Evidence map›Paper›PMID 24753252›Full record

ArticleThe Journal of biological chemistry2014

Heparan sulfate containing unsubstituted glucosamine residues: biosynthesis and heparanase-inhibitory activity.

Satomi Nadanaka, Eko Purunomo, Naoko Takeda, Jun-ichi Tamura, Hiroshi Kitagawa

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. 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 20% 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, 28 citations in OpenAlex.

  1. Article
  2. Article
  3. N-Acetylcysteine and Other Sulfur-Donors as a Preventative and Adjunct Therapy for COVID-19.Advances in pharmacological and pharmaceutical sciences · 2022
    Review
  4. Glycosaminoglycans: Sweet as Sugar Targets for Topical Skin Anti-Aging.Clinical, cosmetic and investigational dermatology · 2021
    Review
  5. Article
  6. Review
  7. Specific functions ofCellular & molecular biology letters · 2020
    Review
  8. Non-Anticoagulant Heparins as Heparanase Inhibitors.Advances in experimental medicine and biology · 2020
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  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

5 authors at 2 institutions in 1 country.

Satomi NadanakaFrom the Department of Biochemistry, Kobe Pharmaceutical University, 4-19-1 Motoyamakita-machi, Higashinada-ku, Kobe, Hyogo 658-8558, Japan.
Eko PurunomoFrom the Department of Biochemistry, Kobe Pharmaceutical University, 4-19-1 Motoyamakita-machi, Higashinada-ku, Kobe, Hyogo 658-8558, Japan.
Naoko Takedathe Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University, 4-101 Koyamacho-Minami, Tottori 680-8552, Japan, and.
Jun-ichi Tamurathe Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University, 4-101 Koyamacho-Minami, Tottori 680-8552, Japan, and the Department of Regional Environment, Faculty of Regional Sciences, Tottori University, Tottori, Tottori 680-8551, Japan.
Hiroshi KitagawaFrom the Department of Biochemistry, Kobe Pharmaceutical University, 4-19-1 Motoyamakita-machi, Higashinada-ku, Kobe, Hyogo 658-8558, Japan, kitagawa@kobepharma-u.ac.jp.
Kobe Pharmaceutical University · JPTottori University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Degradation of heparan sulfate (HS) in the extracellular matrix by heparanase is linked to the processes of tumor invasion and metastasis. Thus, a heparanase inhibitor can be a potential anticancer drug. Because HS with unsubstituted glucosamine residues accumulates in heparanase-expressing breast cancer cells, we assumed that these HS structures are resistant to heparanase and can therefore be utilized as a heparanase inhibitor. As expected, chemically synthetic HS-tetrasaccharides containing unsubstituted glucosamine residues, GlcAβ1-4GlcNH3 (+)(6-O-sulfate)α1-4GlcAβ1-4GlcNH3 (+)(6-O-sulfate), inhibited heparanase activity and suppressed invasion of breast cancer cells in vitro. Bifunctional NDST-1 (N-deacetylase/N-sulfotransferase-1) catalyzes the modification of N-acetylglucosamine residues within HS chains, and the balance of N-deacetylase and N-sulfotransferase activities of NDST-1 is thought to be a determinant of the generation of unsubstituted glucosamine. We also report here that EXTL3 (exostosin-like 3) controls N-sulfotransferase activity of NDST-1 by forming a complex with NDST-1 and contributes to generation of unsubstituted glucosamine residues.

Indexed as

AnimalsBreast NeoplasmsFemaleFibroblastsGlucosamineGlucuronidaseGlycosaminoglycansHeparanaseHeparan Sulfate ProteoglycansHumansMCF-7 CellsMiceN-AcetylglucosaminyltransferasesNeoplasm InvasivenessSulfotransferasesEXTL3 protein, humanExtl3 protein, mouseGlucosamineGlucuronidaseGlycosaminoglycansHeparanaseHeparan Sulfate Proteoglycansheparitin sulfotransferaseN-AcetylglucosaminyltransferasesSulfotransferasesGlycobiologyGlycosaminoglycanGlycosidaseHeparanaseHeparan SulfateProteoglycanProteoglycan Synthesis

Identifiers

PMID24753252
PMCPMC4140882
OpenAlexW2046931245

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.