Evidence map›Paper›PMID 28522939›Full record

ArticleClinical proteomics2017

Identification of protein targets in cerebral endothelial cells for brain arteriovenous malformation (AVMs) molecular therapies.

Margaret Simonian, Rachel R Ogorzalek Loo, Nalaka Rannulu, Joseph A Loo, Mark P Molloy, Marcus A Stoodley

Open access · goldAbstract read
In one paragraph

Article in Clinical proteomics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.5field-weighted citation impact, top 32% 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

5 citing papers in PubMed, 8 citations in OpenAlex.

  1. Review
  2. Proteogenomics for pediatric brain cancer.Biocell : official journal of the Sociedades Latinoamericanas de Microscopia Electronica ... et. al · 2021
    Article
  3. Article
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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

6 authors at 2 institutions in 2 countries.

Margaret SimonianDepartment of Clinical Medicine, Faculty of Medicine and Health Sciences, Macquarie University, North Ryde, NSW 2109 Australia.
Rachel R Ogorzalek LooDavid Geffen School of Medicine, Department of Biological Chemistry, University of California Los Angeles (UCLA), 611 Charles E. Young Drive East, Los Angeles, CA 90095 USA.
Nalaka RannuluDavid Geffen School of Medicine, Department of Biological Chemistry, University of California Los Angeles (UCLA), 611 Charles E. Young Drive East, Los Angeles, CA 90095 USA.
Joseph A LooDavid Geffen School of Medicine, Department of Biological Chemistry, University of California Los Angeles (UCLA), 611 Charles E. Young Drive East, Los Angeles, CA 90095 USA.
Mark P MolloyAustralian Proteome Analysis Facility (APAF), Department of Chemistry and Bimolecular Sciences, Macquarie University, North Ryde, NSW 2109 Australia.
Marcus A StoodleyDepartment of Clinical Medicine, Faculty of Medicine and Health Sciences, Macquarie University, North Ryde, NSW 2109 Australia.
Macquarie University · AUUniversity of California, Los Angeles · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundTo develop a new molecular targeted treatment for brain (AVMs), identification of membrane proteins that are localised on the AVM endothelium is crucial. Current treatment methods are surgery and radiosurgery. However, complete occlusion post radiosurgery are achieved within 3 years, while patient remain at risk of haemorrhage. This study aims to identify potential protein targets in AVM endothelial cells that discriminate these vessels from normal vessels; these proteins targets will be investigated for the molecular therapy of brain AVMs to promote rapid thrombosis after radiosurgery.

methodsWe employed in vitro biotinylation that we developed, and mass spectrometry to detect cell surface-exposed proteins in cultures of murine cerebral endothelial cells (bEnd.3). Two forms of mass spectrometry were applied (iTRAQ-MS and MS

resultsThe proteomics data revealed several differentially expressed membrane proteins between irradiated and non-irradiated cells at specific time points, e.g. PECAM-1, cadherin-5, PDI, EPCR and integrins. Immunocytochemistry data confirmed the expression of these proteins.

conclusionCell surface protein biotinylation and proteomics analysis successfully identified membrane proteins from murine brain endothelial cells in response to irradiation. This work suggests potential target protein molecules for evaluation in animal models of brain-AVM.

Indexed as

Arteriovenous malformationsBiotinylationEndothelial cellsIrradiationMembrane proteins

Identifiers

PMID28522939
PMCPMC5434588
OpenAlexW2616049160

What OpenQuestion holds

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LicenceCC BY
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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.