Evidence map›Paper›PMID 39085140›Full record

ArticleJournal of atherosclerosis and thrombosis2025

Proteomic Analysis of Human Chylomicron Remnants Isolated by Apolipoprotein B-48 Immunoprecipitation.

Daisaku Masuda, Takeshi Okada, Masami Sairyou, Kazuaki Takafuji, Tohru Ohama, Masahiro Koseki, Makoto Nishida, Yasushi Sakata, Shizuya Yamashita

Abstract read
In one paragraph

Article in Journal of atherosclerosis and thrombosis, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Article
  2. Review
  3. Biomolecules · 2025
    Article
  4. 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.

Daisaku MasudaDepartment of Cardiovascular Medicine, Osaka University Graduate School of Medicine.
Takeshi OkadaDepartment of Cardiovascular Medicine, Osaka University Graduate School of Medicine.
Masami SairyouDepartment of Cardiovascular Medicine, Osaka University Graduate School of Medicine.
Kazuaki TakafujiCenter of Medical Innovation and Translational Research, Osaka University Graduate School of Medicine.
Tohru OhamaDepartment of Cardiovascular Medicine, Osaka University Graduate School of Medicine.
Masahiro KosekiDepartment of Cardiovascular Medicine, Osaka University Graduate School of Medicine.
Makoto NishidaDepartment of Cardiovascular Medicine, Osaka University Graduate School of Medicine.
Yasushi SakataDepartment of Cardiovascular Medicine, Osaka University Graduate School of Medicine.
Shizuya YamashitaDepartment of Cardiovascular Medicine, Osaka University Graduate School of Medicine.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

aimPostprandial hypertriglyceridemia (PHTG) is an independent risk factor for coronary heart diseases. PHTG exhibits accumulation of apoB-48 containing chylomicron remnants (CM-Rs) and apoB-100 containing VLDL remnants (VLDL-Rs), which are both known to be atherogenic. However, unlike VLDL-Rs, structural and functional characterization of CM-Rs remains to be elucidated due to challenges in separating CM-Rs from VLDL-Rs. Recently, we successfully isolated CM-Rs and VLDL-Rs utilizing anti-apoB-48 or apoB-100 specific antibodies. This study aimed to characterize the proteome of CM-Rs along with that of VLDL-Rs.

methodsEight healthy subjects were enrolled. Venous blood was drawn 3 hours after high-fat-containing meals. We isolated CM-Rs and VLDL-Rs from sera through combination of ultracentrifugation and immunoprecipitation using apoB-48 or apoB-100 specific antibodies, followed by shotgun proteomic analysis.

resultsWe identified 42 CM-Rs or VLDL-Rs-associated proteins, including 11 potential newly identified proteins such as platelet basic protein (PPBP) and platelet factor 4, which are chemokines secreted from platelets. ApoA-I, apoA-IV, and clusterin, which are also known as HDL-associated proteins, were significantly more abundant in CM-Rs. Interestingly, apoC-I, which reduces the activity of lipoprotein lipase and eventually inhibits catabolism of remnant proteins, was also more abundant in CM-Rs. Moreover, we identified proteins involved in complement regulation such as complement C3 and vitronectin, and those involved in acute-phase response such as PPBP, serum amyloid A protein 2, and protein S100-A8, in both CM-Rs and VLDL-Rs.

conclusionsWe have firstly characterized the proteome of CM-Rs. These findings may provide an explanation for the atherogenic properties of CM-Rs.

Indexed as

Apolipoprotein B-48Chylomicron RemnantsImmunoprecipitationProteomicsAdultAnimalsAtherosclerosisFemaleHumansLipoproteins, VLDLMaleMice, Inbred C57BLApolipoprotein B-48Chylomicron RemnantsLipoproteins, VLDLAtherosclerosisChylomicron remnantsInflammationPostprandial hypertriglyceridemiaProteomicsRemnant lipoproteinsVLDL remnants

Identifiers

PMID39085140
PMCPMC11802255

What Socratic holds

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Registered trials

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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 Socratic graph.