Document Detail

UDP-GlcNAc concentration is an important factor in the biosynthesis of beta1,6-branched oligosaccharides: regulation based on the kinetic properties of N-acetylglucosaminyltransferase V.
MedLine Citation:
PMID:  11886845     Owner:  NLM     Status:  MEDLINE    
Human beta1,6-N-acetylglucosaminyltransferase V (GnT-V) was expressed by baculovirus-insect cell system, and the purified recombinant enzyme was kinetically characterized. The data obtained were used to establish the kinetic basis of the substrate specificity toward donor nucleotide sugars, and also revealed that K(m) values for the donors are much higher compared to those of other GlcNAc transferases, the kinetic properties of which have been reported. Because this exceptionally higher K(m) suggests that GnT-V is physiologically present at far from saturated conditions, it would appear that the production of beta1,6-branched oligosaccharide, which is formed by GnT-V, could be regulated in vivo by the concentration of the donor, UDP-GlcNAc, as well as the expression levels of the enzyme. When B16 melanoma cells, which express high levels of GnT-V, were incubated with GlcNAc, the beta1,6-branched oligosaccharide levels were increased, as judged by a lectin blot analysis, in conjunction with an increase in intracellular UDP-GlcNAc. These findings suggest that the level of UDP-GlcNAc can be a critical factor in the production of beta1,6-branched oligosaccharides, for example, by tumor cells, which have been thought to be closely associated with tumor progression and metastasis.
Ken Sasai; Yoshitaka Ikeda; Tsuneko Fujii; Takeo Tsuda; Naoyuki Taniguchi
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Glycobiology     Volume:  12     ISSN:  0959-6658     ISO Abbreviation:  Glycobiology     Publication Date:  2002 Feb 
Date Detail:
Created Date:  2002-03-11     Completed Date:  2002-09-06     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9104124     Medline TA:  Glycobiology     Country:  England    
Other Details:
Languages:  eng     Pagination:  119-27     Citation Subset:  IM    
Department of Biochemistry, Osaka University Medical School, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan.
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MeSH Terms
Baculoviridae / genetics,  metabolism
Cell Line
Electrophoresis, Polyacrylamide Gel
Mass Spectrometry
Melanoma, Experimental / metabolism
Mutagenesis, Site-Directed
N-Acetylglucosaminyltransferases / genetics,  isolation & purification,  metabolism*
Oligosaccharides, Branched-Chain / metabolism
Recombinant Proteins / antagonists & inhibitors,  chemistry,  metabolism
Substrate Specificity
Uridine Diphosphate N-Acetylglucosamine / biosynthesis*
Reg. No./Substance:
0/Oligosaccharides, Branched-Chain; 0/Recombinant Proteins; 528-04-1/Uridine Diphosphate N-Acetylglucosamine; EC 2.4.1.-/N-Acetylglucosaminyltransferases; EC,6-mannosylglycoprotein beta 1,6-N-acetylglucosaminyltransferase

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