Evidence map›Paper›PMID 19502413›Full record

ArticleDiabetes2009

ApoCIII-enriched LDL in type 2 diabetes displays altered lipid composition, increased susceptibility for sphingomyelinase, and increased binding to biglycan.

Anne Hiukka, Marcus Ståhlman, Camilla Pettersson, Malin Levin, Martin Adiels, Susanne Teneberg, Eeva S Leinonen, Lillemor Mattsson Hultén, Olov Wiklund, Matej Oresic and 4 more

Open access · bronzeAbstract read
In one paragraph

Article in Diabetes, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

65 citing papers in PubMed, 140 citations in OpenAlex.

  1. Trial
  2. Trial
  3. Trial
  4. Trial
  5. Linking Lipidomics to Vulnerable Coronary Plaques: A PROSPECT II Substudy.Arteriosclerosis, thrombosis, and vascular biology · 2026
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Review
  12. Oxidised Apolipoprotein Peptidome Characterises Metabolic Dysfunction-Associated Steatotic Liver Disease.Liver international : official journal of the International Association for the Study of the Liver · 2025
    Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Apolipoprotein C3: form begets function.Journal of lipid research · 2024
    Review

5 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

14 authors at 4 institutions in 2 countries.

Anne HiukkaDepartment of Medicine, Helsinki University Central Hospital and Biomedicum, Helsinki, Finland.
Marcus Ståhlman
Camilla Pettersson
Malin Levin
Martin Adiels
Susanne Teneberg
Eeva S Leinonen
Lillemor Mattsson Hultén
Olov Wiklund
Matej Oresic
Sven-Olof Olofsson
Marja-Riitta Taskinen
Kim Ekroos
Jan Borén
University of Gothenburg · SEHelsinki University Hospital · FIVTT Technical Research Centre of Finland · FIZora Biosciences (Finland) · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

objectiveApolipoprotein CIII (apoCIII) is an independent risk factor for cardiovascular disease, but the molecular mechanisms involved are poorly understood. We investigated potential proatherogenic properties of apoCIII-containing LDL from hypertriglyceridemic patients with type 2 diabetes. RESEARCH DESIGN AND

methodsLDL was isolated from control subjects, subjects with type 2 diabetes, and apoB transgenic mice. LDL-biglycan binding was analyzed with a solid-phase assay using immunoplates coated with biglycan. Lipid composition was analyzed with mass spectrometry. Hydrolysis of LDL by sphingomyelinase was analyzed after labeling plasma LDL with [(3)H]sphingomyelin. ApoCIII isoforms were quantified after isoelectric focusing. Human aortic endothelial cells were incubated with desialylated apoCIII or with LDL enriched with specific apoCIII isoforms.

resultsWe showed that enriching LDL with apoCIII only induced a small increase in LDL-proteoglycan binding, and this effect was dependent on a functional site A in apoB100. Our findings indicated that intrinsic characteristics of the diabetic LDL other than apoCIII are responsible for further increased proteoglycan binding of diabetic LDL with high-endogenous apoCIII, and we showed alterations in the lipid composition of diabetic LDL with high apoCIII. We also demonstrated that high apoCIII increased susceptibility of LDL to hydrolysis and aggregation by sphingomyelinases. In addition, we demonstrated that sialylation of apoCIII increased with increasing apoCIII content and that sialylation of apoCIII was essential for its proinflammatory properties.

conclusionsWe have demonstrated a number of features of apoCIII-containing LDL from hypertriglyceridemic patients with type 2 diabetes that could explain the proatherogenic role of apoCIII.

Indexed as

AgedAnimalsApolipoprotein C-IIIApolipoproteins BBiglycanCells, CulturedDiabetes Mellitus, Type 2Endothelial CellsExtracellular Matrix ProteinsFemaleHumansHydrolysisHypertriglyceridemiaLipoproteins, LDLMaleMiceApolipoprotein C-IIIApolipoproteins BBGN protein, humanBgn protein, mouseBiglycanExtracellular Matrix ProteinsLipoproteins, LDLProteoglycansSphingomyelin Phosphodiesterase

Identifiers

PMID19502413
PMCPMC2731525
OpenAlexW2133896415

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.