C before or after chondroitinase ABC treatment bound to a midkine affinity column. Neuroglycan C lacking chondroitin sulfate chains was eluted with 0.5 m NaCl as a major fraction from the column. We confirmed that CG-4 cells expressed two isoforms of neuroglycan C, I, and III, by isolating cDNA. Among three functional domains of the extracellular part of neuroglycan C, the chondroitin sulfate attachment domain and acidic amino acid cluster box domain showed affinity for midkine, but the epidermal growth factor domain did not. Furthermore, cell surface neuroglycan C could be cross-linked with soluble midkine. Process extension on midkine-coated dishes was inhibited by either a monoclonal anti-neuroglycan C antibody C1 or a glutathione S-transferase-neuroglycan C fusion protein. Finally, stable transfectants of B104 neuroblastoma cells overexpressing neuroglycan C-I or neuroglycan C-III attached to the midkine substrate, spread well, and gave rise to cytoskeletal changes. Based on these results, we conclude that neuroglycan C is a novel component of midkine receptors involved in process elongation.
Authors:
Keiko Ichihara-Tanaka; Atsuhiko Oohira; Martin Rumsby; Takashi Muramatsu
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2006-08-10
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  281     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2006 Oct 
Date Detail:
Created Date:  2006-10-09     Completed Date:  2006-11-27     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  30857-64     Citation Subset:  IM    
Affiliation:
Department of Health Science, Faculty of Psychological and Physical Sciences, Aichi Gakuin University, 12 Araike, Iwasaki-cho, Nisshin, Aichi 470-0195, Japan.
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MeSH Terms
Descriptor/Qualifier:
Animals
Cell Line, Tumor
Cell Membrane / metabolism
Chondroitin ABC Lyase / metabolism
Chondroitin Sulfates / chemistry
Cytokines / metabolism
Epidermal Growth Factor / chemistry
Humans
Mice
Neuregulins / chemistry,  metabolism,  physiology*
Oligodendroglia / metabolism*
Protein Isoforms
Protein Structure, Tertiary
Proteochondroitin Sulfates / chemistry,  metabolism,  physiology*
Rats
Chemical
Reg. No./Substance:
0/Cytokines; 0/Neuregulins; 0/Protein Isoforms; 0/Proteochondroitin Sulfates; 0/neuroglycan C, human; 137497-38-2/midkine; 62229-50-9/Epidermal Growth Factor; 9007-28-7/Chondroitin Sulfates; EC 4.2.2.20/Chondroitin ABC Lyase

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


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