Evidence map›Paper›PMID 11463354›Full record

ArticleThe Biochemical journal2001

Knockout of mouse beta 1,4-galactosyltransferase-1 gene results in a dramatic shift of outer chain moieties of N-glycans from type 2 to type 1 chains in hepatic membrane and plasma glycoproteins.

N Kotani, M Asano, Y Iwakura, S Takasaki

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.5field-weighted citation impact, top 18% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Challenge to the suppression of tumor growth by the β4-galactosyltransferase genes.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2015
    Review
  5. Article
  6. The Angelman syndrome protein Ube3a/E6AP is required for Golgi acidification and surface protein sialylation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. β1,4-Galactosyltransferase-I contributes to the inflammatory processes in synovial tissue of patients with rheumatoid arthritis.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2010
    Article
  13. Article
  14. Article
  15. The congenital disorders of glycosylation: a multifaceted group of syndromes.NeuroRx : the journal of the American Society for Experimental NeuroTherapeutics · 2006
    Review
  16. Article
  17. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 1 country.

N KotaniDivision of Biochemistry, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.
M Asano
Y Iwakura
S Takasaki
Tokyo University of Science · JPThe University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To understand the contribution of beta 1,4-galactosyltransferase (beta 4Gal-T)-1 to galactosylation in vivo, N-glycans of hepatic membrane glycoproteins and plasma glycoproteins from beta 4Gal-T1 wild-type (beta 4Gal-T1(+/+)) and beta 4Gal-T1 knockout mice were compared. Unexpectedly, glycoproteins from the knockout mice were found to express considerable amounts of sialylated, galactosylated N-glycans. A striking contrast was that galactose residues were largely beta 1,4-linked to GlcNAc residues in the beta 4Gal-T1(+/+) mouse glycans but beta 1,3-linked in the knockout mouse glycans, thus resulting in the shift of the backbone structure from type 2 chain (Gal beta 1-->4GlcNAc) to type 1 chain (Gal beta 1-->3GlcNAc). Detailed analysis of plasma glycoproteins revealed that the expression of sialyl linkage in N-glycans was shifted from the Sia alpha 2-->6Gal to the Sia alpha 2-->3Gal, and oversialylated type 1 chains were, remarkably, found in the knockout mouse glycans. Thus beta 4Gal-T1 deficiency was primarily compensated for by beta1,3-galactosyltransferases, which resulted in different sialyl linkages being formed on the outer chains and altered backbone structures, depending on the acceptor specificities of sialyltransferases. These results suggest that beta 4Gal-T1 in mouse liver plays a central role in the synthesis of type 2 chain and is also involved in the regulation of sialylation of N-glycans. The knockout mice may prove useful in investigation of the mechanism which regulates the tissue-dependent terminal glycosylation.

Indexed as

AnimalsCell MembraneGalactoseGalactosyltransferasesLiverMembrane GlycoproteinsMiceMice, KnockoutPolysaccharidesbeta-1,4-galactosyltransferase IGalactoseGalactosyltransferasesMembrane GlycoproteinsPolysaccharides

Identifiers

PMID11463354
PMCPMC1222013
OpenAlexW2057600288

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.