Document Detail

Occurrence of terminal alpha 2-->8-linked disialylated poly-N-acetyllactosamine chains with Le(X) and I antigenic glycotopes in tetraantennary arms of an N-linked glycoprotein isolated from rainbow trout ovarian fluid.
MedLine Citation:
PMID:  9134426     Owner:  NLM     Status:  MEDLINE    
The Pronase digestion of a 54K glycoprotein present in ovarian fluid of rainbow trout yielded a major glycopeptide. Carbohydrate compositional analysis revealed that this glycopeptide was likely to possess a single large N-glycan chain having low molecular weight oligomers of N-acetylneuraminic acid (oligoNeu5Ac). Structural studies of this glycopeptide revealed novel alpha 2-->8-linked disialylated poly-N-acetyllactosamine chains with Le(X) and I antigenic determinants on the N-linked tetraantennary core glycan. In our recent studies (Kitazume,S., Kitajima,K., Inoue,S., Inoue,Y. and Troy,F.A. (1994) J. Biol. Chem. 269, 10330-10340) we presented evidence that synthesis of alpha 2-->8-linked polysialic acid (polySia) chains is a two-step process in which chain initiation is catalyzed by an alpha 2-->8-sialyltransferase (alpha 2-->8-ST; initiase) that catalyzes synthesis of the first Sia alpha 2-->8-linkage, forming the disialic acid (diSia) unit, Sia alpha 2-->8-Sia alpha 2-->6-Gal-. Chain polymerization is then postulated to be catalyzed by a second enzyme, an alpha 2-->8-polyST ("polymerase") that converts the diSia units to polySia chains. The present structural studies leading to the discovery of alpha 2-->8-linked disialylated units that terminate poly-N-acetyllactosamine chains in an N-linked glycoprotein is further evidence in support of our hypothesis that more than one sialyltransferase activity is required for polySia chain synthesis and polymerization.
Y Funakoshi; T Taguchi; C Sato; K Kitajima; S Inoue; H R Morris; A Dell; Y Inoue
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Glycobiology     Volume:  7     ISSN:  0959-6658     ISO Abbreviation:  Glycobiology     Publication Date:  1997 Mar 
Date Detail:
Created Date:  1997-07-14     Completed Date:  1997-07-14     Revised Date:  2009-09-29    
Medline Journal Info:
Nlm Unique ID:  9104124     Medline TA:  Glycobiology     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  195-205     Citation Subset:  IM    
Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, Japan.
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MeSH Terms
Antigens, CD15
Carbohydrate Sequence
Magnetic Resonance Spectroscopy
Molecular Sequence Data
Oncorhynchus mykiss*
Ovary / chemistry*,  immunology
Polysaccharides / chemistry*,  immunology
Sequence Analysis
Sialoglycoproteins / chemistry*,  immunology
Spectrometry, Mass, Fast Atom Bombardment
Grant Support
//Wellcome Trust
Reg. No./Substance:
0/Antigens, CD15; 0/Epitopes; 0/Polysaccharides; 0/Sialoglycoproteins; 82441-98-3/poly-N-acetyllactosamine

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