Evidence map›Paper›PMID 23150666›Full record

ArticleThe Journal of biological chemistry2013

The polybasic insertion in autotaxin α confers specific binding to heparin and cell surface heparan sulfate proteoglycans.

Anna J S Houben, Xander M R van Wijk, Laurens A van Meeteren, Leonie van Zeijl, Els M A van de Westerlo, Jens Hausmann, Alexander Fish, Anastassis Perrakis, Toin H van Kuppevelt, Wouter H Moolenaar

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

23 citing papers in PubMed, 56 citations in OpenAlex.

  1. Review
  2. Article
  3. Lysophosphatidic acid signaling via LPAJournal of neurochemistry · 2022
    Article
  4. Review
  5. Design and Development of Autotaxin Inhibitors.Pharmaceuticals (Basel, Switzerland) · 2021
    Review
  6. Article
  7. Review
  8. Review
  9. Review
  10. Article
  11. Review
  12. Autotaxin determines colitis severity in mice and is secreted by B cells in the colon.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. 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

10 authors at 3 institutions in 1 country.

Anna J S HoubenDivision of Cell Biology, The Netherlands Cancer Institute, 1066CX Amsterdam, The Netherlands.
Xander M R van Wijk
Laurens A van Meeteren
Leonie van Zeijl
Els M A van de Westerlo
Jens Hausmann
Alexander Fish
Anastassis Perrakis
Toin H van Kuppevelt
Wouter H Moolenaar
The Netherlands Cancer Institute · NLRadboud University Medical Center · NLRadboud University Nijmegen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autotaxin (ATX) is a secreted lysophospholipase D that generates the lipid mediator lysophosphatidic acid (LPA), playing a key role in diverse physiological and pathological processes. ATX exists in distinct splice variants, but isoform-specific functions remain elusive. Here we characterize the ATXα isoform, which differs from the canonical form (ATXβ) in having a 52-residue polybasic insertion of unknown function in the catalytic domain. We find that the ATXα insertion is susceptible to cleavage by extracellular furin-like endoproteases, but cleaved ATXα remains structurally and functionally intact due to strong interactions within the catalytic domain. Through ELISA and surface plasmon resonance assays, we show that ATXα binds specifically to heparin with high affinity (K(d) ~10(-8) M), whereas ATXβ does not; furthermore, heparin moderately enhanced the lysophospholipase D activity of ATXα. We further show that ATXα, but not ATXβ, binds abundantly to SKOV3 carcinoma cells. ATXα binding was abolished after treating the cells with heparinase III, but not after chondroitinase treatment. Thus, the ATXα insertion constitutes a cleavable heparin-binding domain that mediates interaction with heparan sulfate proteoglycans, thereby targeting LPA production to the plasma membrane.

Indexed as

Amino Acid SequenceCell MembraneCell MovementCrystallography, X-RayEnzyme-Linked Immunosorbent AssayHEK293 CellsHeparan Sulfate ProteoglycansHeparinHumansKineticsLipidsLysophospholipase DLysophospholipidsMicroscopy, FluorescenceMolecular Sequence DataPhosphoric Diester HydrolasesHeparan Sulfate ProteoglycansHeparinLipidslysophosphatidic acidLysophospholipase DLysophospholipidsPhosphoric Diester Hydrolases

Identifiers

PMID23150666
PMCPMC3537048
OpenAlexW2081299557

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.