Evidence map›Paper›PMID 21690299›Full record

ArticleMolecular and cellular biology2011

The lysyl oxidase propeptide interacts with the receptor-type protein tyrosine phosphatase kappa and inhibits β-catenin transcriptional activity in lung cancer cells.

Nuria Sánchez-Morgan, Kathrin H Kirsch, Philip C Trackman, Gail E Sonenshein

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

22 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Article
  3. IGF-II regulates lysyl oxidase propeptide and mediates its effects in part via basic helix-loop-helix E40.Matrix biology : journal of the International Society for Matrix Biology · 2024
    Article
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  6. Review
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  11. Article
  12. Article
  13. Functional importance of lysyl oxidase family propeptide regions.Journal of cell communication and signaling · 2018
    Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Human copper-dependent amine oxidases.Archives of biochemistry and biophysics · 2014
    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

4 authors at 2 institutions in 1 country.

Nuria Sánchez-MorganDepartment of Biochemistry, Tufts University School of Medicine, Boston, Massachusetts 02111, USA.
Kathrin H Kirsch
Philip C Trackman
Gail E Sonenshein
Boston University · USTufts University · US

Funding

Signaling Pathways in Stages of TumorigenesisP01ES011624 · NIEHS · TUFTS UNIVERSITY BOSTON · PI SONENSHEIN, GAIL E. · 2001 to 2012
$11.4M
Lysyl Oxidase Propeptide: Breast Cancer InhibitorR01CA143108 · NCI · TUFTS UNIVERSITY BOSTON · PI SONENSHEIN, GAIL E. · 2010 to 2014
$2.5M
NFKB/REL AND THE PATHOGENESIS OF BREAST CANCERR01CA082742 · NCI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI SONENSHEIN, GAIL E. · 1999 to 2008
$2.2M
NCI NIH HHS R01 CA082742NCI NIH HHS R01 CA143108NIEHS NIH HHS P01 ES011624
6 · The paper itself

Abstract

The propeptide region of the lysyl oxidase proenzyme (LOX-PP) has been shown to inhibit Ras signaling in NIH 3T3 and lung cancer cells with activated RAS, but its mechanism of action is poorly understood. Here, a yeast two-hybrid assay of LOX-PP-interacting proteins identified a clone encoding the intracellular phosphatase domains of receptor-type protein tyrosine phosphatase kappa (RPTP-κ), and the interaction of the two proteins in mammalian cells was confirmed. RPTP-κ is proteolytically processed to isoforms that have opposing effects on β-catenin activity. The RPTP-κ transmembrane P subunit interacts with and sequesters β-catenin at the cell membrane, where it can associate with E-cadherin and promote intercellular interactions. At high cell density, further processing of the P subunit yields a phosphatase intracellular portion (PIC) subunit, which chaperones β-catenin to the nucleus, where it can function to activate transcription. Lung cancer cells were found to contain higher PIC levels than untransformed lung epithelial cells. In H1299 lung cancer cells, ectopic LOX-PP expression reduced the nuclear levels of PIC by increasing its turnover in the lysosome, thereby decreasing the nuclear levels and transcriptional activity of β-catenin while increasing β-catenin membrane localization. Thus, LOX-PP is shown to negatively regulate pro-oncogenic β-catenin signaling in lung cancer cells.

Indexed as

Transcription, Genetic3T3 CellsActive Transport, Cell NucleusAnimalsbeta CateninCell Line, TumorEnzyme PrecursorsGene Expression Regulation, NeoplasticHumansLung NeoplasmsMiceProtein-Lysine 6-Oxidaseras ProteinsReceptor-Like Protein Tyrosine Phosphatases, Class 2Signal Transductionbeta CateninCTNNB1 protein, mouseEnzyme PrecursorsProtein-Lysine 6-Oxidaseras ProteinsReceptor-Like Protein Tyrosine Phosphatases, Class 2

Identifiers

PMID21690299
PMCPMC3147807
OpenAlexW2171922931

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.