Evidence map›Paper›PMID 26345369›Full record

ArticleJournal of cell science2015

LPP3 localizes LPA6 signalling to non-contact sites in endothelial cells.

Hiroshi Yukiura, Kuniyuki Kano, Ryoji Kise, Asuka Inoue, Junken Aoki

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2015. 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
1.8field-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, 33 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Role of G-protein coupled receptors in cardiovascular diseases.Frontiers in cardiovascular medicine · 2023
    Review
  5. Article
  6. An ATX-LPAiScience · 2021
    Article
  7. Lysolipids in Vascular Development, Biology, and Disease.Arteriosclerosis, thrombosis, and vascular biology · 2021
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Emerging structural biology of lipid G protein-coupled receptors.Protein science : a publication of the Protein Society · 2019
    Review
  14. Bioactive lysolipids in cancer and angiogenesis.Pharmacology & therapeutics · 2019
    Review
  15. Article
  16. Regulation of Lysophosphatidic Acid Metabolism and Signaling by Lipoproteins.Arteriosclerosis, thrombosis, and vascular biology · 2016
    Article
  17. 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

5 authors at 3 institutions in 1 country.

Hiroshi YukiuraGraduate School of Pharmaceutical Sciences, Tohoku University, 6-3, Aoba, Aramaki, Aoba-ku, Sendai 980-8578, Japan.
Kuniyuki KanoGraduate School of Pharmaceutical Sciences, Tohoku University, 6-3, Aoba, Aramaki, Aoba-ku, Sendai 980-8578, Japan.
Ryoji KiseGraduate School of Pharmaceutical Sciences, Tohoku University, 6-3, Aoba, Aramaki, Aoba-ku, Sendai 980-8578, Japan.
Asuka InoueGraduate School of Pharmaceutical Sciences, Tohoku University, 6-3, Aoba, Aramaki, Aoba-ku, Sendai 980-8578, Japan PRESTO, Japan Science and Technology Agency, Chiyoda-ku, Tokyo 100-0004, Japan.
Junken AokiGraduate School of Pharmaceutical Sciences, Tohoku University, 6-3, Aoba, Aramaki, Aoba-ku, Sendai 980-8578, Japan Japan Agency for Medical Research and Development, Core Research for Evolutional Science and Technology (AMED-CREST), Chiyoda-ku, Tokyo 100-0004, Japan jaoki@m.tohoku.ac.jp.
Tohoku University · JPJapan Agency for Medical Research and Development · JPJapan Science and Technology Agency · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lysophosphatidic acid (LPA) is emerging as an angiogenic factor, because knockdown of the enzyme that produces it (autotaxin, also known as ENPP2) and its receptors cause severe developmental vascular defects in both mice and fish. In addition, overexpression of autotaxin in mice causes similar vascular defects, indicating that the extracellular amount of LPA must be tightly regulated. Here, we focused on an LPA-degrading enzyme, lipid phosphate phosphatase 3 (LPP3, also known as PPAP2B), and showed that LPP3 was localized in specific cell-cell contact sites of endothelial cells and suppresses LPA signalling through the LPA6 receptor (also known as LPAR6). In HEK293 cells, overexpression of LPP3 dramatically suppressed activation of LPA6. In human umbilical vein endothelial cells (HUVECs), LPA induced actin stress fibre formation through LPA6, which was substantially upregulated by LPP3 knockdown. LPP3 was localized to cell-cell contact sites and was missing in non-contact sites to which LPA-induced actin stress fibre formation mediated by LPA6 was restricted. Interestingly, the expression of LPP3 in HUVECs was dramatically increased after forskolin treatment in a process involving Notch signalling. These results indicate that LPP3 regulates and localizes LPA signalling in endothelial cells, thereby stabilizing vessels through Notch signalling for proper vasculature.

Indexed as

AnimalsCell LineColforsinHumansHuman Umbilical Vein Endothelial CellsLysophospholipidsMiceMice, KnockoutPhosphatidate PhosphataseReceptors, NotchReverse Transcriptase Polymerase Chain ReactionColforsinlysophosphatidic acidLysophospholipidsPhosphatidate PhosphatasePLPP3 protein, humanReceptors, NotchEndothelial cellLPA receptorLPP3Lysophosphatidic acid

Identifiers

PMID26345369
PMCPMC4657331
OpenAlexW2132734436

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.