Document Detail

Expression of human alpha-l-fucosyltransferase gene homologs in monkey kidney COS cells and modification of potential fucosyltransferase acceptor substrates by an endogenous glycosidase.
MedLine Citation:
PMID:  9949196     Owner:  NLM     Status:  MEDLINE    
Previous investigations on the monkey kidney COS cell line demonstrated the weak expression of fucosylated cell surface antigens and presence of endogenous fucosyltransferase activities in cell extracts. RT-PCR analyses have now revealed expression of five homologs of human fucosyltransferase genes, FUT1, FUT4, FUT5, FUT7, and FUT8, in COS cell mRNA. The enzyme in COS cell extracts acting on unsialylated Type 2 structures is closely similar in its properties to the alpha1,3-fucosyltransferase encoded by human FUT4 gene and does not resemble the product of the FUT5 gene. Although FUT1 is expressed in the COS cell mRNA, it has not been possible to demonstrate alpha1,2-fucosyltransferase activity in cell extracts but the presence of Le(y) and blood-group A antigenic determinants on the cell surface imply the formation of H-precursor structures at some stage. The most strongly expressed fucosyltransferase in the COS cells is the alpha1,6-enzyme transferring fucose to the innermost N -acetylglucosamine unit in N -glycan chains; this enzyme is similar in its properties to the product of the human FUT8 gene. The enzymes resembling the human FUT4 and FUT8 gene products both had pH optima of 7.0 and were resistant to 10 mM NEM. The incorporation of fucose into asialo-fetuin was optimal at 5.5 and was inhibited by 10 mM NEM. This result initially suggested the presence of a third fucosyltransferase expressed in the COS cells but we have now shown that triantennary N- glycans with terminal nonreducing galactose units, similar to those present in asialo-fetuin, are modified by a weak endogenous beta-galactosidase in the COS cell extracts and thereby rendered suitable substrates for the alpha1,6-fucosyltransferase.
J L Clarke; W M Watkins
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Glycobiology     Volume:  9     ISSN:  0959-6658     ISO Abbreviation:  Glycobiology     Publication Date:  1999 Feb 
Date Detail:
Created Date:  1999-03-12     Completed Date:  1999-03-12     Revised Date:  2009-09-29    
Medline Journal Info:
Nlm Unique ID:  9104124     Medline TA:  Glycobiology     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  191-202     Citation Subset:  IM    
Department of Haematology, Imperial College School of Medicine, Hammersmith Hospital, London W12 ONN, UK.
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MeSH Terms
ABO Blood-Group System
Asialoglycoproteins / metabolism
COS Cells / enzymology*
Carbohydrate Sequence
Cercopithecus aethiops / genetics
Cross Reactions
DNA, Complementary / genetics
Fucosyltransferases / antagonists & inhibitors,  genetics,  immunology,  metabolism*
Glycoside Hydrolases / analysis
Glycosyltransferases / analysis
Kidney / enzymology
Lactose / metabolism
Molecular Sequence Data
Oligosaccharides / biosynthesis*,  metabolism
Polymerase Chain Reaction
RNA, Messenger / genetics
Sequence Homology, Amino Acid
Species Specificity
Substrate Specificity
Sugar Acids / pharmacology
alpha-Fetoproteins / metabolism
beta-Galactosidase / analysis
Grant Support
//Wellcome Trust
Reg. No./Substance:
0/5-acetylneuraminyl-(2-3)-galactosyl-(1-4)-(fucopyranosyl-(1-3))-N-acetylglucosamine; 0/ABO Blood-Group System; 0/Asialoglycoproteins; 0/DNA, Complementary; 0/Oligosaccharides; 0/RNA, Messenger; 0/Sugar Acids; 0/alpha-Fetoproteins; 0/asialofetuin; 2426-46-2/galactonolactone; 63-42-3/Lactose; EC 2.4.-/Glycosyltransferases; EC 2.4.1.-/Fucosyltransferases; EC 3.2.1.-/Glycoside Hydrolases; EC

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