Evidence map›Paper›PMID 24788042›Full record

ArticleCellular and molecular life sciences : CMLS2014

Processing of heparanase is mediated by syndecan-1 cytoplasmic domain and involves syntenin and α-actinin.

Anna Shteingauz, Neta Ilan, Israel Vlodavsky

Abstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 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
2.1field-weighted citation impact, top 15% 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, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Review
  7. Heparanase in Acute Kidney Injury.Advances in experimental medicine and biology · 2020
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Heparanase: From basic research to therapeutic applications in cancer and inflammation.Drug resistance updates : reviews and commentaries in antimicrobial and anticancer chemotherapy · 2016
    Review
  13. Article
  14. Observational
  15. Article
  16. Article
  17. Targeting tumor invasion: the roles of MDA-9/Syntenin.Expert opinion on therapeutic targets · 2015
    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

3 authors at 1 institution in 1 country.

Anna ShteingauzCancer and Vascular Biology Research Center, the Bruce Rappaport Faculty of Medicine, Technion, 9649, 31096, Haifa, Israel.
Neta Ilan
Israel Vlodavsky
Rappaport Family Institute for Research in the Medical Sciences · 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 CA106456NCI NIH HHS R01 CA106456
6 · The paper itself

Abstract

Heparanase activity plays a decisive role in cell dissemination associated with cancer metastasis. Cellular uptake of heparanase is considered a pre-requisite for the delivery of latent 65-kDa heparanase to lysosomes and its subsequent proteolytic processing and activation into 8- and 50-kDa protein subunits by cathepsin L. Heparan sulfate proteoglycans, and particularly syndecan, are instrumental for heparanase uptake and activation, through a process that has been shown to occur independent of rafts. Nevertheless, the molecular mechanism underlying syndecan-mediated internalization outside of rafts is unclear. Here, we examined the role of syndecan-1 cytoplasmic domain in heparanase processing, utilizing deletion constructs lacking the entire cytoplasmic domain (Delta), the conserved (C1 or C2), or variable (V) regions. Heparanase processing was markedly increased following syndecan-1 over-expression; in contrast, heparanase was retained at the cell membrane and its processing was impaired in cells over-expressing syndecan-1 deleted for the entire cytoplasmic tail. We have next revealed that conserved domain 2 (C2) and variable (V) regions of syndecan-1 cytoplasmic tail mediate heparanase processing. Furthermore, we found that syntenin, known to interact with syndecan C2 domain, and α actinin are essential for heparanase processing.

Indexed as

ActininAnimalsCell Line, TumorCell MembraneGlucuronidaseHEK293 CellsHeparanaseHumansMiceProtein Structure, TertiaryRNA InterferenceRNA, Small InterferingSyndecan-1SynteninsActininGlucuronidaseHeparanaseRNA, Small InterferingSyndecan-1Syntenins

Identifiers

PMID24788042
PMCPMC4209210
OpenAlexW1970851962

What OpenQuestion holds

Textmetadata
LicenceTDM
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.