Evidence map›Paper›PMID 18302337›Full record

ArticleBiochemistry2008

Effects of protein oxidation on the structure and stability of model discoidal high-density lipoproteins.

Shobini Jayaraman, Donald L Gantz, Olga Gursky

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.4field-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

16 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. High Density Lipoprotein and it's Dysfunction.The open biochemistry journal · 2012
    Article
  11. Article
  12. Article
  13. Article
  14. Maturation of high-density lipoproteins.Journal of the Royal Society, Interface · 2009
    Article
  15. HDL: bridging past and present with a look at the future.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2008
    Review
  16. 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

3 authors at 1 institution in 1 country.

Shobini JayaramanDepartment of Physiology and Biophysics, Boston University School of Medicine, Boston, Massachusetts 02118, USA. shobini@bu.edu
Donald L Gantz
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 HL 026355NHLBI NIH HHS P01 HL026335NIGMS NIH HHS R01 GM 067260NIGMS NIH HHS R01 GM067260
6 · The paper itself

Abstract

High-density lipoproteins (HDLs) prevent atherosclerosis by removing cholesterol from macrophages and by providing antioxidants for low-density lipoproteins. Oxidation of HDLs affects their functions via the complex mechanisms that involve multiple protein and lipid modifications. To differentiate between the roles of oxidative modifications in HDL proteins and lipids, we analyzed the effects of selective protein oxidation by hypochlorite (HOCl) on the structure, stability, and remodeling of discoidal HDLs reconstituted from human apolipoproteins (A-I, A-II, or C-I) and phosphatidylcholines. Gel electrophoresis and electron microscopy revealed that, at ambient temperatures, protein oxidation in discoidal complexes promotes their remodeling into larger and smaller particles. Thermal denaturation monitored by far-UV circular dichroism and light scattering in melting and kinetic experiments shows that protein oxidation destabilizes discoidal lipoproteins and accelerates protein unfolding, dissociation, and lipoprotein fusion. This is likely due to the reduced affinity of the protein for lipid resulting from oxidation of Met and aromatic residues in the lipid-binding faces of amphipathic alpha-helices and to apolipoprotein cross-linking into dimers and trimers on the particle surface. We conclude that protein oxidation destabilizes HDL disk assembly and accelerates its remodeling and fusion. This result, which is not limited to model discoidal but also extends to plasma spherical HDL, helps explain the complex effects of oxidation on plasma lipoproteins.

Indexed as

Apolipoprotein A-IApolipoprotein A-IIApolipoprotein C-IDimyristoylphosphatidylcholineDrug StabilityElectrophoresis, Polyacrylamide GelHumansHypochlorous AcidLipoproteins, HDLMicroscopy, ElectronOxidantsOxidation-ReductionProtein DenaturationSpectrometry, FluorescenceApolipoprotein A-IApolipoprotein A-IIApolipoprotein C-IDimyristoylphosphatidylcholineHypochlorous AcidLipoproteins, HDLOxidants

Identifiers

PMID18302337
PMCPMC2823073
OpenAlexW2051238291

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.