Evidence map›Paper›PMID 22219194›Full record

ArticleThe Journal of biological chemistry2012

Myeloperoxidase targets apolipoprotein A-I, the major high density lipoprotein protein, for site-specific oxidation in human atherosclerotic lesions.

Baohai Shao, Subramaniam Pennathur, Jay W Heinecke

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
8.0field-weighted citation impact, top 2% 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

90 citing papers in PubMed, 166 citations in OpenAlex.

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30 more citing papers are in PubMed but not listed here.

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

3 authors at 2 institutions in 1 country.

Baohai ShaoDepartment of Medicine and Diabetes and Obesity Center of Excellence, University of Washington, Seattle, Washington 98195, USA. bhshao@u.washington.edu
Subramaniam Pennathur
Jay W Heinecke
University of Washington · USUniversity of Michigan–Ann Arbor · US

Funding

Vector and Transgenic Mouse CoreP30DK017047 · NIDDK · UNIVERSITY OF WASHINGTON · PI Julie Mathieu · 1986 to 2026
$41.4M
Regional Pilot And Feasibility Study Grants ProgramP30DK020572 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI DAVID P OLSON · 2013 to 2026
$24.3M
Pilot and Feasibility (P and F) ProgramP30DK089503 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RANDY J SEELEY · 2010 to 2026
$20.3M
Structure of apolipoprotein A-I on defined states of HDLR01HL077268 · NHLBI · CHILDREN'S HOSPITAL &RES CTR AT OAKLAND · PI ODA, MICHAEL NOBUAKI · 2004 to 2010
$2.0M
Molecular Mechanisms for Dysfunctional High Density Lipoprotein (HDL)R01HL086798 · NHLBI · UNIVERSITY OF WASHINGTON · PI HEINECKE, JAY W · 2007 to 2011
$1.9M
Atherogenic Effects of Oxidized High Density LipoproteinsR01HL085437 · NHLBI · UNIVERSITY OF WASHINGTON · PI HEINECKE, JAY W · 2006 to 2010
$1.9M
Anti-inflammatory properties of high-density lipoproteinR00HL091055 · NHLBI · UNIVERSITY OF WASHINGTON · PI SHAO, BAOHAI · 2010 to 2012
$747k
NHLBI NIH HHS R00 HL091055NHLBI NIH HHS R00HL091055NHLBI NIH HHS R01 HL077268NHLBI NIH HHS R01HL077268NHLBI NIH HHS R01 HL085437NHLBI NIH HHS R01HL085437NHLBI NIH HHS R01 HL086798NHLBI NIH HHS R01HL086798NIDDK NIH HHS DK089503NIDDK NIH HHS P30 DK017047NIDDK NIH HHS P30DK017047NIDDK NIH HHS P30 DK020572NIDDK NIH HHS P30 DK089503
6 · The paper itself

Abstract

Oxidative damage by myeloperoxidase (MPO) has been proposed to deprive HDL of its cardioprotective effects. In vitro studies reveal that MPO chlorinates and nitrates specific tyrosine residues of apoA-I, the major HDL protein. After Tyr-192 is chlorinated, apoA-I is less able to promote cholesterol efflux by the ABCA1 pathway. To investigate the potential role of this pathway in vivo, we used tandem mass spectrometry with selected reaction monitoring to quantify the regiospecific oxidation of apoA-I. This approach demonstrated that Tyr-192 is the major chlorination site in apoA-I in both plasma and lesion HDL of humans. We also found that Tyr-192 is the major nitration site in apoA-I of circulating HDL but that Tyr-18 is the major site in lesion HDL. Levels of 3-nitrotyrosine strongly correlated with levels of 3-chlorotyrosine in lesion HDL, and Tyr-18 of apoA-I was the major nitration site in HDL exposed to MPO in vitro, suggesting that MPO is the major pathway for chlorination and nitration of HDL in human atherosclerotic tissue. These observations may have implications for treating cardiovascular disease, because recombinant apoA-I is under investigation as a therapeutic agent and mutant forms of apoA-I that resist oxidation might be more cardioprotective than the native form.

Indexed as

Apolipoprotein A-IAtherosclerosisHalogenationHumansHypochlorous AcidLipoproteins, HDLNitrogenOxidation-ReductionOxidative StressPeroxidaseProtein Processing, Post-TranslationalTyrosine3-chlorotyrosine3-nitrotyrosineApolipoprotein A-IHypochlorous AcidLipoproteins, HDLNitrogenPeroxidaseTyrosine

Identifiers

PMID22219194
PMCPMC3307260
OpenAlexW2031748708

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.