Evidence map›Paper›PMID 22589558›Full record

ArticleJournal of lipid research2012

Preservation of biological function despite oxidative modification of the apolipoprotein A-I mimetic peptide 4F.

C Roger White, Geeta Datta, Amanda K W Buck, Manjula Chaddha, Gautam Reddy, Landon Wilson, Mayakonda N Palgunachari, Mohammad Abbasi, G M Anantharamaiah

Open access · hybridAbstract read
In one paragraph

Article in Journal of lipid research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

9 citing papers in PubMed, 12 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Apolipoprotein A-I mimetics.Current opinion in lipidology · 2014
    Review
  9. 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 1 institution in 1 country.

C Roger WhiteDepartment of Medicine, University of Alabama at Birmingham, Birmingham, AL, USA. crwhite@uab.edu
Geeta Datta
Amanda K W Buck
Manjula Chaddha
Gautam Reddy
Landon Wilson
Mayakonda N Palgunachari
Mohammad Abbasi
G M Anantharamaiah
University of Alabama at Birmingham · US

Funding

SYNTHETIC PEPTIDE STUDIES OF THE AMPHIPATHIC HELIXP01HL034343 · NHLBI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI SEGREST, JERE P · 1985 to 2012
$18.8M
MECHANISMS OF HYPERTENSION AND CARDIOVASCULAR DISEASEST32HL007457 · NHLBI · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI Martin E Young · 1985 to 2026
$8.6M
HDL Modulation of monocyte function in endotoxemiaR01GM082952 · NIGMS · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI DATTA, GEETA, WHITE, C ROGER · 2008 to 2011
$1.3M
5500 Q-Trap Mass SpectrometerS10RR027822 · NCRR · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI BARNES, STEPHEN · 2010 to 2010
$469k
MICROMASS HYBRID QUADRUPOLE--TOF MASS SPECTROMETERS10RR013795 · NCRR · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI BARNES, STEPHEN · 1999 to 1999
–
NCRR NIH HHS S10 RR027822NCRR NIH HHS S10 RR-027822-01NCRR NIH HHS S10 RR-13795NHLBI NIH HHS P01 HL034343NHLBI NIH HHS T32 HL-007457NHLBI NIH HHS T32 HL007457NIGMS NIH HHS GM-082952NIGMS NIH HHS R01 GM082952PHS HHS H-L34343
6 · The paper itself

Abstract

Myeloperoxidase (MPO)-derived hypochlorous acid induces changes in HDL function via redox modifications at the level of apolipoprotein A-I (apoA-I). As 4F and apoA-I share structural and functional properties, we tested the hypothesis that 4F acts as a reactive substrate for hypochlorous acid (HOCl). 4F reduced the HOCl-mediated oxidation of the fluorescent substrate APF in a concentration-dependent manner (ED(50) ∼ 56 ± 3 μM). This reaction induced changes in the physical properties of 4F. Addition of HOCl to 4F at molar ratios ranging from 1:1 to 3:1 reduced 4F band intensity on SDS-PAGE gels and was accompanied by the formation of a higher molecular weight species. Chromatographic studies showed a reduction in 4F peak area with increasing HOCl and the formation of new products. Mass spectral analyses of collected fractions revealed oxidation of the sole tryptophan (Trp) residue in 4F. 4F was equally susceptible to oxidation in the lipid-free and lipid-bound states. To determine whether Trp oxidation influenced its apoA-I mimetic properties, we monitored effects of HOCl on 4F-mediated lipid binding and ABCA1-dependent cholesterol efflux. Neither property was altered by HOCl. These results suggest that 4F serves as a reactive substrate for HOCl, an antioxidant response that does not influence the lipid binding and cholesterol effluxing capacities of the peptide.

Indexed as

Amino Acid SequenceApolipoprotein A-IBiological TransportCell Line, TumorCholesterolHumansHypochlorous AcidMolecular Dynamics SimulationMolecular Sequence DataOxidation-ReductionPeptidesPeptidomimeticsProtein ConformationApolipoprotein A-ICholesterolHypochlorous AcidPeptidesPeptidomimetics

Identifiers

PMID22589558
PMCPMC3540838
OpenAlexW2150380468

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.