Evidence map›Paper›PMID 25678897›Full record

ArticleClinical proteomics2015

Proteomic signatures of serum albumin-bound proteins from stroke patients with and without endovascular closure of PFO are significantly different and suggest a novel mechanism for cholesterol efflux.

Mary F Lopez, Bryan Krastins, David A Sarracino, Gregory Byram, Maryann S Vogelsang, Amol Prakash, Scott Peterman, Shadab Ahmad, Gouri Vadali, Wenjun Deng and 8 more

Open access · goldAbstract read
In one paragraph

Article in Clinical proteomics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

14 citing papers in PubMed, 40 citations in OpenAlex.

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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

18 authors at 2 institutions in 1 country.

Mary F LopezThermo Scientific BRIMS, 790 Memorial Dr, Cambridge, MA 02139 UK.
Bryan KrastinsThermo Scientific BRIMS, 790 Memorial Dr, Cambridge, MA 02139 UK.
David A SarracinoThermo Scientific BRIMS, 790 Memorial Dr, Cambridge, MA 02139 UK.
Gregory ByramThermo Scientific BRIMS, 790 Memorial Dr, Cambridge, MA 02139 UK.
Maryann S VogelsangThermo Scientific BRIMS, 790 Memorial Dr, Cambridge, MA 02139 UK.
Amol PrakashThermo Scientific BRIMS, 790 Memorial Dr, Cambridge, MA 02139 UK.
Scott PetermanThermo Scientific BRIMS, 790 Memorial Dr, Cambridge, MA 02139 UK.
Shadab AhmadThermo Scientific BRIMS, 790 Memorial Dr, Cambridge, MA 02139 UK.
Gouri VadaliThermo Scientific BRIMS, 790 Memorial Dr, Cambridge, MA 02139 UK.
Wenjun DengClinical Proteomics Research Center and Cardio-Neurology Clinic, Department of Neurology, Massachusetts General Hospital, Harvard Medical School, Boston, MA USA.
Ignacio InglessisClinical Proteomics Research Center and Cardio-Neurology Clinic, Department of Neurology, Massachusetts General Hospital, Harvard Medical School, Boston, MA USA.
Tom WickhamClinical Proteomics Research Center and Cardio-Neurology Clinic, Department of Neurology, Massachusetts General Hospital, Harvard Medical School, Boston, MA USA.
Kathleen FeeneyClinical Proteomics Research Center and Cardio-Neurology Clinic, Department of Neurology, Massachusetts General Hospital, Harvard Medical School, Boston, MA USA.
G William DecClinical Proteomics Research Center and Cardio-Neurology Clinic, Department of Neurology, Massachusetts General Hospital, Harvard Medical School, Boston, MA USA.
Igor PalaciosClinical Proteomics Research Center and Cardio-Neurology Clinic, Department of Neurology, Massachusetts General Hospital, Harvard Medical School, Boston, MA USA.
Ferdinando S BuonannoClinical Proteomics Research Center and Cardio-Neurology Clinic, Department of Neurology, Massachusetts General Hospital, Harvard Medical School, Boston, MA USA.
Eng H LoClinical Proteomics Research Center and Cardio-Neurology Clinic, Department of Neurology, Massachusetts General Hospital, Harvard Medical School, Boston, MA USA.
MingMing NingClinical Proteomics Research Center and Cardio-Neurology Clinic, Department of Neurology, Massachusetts General Hospital, Harvard Medical School, Boston, MA USA.
Massachusetts General Hospital · USHarvard University · US

Funding

Proteomic Profiling of Patent Foramen Ovale Related Neurovascular InjuryR01NS067139 · NINDS · MASSACHUSETTS GENERAL HOSPITAL · PI NING, MINGMING · 2010 to 2023
$3.7M
Thrombolysis Profiles in tPA ResponseR01NS093415 · NINDS · MASSACHUSETTS GENERAL HOSPITAL · PI LO, ENG H., NING, MINGMING · 2015 to 2019
$1.9M
NINDS NIH HHS R01 NS067139NINDS NIH HHS R01 NS093415
6 · The paper itself

Abstract

backgroundThe anatomy of PFO suggests that it can allow thrombi and potentially harmful circulatory factors to travel directly from the venous to the arterial circulation - altering circulatory phenotype. Our previous publication using high-resolution LC-MS/MS to profile protein and peptide expression patterns in plasma showed that albumin was relatively increased in donor samples from PFO-related than other types of ischemic strokes. Since albumin binds a host of molecules and acts as a carrier for lipoproteins, small molecules and drugs, we decided to investigate the albumin-bound proteins (in a similar sample cohort) in an effort to unravel biological changes and potentially discover biomarkers related to PFO-related stroke and PFO endovascular closure.

methodsThe method used in this study combined albumin immuno-enrichment with high resolution LC-MS in order to specifically capture and quantify the albumin-bound proteins. Subsequently, we measured cholesterol and HDL in a larger, separate cohort of PFO stroke patients, pre and post closure.

resultsThe results demonstrated that a number of proteins were specifically associated with albumin in samples with and without endovascular closure of the PFO, and that the protein profiles were very different. Eight proteins, typically associated with HDL were common to both sample sets and quantitatively differently abundant. Pathway analysis of the MS results suggested that enhanced cholesterol efflux and reduced lipid oxidation were associated with PFO closure. Measurement of total cholesterol and HDL in a larger cohort of PFO closure samples using a colorimetric assay was consistent with the proteomic predictions.

conclusionsThe collective data presented in this study demonstrate that analysis of albumin-bound proteins could provide a valuable tool for biomarker discovery on the effects of PFO endovascular closure. In addition, the results suggest that PFO endovascular closure can potentially have effects on HDL, cholesterol and albumin-bound ApoA-I abundance, therefore possibly providing benefits in cardioprotective functions.

Indexed as

AlbuminBiomarkerCerebrovascular diseaseDiscoveryIschemic strokeMass spectrometryPatent foramen ovalePFOProteomicsStroke

Identifiers

PMID25678897
PMCPMC4305391
OpenAlexW2153807501

What OpenQuestion holds

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LicenceCC BY
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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.