ArticleJournal of lipid research2016
Multiplexed peptide analysis for kinetic measurements of major human apolipoproteins by LC/MS/MS.
Article in Journal of lipid research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Associations between physical activity levels and ATPase inhibitory factor 1 concentrations in older adults.Journal of sport and health science · 2024Article
- Understanding HDL Metabolism and Biology Through In Vivo Tracer Kinetics.Arteriosclerosis, thrombosis, and vascular biology · 2024Review
- Characterization of lipoproteins and associated lipidome in very preterm infants: a pilot study.Pediatric research · 2023Article
- Apolipoprotein E content of VLDL limits LPL-mediated triglyceride hydrolysis.Journal of lipid research · 2022Article
- Characterization of Affitin proteolytic digestion in biorelevant media and improvement of their stabilities via protein engineering.Scientific reports · 2020Article
- A high-throughput mass spectrometry-based assay for large-scale profiling of circulating human apolipoproteins.Journal of lipid research · 2020Article
- Kinetics of plasma apolipoprotein E isoforms by LC-MS/MS: a pilot study.Journal of lipid research · 2018Article
- Unbiased and targeted mass spectrometry for the HDL proteome.Current opinion in lipidology · 2017Review
- Automation of PRM-dependent D3-Leu tracer enrichment in HDL to study the metabolism of apoA-I, LCAT and other apolipoproteins.Proteomics · 2017Article
- IRES-dependent translation of the long non coding RNA meloe in melanoma cells produces the most immunogenic MELOE antigens.Oncotarget · 2016Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A multiplexed assay was developed by MS to analyze, in a single run, six major human Apos involved in lipoprotein metabolism: ApoA-I, ApoA-II, ApoB100, ApoC-II, ApoC-III, and ApoE. This method was validated in vivo in six subjects who received a 14 h constant infusion of [5,5,5-(2)H3]L-leucine at 10 μM/kg/h. Plasma lipoprotein fractions were isolated from collected blood samples and were digested with trypsin. Proteotypic peptides were subsequently analyzed by LC/MS/MS. Enrichment measurement data were compared with those obtained by the standard method using GC/MS. The required time to obtain the LC/MS/MS data was less than that needed for GC/MS. The enrichments from both methods were correlated for ApoA-I (r = 0.994; P < 0.0001) and ApoB100 (r = 0.999; P < 0.0001), and the Bland-Altman plot confirmed the similarity of the two methods. Intra- and inter-assay variability calculated for the six Apos of interest did not exceed 10.7 and 12.5%, respectively, and kinetic parameters were similar and/or in agreement with previously reported data. Therefore, LC/MS/MS can be considered as a useful tool for human Apo kinetic studies using stable isotopes.
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