Evidence map›Paper›PMID 16314835›Full record

ArticleOncogene2006

Full-length ADAMTS-1 and the ADAMTS-1 fragments display pro- and antimetastatic activity, respectively.

Y-J Liu, Y Xu, Q Yu

Open access · greenAbstract read
In one paragraph

Article in Oncogene, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

69 citing papers in PubMed, 163 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Loss ofInternational journal of molecular sciences · 2023
    Article
  8. The Role of ADAMTS Proteoglycanases in Thoracic Aortic Disease.International journal of molecular sciences · 2023
    Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Metalloproteases in gonad formation and ovulation.General and comparative endocrinology · 2021
    Review
  14. Regulation of ADAMTS Proteases.Frontiers in molecular biosciences · 2021
    Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article

9 more citing papers are in PubMed but not listed here.

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.

Y-J LiuDepartment of Pathobiology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.
Y Xu
Q Yu
University of Pennsylvania · US

Funding

Anti-cancer Activity and Mechanism of ADAMTS-1 FragmentsR01CA116510 · NCI · UNIVERSITY OF PENNSYLVANIA · PI YU, QIN · 2006 to 2010
$1.5M
Angiopoietins in AngiogenesisR01HL074117 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI YU, QIN · 2003 to 2006
$1.3M
NCI NIH HHS R01 CA116510NHLBI NIH HHS R01 HL074117NHLBI NIH HHS R01HL074117
6 · The paper itself

Abstract

The exact role of a disintegrin and metalloproteinase with thrombospondin motifs-1 (ADAMTS-1) and the underlying mechanism of its involvement in tumor metastasis have not been established. We have now demonstrated that overexpression of ADAMTS-1 promotes pulmonary metastasis of TA3 mammary carcinoma and Lewis lung carcinoma cells and that a proteinase-dead mutant of ADAMTS-1 (ADAMTS-1E/Q) inhibits their metastasis, indicating that the prometastatic activity of ADAMTS-1 requires its metalloproteinase activity. Overexpression of ADAMTS-1 in these cells promoted tumor angiogenesis and invasion, shedding of the transmembrane precursors of heparin-binding epidermal growth factor (EGF) and amphiregulin (AR), and activation of the EGF receptor and ErbB-2, while overexpression of ADAMTS-1E/Q inhibited these events. Furthermore, we found that ADAMTS-1 undergoes auto-proteolytic cleavage to generate the NH(2)- and COOH-terminal cleavage fragments containing at least one thrombospondin-type-I-like motif and that overexpression of the NH(2)-terminal ADAMTS-1 fragment and the COOH-terminal ADAMTS-1 fragment can inhibit pulmonary tumor metastasis. These fragments also inhibited Erk1/2 kinase activation induced by soluble heparin-binding EGF and AR. Taken together, our results suggest that the proteolytic status of ADAMTS-1 determines its effect on tumor metastasis, and that the ADAMTS-1E/Q and the ADAMTS-1 fragments likely inhibit tumor metastasis by negatively regulating the availability and activity of soluble heparin-binding EGF and AR.

Indexed as

Mammary Neoplasms, ExperimentalADAM ProteinsADAMTS1 ProteinAmino Acid SequenceAmphiregulinAnimalsApoptosisCarcinoma, Lewis LungCell ProliferationCollagenDrug CombinationsEGF Family of ProteinsEpidermal Growth FactorErb-b2 Receptor Tyrosine KinasesErbB ReceptorsFemaleADAM ProteinsADAMTS1 ProteinADAMTS1 protein, humanAmphiregulinAREG protein, humanAreg protein, mouseCollagenDrug CombinationsEGF Family of ProteinsEpidermal Growth FactorErb-b2 Receptor Tyrosine KinasesErbB ReceptorsGlycoproteinsHBEGF protein, humanHbegf protein, mouseHeparin-binding EGF-like Growth FactorIntercellular Signaling Peptides and ProteinsLamininmatrigelMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Proteoglycans

Identifiers

PMID16314835
PMCPMC2759703
OpenAlexW2091789160

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.