ArticleFrontiers in chemistry2021
Large-Scale Analysis of Apolipoprotein CIII Glycosylation by Ultrahigh Resolution Mass Spectrometry.
Article in Frontiers in chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 16 citations in OpenAlex.
- A genome-wide association study in 10,000 individuals links plasma N-glycome to liver disease and anti-inflammatory proteins.Nature communications · 2025Article
- ApoC-III proteoforms are associated with better lipid, inflammatory, and glucose profiles independent of total apoC-III.Cardiovascular diabetology · 2024Article
- Apolipoprotein-CIII O-Glycosylation Is Associated with Micro- and Macrovascular Complications of Type 2 Diabetes.International journal of molecular sciences · 2024Article
- Orbitrap Mass Spectrometry and High-Field Asymmetric Waveform Ion Mobility Spectrometry (FAIMS) Enable the in-Depth Analysis of Human Serum Proteoforms.Journal of proteome research · 2023Article
- Apolipoprotein-CIIIInternational journal of molecular sciences · 2023Article
- The Role of Clinical Glyco(proteo)mics in Precision Medicine.Molecular & cellular proteomics : MCP · 2023Article
- Comparative analysis of transferrin and IgG N-glycosylation in two human populations.Communications biology · 2023Article
- High-Throughput Glycomic Methods.Chemical reviews · 2022Review
- Review
- Developments and perspectives in high-throughput protein glycomics: enabling the analysis of thousands of samples.Glycobiology · 2022Article
- Mass Spectrometry of Transferrin and Apolipoprotein CIII from Dried Blood Spots for Congenital Disorders of Glycosylation.Mass spectrometry (Tokyo, Japan) · 2022Article
- Analysis of carbohydrates and glycoconjugates by matrix-assisted laser desorption/ionization mass spectrometry: An update for 2021-2022.Mass spectrometry reviewsReview
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Apolipoprotein-CIII (apo-CIII) is a glycoprotein involved in lipid metabolism and its levels are associated with cardiovascular disease risk. Apo-CIII sialylation is associated with improved plasma triglyceride levels and its glycosylation may have an effect on the clearance of triglyceride-rich lipoproteins by directing these particles to different metabolic pathways. Large-scale sample cohort studies are required to fully elucidate the role of apo-CIII glycosylation in lipid metabolism and associated cardiovascular disease. In this study, we revisited a high-throughput workflow for the analysis of intact apo-CIII by ultrahigh-resolution MALDI FT-ICR MS. The workflow includes a chemical oxidation step to reduce methionine oxidation heterogeneity and spectrum complexity. Sinapinic acid matrix was used to minimize the loss of sialic acids upon MALDI. MassyTools software was used to standardize and automate MS data processing and quality control. This method was applied on 771 plasma samples from individuals without diabetes allowing for an evaluation of the expression levels of apo-CIII glycoforms against a panel of lipid biomarkers demonstrating the validity of the method. Our study supports the hypothesis that triglyceride clearance may be regulated, or at least strongly influenced by apo-CIII sialylation. Interestingly, the association of apo-CIII glycoforms with triglyceride levels was found to be largely independent of body mass index. Due to its precision and throughput, the new workflow will allow studying the role of apo-CIII in the regulation of lipid metabolism in various disease settings.
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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.