Evidence map›Paper›PMID 20007507›Full record

ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2010

A novel human heparanase splice variant, T5, endowed with protumorigenic characteristics.

Uri Barash, Victoria Cohen-Kaplan, Gil Arvatz, Svetlana Gingis-Velitski, Flonia Levy-Adam, Ofer Nativ, Ronen Shemesh, Michal Ayalon-Sofer, Neta Ilan, Israel Vlodavsky

Abstract read
In one paragraph

Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

25 citing papers in PubMed, 38 citations in OpenAlex.

  1. The Pathophysiological Functions of Heparanases: From Evolution, Structural and Tissue-Specific Perspectives.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Expression of heparanase in soft tissue sarcomas of adults.Journal of experimental & clinical cancer research : CR · 2014
    Article
  16. Article
  17. Significance of heparanase in cancer and inflammation.Cancer microenvironment : official journal of the International Cancer Microenvironment Society · 2012
    Article
  18. Article
  19. Article
  20. 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

10 authors at 3 institutions in 1 country.

Uri BarashCancer and Vascular Biology Research Center, Faculty of Medicine, Technion, P.O. Box 9649, Haifa 31096, Israel.
Victoria Cohen-Kaplan
Gil Arvatz
Svetlana Gingis-Velitski
Flonia Levy-Adam
Ofer Nativ
Ronen Shemesh
Michal Ayalon-Sofer
Neta Ilan
Israel Vlodavsky
Rappaport Family Institute for Research in the Medical Sciences · ILCompugen (Israel) · ILBnai Zion Medical Center · IL

Funding

Regulation of heparanase in cancer progressionR01CA106456 · NCI · TECHNION-ISRAEL INSTITUTE OF TECHNOLOGY · PI VLODAVSKY, ISRAEL · 2004 to 2013
$1.7M
NCI NIH HHS R01 CA106456NCI NIH HHS R01-CA106456
6 · The paper itself

Abstract

Heparanase is a mammalian endo-beta-d-glucuronidase that can cleave heparan sulfate side chains, an activity strongly implicated in tumor cell dissemination. The current study aimed to identify and characterize heparanase splice variants. LEADS, Compugen's alternative splicing modeling platform (Compugen, Tel Aviv, Israel), was used to search for splice variants in silico; tumor-derived cell lines (i.e., CAG myeloma) and tumor biopsies were utilized to validate T5 expression in vivo; signaling (i.e., Src phosphorylation) was evaluated following T5 gene silencing or overexpression and correlated with cell proliferation, colony formation, and tumor xenograft development. A novel spliced form of human heparanase, termed T5, was identified. In this splice variant, 144 bp of intron 5 are joined with exon 4, which results in a truncated, enzymatically inactive protein. T5 overexpression resulted in increased cell proliferation and larger colonies in soft agar, mediated by Src activation. Furthermore, T5 overexpression markedly enhanced tumor xenograft development. T5 expression is up-regulated in 75% of human renal cell carcinoma biopsies examined, which suggests that this splice variant is clinically relevant. Controls included cells overexpressing wild-type heparanase or an empty plasmid and normal-looking tissue adjacent the carcinoma lesion. T5 is a novel functional splice variant of human heparanase endowed with protumorigenic characteristics.-Barash, U., Cohen-Kaplan, V., Arvatz, G., Gingis-Velitski, S., Levy-Adam, F., Nativ, O., Shemesh, R., Ayalon-Sofer, M., Ilan, N., Vlodavsky, I. A novel human heparanase splice variant, T5, endowed with protumorigenic characteristics.

Indexed as

Alternative SplicingGene Expression Regulation, EnzymologicGene Expression Regulation, NeoplasticAnimalsCell Line, TumorCell ProliferationFemaleGene SilencingGlucuronidaseHeparanaseHeparan SulfateHumansMaleMiceMice, NudeModels, GeneticGlucuronidaseHeparanaseHeparan SulfateNeoplasm Proteins

Identifiers

PMID20007507
PMCPMC2845434
OpenAlexW2063158419

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.