Evidence map›Paper›PMID 24417605›Full record

ArticleJournal of proteome research2014

Glycomic analysis of high density lipoprotein shows a highly sialylated particle.

Jincui Huang, Hyeyoung Lee, Angela M Zivkovic, Jennifer T Smilowitz, Nancy Rivera, J Bruce German, Carlito B Lebrilla

Registry-linked trialOpen access · bronzeAbstract read
In one paragraph

Article in Journal of proteome research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT01817127 (Functional Deconstruction of Human Milk Oligosaccharides and Lipids), which is not on this map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.7field-weighted citation impact, top 15% 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.

NCT01817127 active not recruitingnot on this map

Functional Deconstruction of Human Milk Oligosaccharides and Lipids

TypeobservationalSponsorUniversity of California, DavisRan2009 to 2028Enrolled395ConditionsHealthy, Gestational Diabetes Mellitus, Type 2 Diabetes Mellitus
3 · Its place in the literature

Who cites it

20 citing papers in PubMed, 36 citations in OpenAlex.

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  14. iScience · 2021
    Article
  15. Article
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  20. Human plasma protein N-glycosylation.Glycoconjugate journal · 2016
    Review
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

7 authors at 1 institution in 1 country.

Jincui HuangDepartment of Chemistry, ‡Department of Food Science and Technology, and §Foods for Health Institute, University of California , Davis, California 95616, United States.
Hyeyoung Lee
Angela M Zivkovic
Jennifer T Smilowitz
Nancy Rivera
J Bruce German
Carlito B Lebrilla
University of California, Davis · US

Funding

The incorporation of human milk oligosaccharides in brain glycoconjugatesR01GM049077 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI LEBRILLA, CARLITO B · 1999 to 2024
$6.3M
Mechanism of Activation of Probiotic Bifidobacteria by Prebiotic Milk GlycansR01AT007079 · NCCIH · UNIVERSITY OF CALIFORNIA AT DAVIS · PI GERMAN, BRUCE, LEBRILLA, CARLITO B · 2012 to 2016
$2.2M
Structures, Functions, & Genetic Diversity of Oligosaccharides in MilkR01HD061923 · NICHD · UNIVERSITY OF CALIFORNIA AT DAVIS · PI LEBRILLA, CARLITO B · 2009 to 2013
$1.6M
Glycomics Equipment: NanoLC CHIP-QTOF Mass SpectrometerS10RR027639 · NCRR · UNIVERSITY OF CALIFORNIA AT DAVIS · PI LEBRILLA, CARLITO B · 2010 to 2010
$500k
NCCIH NIH HHS R01 AT007079NCRR NIH HHS S10 RR027639NICHD NIH HHS R01 HD061923NIGMS NIH HHS R01 GM049077NIGMS NIH HHS R01GM049077
6 · The paper itself

Abstract

Many of the functional proteins and lipids in high density lipoprotein (HDL) particles are potentially glycosylated, yet very little is known about the glycoconjugates of HDL. In this study, HDL was isolated from plasma by sequential micro-ultracentrifugation, followed by glycoprotein and glycolipid analysis. N-Glycans, glycopeptides, and gangliosides were extracted and purified followed by analysis with nano-HPLC Chip quadrupole time of flight mass spectrometry and MS/MS. HDL particles were found to be highly sialylated. Most of the N-glycans (∼90%) from HDL glycoproteins were sialylated with one or two neuraminic acids (Neu5Ac). The most abundant N-glycan was a biantennary complex type glycan with two sialic acids (Hexose5HexNAc4Neu5Ac2) and was found in multiple glycoproteins using site-specific glycosylation analysis. The observed O-glycans were all sialylated, and most contained a core 1 structure with two Neu5Acs, including those that were associated with apolipoprotein CIII (ApoC-III) and fetuin A. GM3 (monosialoganglioside, NeuAc2-3Gal1-4Glc-Cer) and GD3 (disialoganglioside, NeuAc2-8NeuAc2-3Gal1-4Glc-Cer) were the major gangliosides in HDL. A 60% GM3 and 40% GD3 distribution was observed. Both GM3 and GD3 were composed of heterogeneous ceramide lipid tails, including d18:1/16:0 and d18:1/23:0. This report describes for the first time a glycomic approach for analyzing HDL, highlighting that HDL are highly sialylated particles.

Indexed as

Amino Acid SequenceCarbohydratesChromatography, High Pressure LiquidGangliosidesLipoproteins, HDLMolecular Sequence DataN-Acetylneuraminic AcidTandem Mass SpectrometryCarbohydratesGangliosidesLipoproteins, HDLN-Acetylneuraminic Acid

Identifiers

PMID24417605
PMCPMC3975653
OpenAlexW2316416887

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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.