Evidence map›Paper›PMID 17284253›Full record

ArticleCancer science2007

Translocation of heparanase into nucleus results in cell differentiation.

Tetsuji Nobuhisa, Yoshio Naomoto, Takaomi Okawa, Munenori Takaoka, Mehmet Gunduz, Takayuki Motoki, Hitoshi Nagatsuka, Hidetsugu Tsujigiwa, Yasuhiro Shirakawa, Tomoki Yamatsuji and 8 more

Open access · greenAbstract read
In one paragraph

Article in Cancer science, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.7field-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

20 citing papers in PubMed, 48 citations in OpenAlex.

  1. Review
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  6. Heparanase-enhanced Shedding of Syndecan-1 and Its Role in Driving Disease Pathogenesis and Progression.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2020
    Review
  7. Heparanase and the hallmarks of cancer.Journal of translational medicine · 2020
    Review
  8. Review
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  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Mammalian heparanase: what is the message?Journal of cellular and molecular medicine
    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

18 authors at 4 institutions in 1 country.

Tetsuji NobuhisaDepartment of Gastroenterological Surgery, Transplant and Surgical Oncology, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, 2-5-1 Shikatacho, Okayama 700-8558, Japan.
Yoshio Naomoto
Takaomi Okawa
Munenori Takaoka
Mehmet Gunduz
Takayuki Motoki
Hitoshi Nagatsuka
Hidetsugu Tsujigiwa
Yasuhiro Shirakawa
Tomoki Yamatsuji
Minoru Haisa
Junji Matsuoka
Junichi Kurebayashi
Motowo Nakajima
Shun'ichiro Taniguchi
Junji Sagara
Jian Dong
Noriaki Tanaka
Okayama University · JPShinshu University · JPKawasaki Medical School · JPNovartis (Japan) · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We recently reported that heparanase, one of the extracellular matrix-degrading enzymes, which plays a critical role in cancer progression, is located not only in the cytoplasm but also in the nucleus. Here we identified nuclear translocation of heparanase as a key step in cell differentiation. We applied an in vitro differentiation model of HL-60 cells with 12-0-tetradecanoylphorbol-13-acetate (TPA), in which nuclear translocation of heparanase was observed using immunohistochemical analysis. In this system, nuclear translocation of heparanase was abolished by inhibitors of heat shock protein 90 (HSP90), suggesting the involvement of HSP90 in translocation of heparanase. We further confirmed that overexpression of active form of heparanase induced differentiation of HL-60 cells, although the catalytic negative form of heparanase did not. Therefore we speculate that nuclear translocation of enzymatically active heparanase may be involved in cellular differentiation. Our results suggest that a novel function of heparanase upon cell differentiation would raise a potential new strategy for cancer therapy of promyeloid leukemia and other types of cancer.

Indexed as

Cell DifferentiationBenzoquinonesCell NucleusCytoplasmGlucuronidaseHeparanaseHL-60 CellsHSP90 Heat-Shock ProteinsHumansLactams, MacrocyclicProtein TransportTetradecanoylphorbol AcetateBenzoquinonesgeldanamycinGlucuronidaseHeparanaseHSP90 Heat-Shock ProteinsLactams, MacrocyclicTetradecanoylphorbol Acetate

Identifiers

PMID17284253
PMCPMC11158264
OpenAlexW2045962611

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.