Evidence map›Paper›PMID 18190928›Full record

ArticleJournal of molecular biology2008

Mild oxidation promotes and advanced oxidation impairs remodeling of human high-density lipoprotein in vitro.

Xuan Gao, Shobini Jayaraman, Olga Gursky

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.3field-weighted citation impact, top 23% 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

17 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Article
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  4. Effects of triacylglycerol on the structural remodeling of human plasma very low- and low-density lipoproteins.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2019
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  7. Review
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  12. High density lipoproteins-based therapies for cardiovascular disease.Journal of cardiovascular disease research · 2010
    Article
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  14. Article
  15. 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

3 authors at 1 institution in 1 country.

Xuan GaoDepartment of Physiology and Biophysics, W329, Boston University School of Medicine, 715 Albany Street, Boston, MA 02118, USA.
Shobini Jayaraman
Olga Gursky
Boston University · US

Funding

STRUCTURE AND INTERACTIONS OF COMPLEX POLAR LIPIDSP01HL026335 · NHLBI · BOSTON UNIVERSITY MEDICAL CAMPUS · PI CARRAWAY, MARGARETHA · 1985 to 2010
$23.1M
Structural Thermodynamics of Human Apolipoprotein C-1R01GM067260 · NIGMS · BOSTON UNIVERSITY MEDICAL CAMPUS · PI GURSKY, OLGA · 2003 to 2024
$7.4M
NHLBI NIH HHS HL026355NHLBI NIH HHS P01 HL026335NIGMS NIH HHS GM067260NIGMS NIH HHS R01 GM067260
6 · The paper itself

Abstract

High-density lipoproteins (HDLs) prevent atherosclerosis by removing cholesterol from macrophages and by exerting antioxidant and anti-inflammatory effects. Oxidation is thought to impair HDL functions, yet certain oxidative modifications may be advantageous; thus, mild oxidation reportedly enhances cell cholesterol uptake by HDL whereas extensive oxidation impairs it. To elucidate the underlying energetic and structural basis, we analyzed the effects of copper and hypochlorite (which preferentially oxidize lipids and proteins, respectively) on thermal stability of plasma spherical HDL. Circular dichroism, light scattering, calorimetry, gel electrophoresis, and electron microscopy showed that mild oxidation destabilizes HDL and accelerates protein dissociation and lipoprotein fusion, while extensive oxidation inhibits these reactions; this inhibition correlates with massive protein cross-linking and with lipolysis. We propose that mild oxidation lowers kinetic barriers for HDL remodeling due to diminished apolipoprotein affinity for lipids resulting from oxidation of methionine and aromatic residues in apolipoproteins A-I and A-II followed by protein cross-linking into dimers and/or trimers. In contrast, advanced oxidation inhibits protein dissociation and HDL fusion due to lipid redistribution from core to surface upon lipolysis and to massive protein cross-linking. Our results help reconcile the apparent controversy in the studies of oxidized HDL and suggest that mild oxidation may benefit HDL functions.

Indexed as

CopperCross-Linking ReagentsElectrophoresis, Polyacrylamide GelHumansKineticsLipid MetabolismLipoproteins, HDLOxidation-ReductionProtein ConformationProtein FoldingSolutionsThermodynamicsTime FactorsTransition TemperatureCopperCross-Linking ReagentsLipoproteins, HDLSolutions

Identifiers

PMID18190928
PMCPMC2276461
OpenAlexW2041701525

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.