Document Detail


Reduced sialylation status in UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase (GNE)-deficient mice.
MedLine Citation:
PMID:  17235685     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Sialic acids are widely expressed as terminal carbohydrates on glycoconjugates of eukaryotic cells. They are involved in a variety of cellular functions, such as cell adhesion or signal recognition. The key enzyme of sialic acid biosynthesis is the bifunctional UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase (GNE), which catalyzes the first two steps of sialic acid biosynthesis in the cytosol. Previously, we have shown that inactivation of the GNE by gene targeting causes early embryonic lethality in mice, whereas heterozygous GNE-deficient mice are vital. In this study we compared the amount of membrane-bound sialic acids of wildtype mice with those of heterozygous GNE-deficient mice. For that we quantified membrane-bound sialic acid concentration in various organs of wildtype- and heterozygous GNE-deficient mice. We found an organ-specific reduction of membrane-bound sialic acids in heterozygous GNE-deficient mice. The overall reduction was 25%. Additionally, we analyzed transferrin and polysialylated neural cell adhesion molecule (NCAM) by one- or two-dimensional gel electrophoresis. Transferrin-expression was unchanged in heterozygous GNE-deficient mice; however the isoelectric point of transferrin was shifted towards basic pH, indicating a reduced sialylation. Furthermore, the expression of polysialic acids on NCAM was reduced in GNE-deficient mice.
Authors:
Daniel Gagiannis; André Orthmann; Ilona Danssmann; Martina Schwarzkopf; Wenke Weidemann; Rüdiger Horstkorte
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2007-01-19
Journal Detail:
Title:  Glycoconjugate journal     Volume:  24     ISSN:  0282-0080     ISO Abbreviation:  Glycoconj. J.     Publication Date:  2007 Apr 
Date Detail:
Created Date:  2007-03-02     Completed Date:  2007-11-08     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8603310     Medline TA:  Glycoconj J     Country:  United States    
Other Details:
Languages:  eng     Pagination:  125-30     Citation Subset:  IM    
Affiliation:
Institut für Physiologische, Chemie Hollystr. 1, 06114, Halle (Saale), Germany.
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MeSH Terms
Descriptor/Qualifier:
Animals
Cell Membrane / metabolism
Female
Glycoconjugates / chemistry,  metabolism
Heterozygote
Mice
Mice, Inbred C57BL
Mice, Knockout
Multienzyme Complexes / deficiency*,  genetics,  metabolism
Neural Cell Adhesion Molecules / chemistry,  metabolism
Sialic Acids / chemistry,  metabolism
Tissue Distribution
Transferrin / chemistry,  metabolism
Chemical
Reg. No./Substance:
0/Glycoconjugates; 0/Multienzyme Complexes; 0/Neural Cell Adhesion Molecules; 0/Sialic Acids; 0/UDP-N-acetylglucosamine 2-epimerase - N-acetylmannosamine kinase; 11096-37-0/Transferrin

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


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