Evidence map›Paper›PMID 11511814›Full record

ArticleGlycoconjugate journal2000

Genetic engineering of CHO cells producing human interferon-gamma by transfection of sialyltransferases.

K Fukuta, T Yokomatsu, R Abe, M Asanagi, T Makino

Abstract read
PubMed Publisher
In one paragraph

Article in Glycoconjugate journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.6field-weighted citation impact, top 30% 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

18 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Review
  3. Considerations for Glycoprotein Production.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Glycoengineering of Mammalian Expression Systems on a Cellular Level.Advances in biochemical engineering/biotechnology · 2021
    Article
  10. Article
  11. Implementation of Glycan Remodeling to Plant-Made Therapeutic Antibodies.International journal of molecular sciences · 2018
    Article
  12. Improving Immunotherapy Through Glycodesign.Frontiers in immunology · 2018
    Review
  13. Article
  14. Article
  15. Article
  16. Removal of sialic acid involving Klotho causes cell-surface retention of TRPV5 channel via binding to galectin-1.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  17. Article
  18. Article
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

5 authors at 2 institutions in 2 countries.

K FukutaLife Science Laboratory, Mitsui Chemicals, Inc., 1144 Togo, Mobara, Chiba 297-0017, Japan. kazuhiro.fukuta@mitsui-chem.co.jp
T Yokomatsu
R Abe
M Asanagi
T Makino
Life Science Institute · JPMitsui Chemicals (Japan) · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Natural human interferon-gamma (hIFN-gamma) contains mainly biantennary complex-type sugar chains. We previously remodeled the branch structures of N-glycans on hIFN-gamma in Chinese hamster ovary (CHO) cells by overexpressing UDP-N-acetylglucosamine: alpha1,6-D-mannoside beta1,6-N-acetylglucosaminyltransferase (GnT-V). Normal CHO cells primarily produced hIFN-gamma having biantennary sugar chains, whereas a CHO clone, designated IM4/Vh, transfected with GnT-V, primarily produced hIFN-gamma having GlcNAcbeta1-6 branched triantennary sugar chains when sialylation was incomplete and an increase in poly-N-acetyllactosamine (Galbeta1-4GlcNAcbeta1-3)n was observed. In the present study, we introduced mouse Galbeta1-3/4GlcNAc-R alpha2,3-sialyltransferase (ST3Gal IV) and/or rat Galbeta1-4GlcNAc-R alpha2,6-sialyltransferase (ST6Gal I) cDNAs into the IM4/Vh cells to increase the extent of sialylation and to examine the effect of sialyltransferase (ST) type on the linkage of sialic acid. Furthermore, we speculated that sialylation extent might affect the level of poly-N-acetyllactosamine. We isolated four clones expressing different levels of alpha2,3-ST and/or alpha2,6-ST. The extent of sialylation of hIFN-gamma from the IM4/Vh clone was 61.2%, which increased to about 80% in every ST transfectant. The increase occurred regardless of the type of overexpressed ST, and the proportion of alpha2,3- and alpha2,6-sialic acid corresponded to the activity ratio of alpha2,3-ST to alpha2,6-ST. Furthermore, the proportion of N-glycans containing poly-N-acetyllactosamine was significantly reduced (less than 10%) in the ST transfectants compared with the parental IM4/Vh clone (22.9%). These results indicated that genetic engineering of STs is highly effective for regulating the terminal structures of sugar chains on recombinant proteins in CHO cells.

Indexed as

Animalsbeta-D-Galactoside alpha 2-6-Sialyltransferasebeta-Galactoside alpha-2,3-SialyltransferaseCarbohydrate ConformationCarbohydrate SequenceCHO CellsChromatography, High Pressure LiquidClone CellsCloning, MolecularCricetinaeGenetic EngineeringHumansInterferon-gammaMiceMolecular Sequence DataN-Acetylneuraminic Acidbeta-D-Galactoside alpha 2-6-Sialyltransferasebeta-Galactoside alpha-2,3-SialyltransferaseInterferon-gammaN-Acetylneuraminic AcidRecombinant ProteinsSialyltransferases

Identifiers

PMID11511814
OpenAlexW1550849207

What OpenQuestion holds

Textmetadata
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.