Evidence map›Paper›PMID 26478188›Full record

ArticleScientific reports2015

A Designed Angiopoietin-1 Variant, Dimeric CMP-Ang1 Activates Tie2 and Stimulates Angiogenesis and Vascular Stabilization in N-glycan Dependent Manner.

Nuri Oh, Kangsan Kim, Soo Jin Kim, Intae Park, Jung-Eun Lee, Young Suk Seo, Hyun Joo An, Ho Min Kim, Gou Young Koh

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

16 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
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  3. Review
  4. Article
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  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Targeting the Tie2-αBMC biology · 2018
    Article
  13. Therapeutic targeting of the angiopoietin-TIE pathway.Nature reviews. Drug discovery · 2017
    Review
  14. Structural basis of Tie2 activation and Tie2/Tie1 heterodimerization.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  15. Review
  16. 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

9 authors at 2 institutions in 1 country.

Nuri OhGraduate School of Medical Science and Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, 305-701, Korea.
Kangsan KimGraduate School of Medical Science and Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, 305-701, Korea.
Soo Jin KimGraduate School of Medical Science and Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, 305-701, Korea.
Intae ParkGraduate School of Medical Science and Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, 305-701, Korea.
Jung-Eun LeeGraduate School of Medical Science and Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, 305-701, Korea.
Young Suk SeoGraduate School of Analytical Science and Technology, Chungnam National University, Daejeon, 305-764, Korea.
Hyun Joo AnGraduate School of Analytical Science and Technology, Chungnam National University, Daejeon, 305-764, Korea.
Ho Min KimGraduate School of Medical Science and Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, 305-701, Korea.
Gou Young KohGraduate School of Medical Science and Engineering, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, 305-701, Korea.
Korea Advanced Institute of Science and Technology · KRChungnam National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Angiopoietin-1 (Ang1), a potential growth factor for therapeutic angiogenesis and vascular stabilization, is known to specifically cluster and activate Tie2 in high oligomeric forms, which is a unique and essential process in this ligand-receptor interaction. However, highly oligomeric native Ang1 and Ang1 variants are difficult to produce, purify, and store in a stable and active form. To overcome these limitations, we developed a simple and active dimeric CMP-Ang1 by replacing the N-terminal of native Ang1 with the coiled-coil domain of cartilage matrix protein (CMP) bearing mutations in its cysteine residues. This dimeric CMP-Ang1 effectively increased the migration, survival, and tube formation of endothelial cells via Tie2 activation. Furthermore, dimeric CMP-Ang1 induced angiogenesis and suppressed vascular leakage in vivo. Despite its dimeric structure, the potencies of such Tie2-activation-induced effects were comparable to those of a previously engineered protein, COMP-Ang1. We also revealed that these effects of dimeric CMP-Ang1 were affected by specified N-glycosylation in its fibrinogen-like domain. Taken together, our results indicate that dimeric CMP-Ang1 is capable of activating Tie2 and stimulating angiogenesis in N-glycan dependent manner.

Indexed as

Angiopoietin-1Matrilin ProteinsAnimalsCapillary PermeabilityCell LineEndothelial CellsGlycosylationHumansMiceModels, MolecularNeovascularization, PhysiologicPolysaccharidesProtein ConformationProtein MultimerizationProto-Oncogene Proteins c-aktReceptor, TIE-2Angiopoietin-1Matrilin ProteinsPolysaccharidesProto-Oncogene Proteins c-aktReceptor, TIE-2Recombinant Fusion Proteins

Identifiers

PMID26478188
PMCPMC4609988
OpenAlexW1776918976

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

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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.