In vivo stable-isotope kinetic study suggests intracellular assembly of lipoprotein(a)

Frischmann, Michael E.; Ikewaki, Katsunori; Trenkwalder, Evi; Lamina, Claudia; Dieplinger, Benjamin; Soufi, Muhidien; Schweer, Horst; Schaefer, Juergen R.; König, Paul; Kronenberg, Florian; Dieplinger, Hans

doi:10.1016/j.atherosclerosis.2012.09.031

Cited by 58 publications

(42 citation statements)

References 42 publications

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“…The problem was overcome by using higher sample volumes (400 l) during the concentration step. As shown by the Bland-Altman analysis, the enrichments measured by LC/MS/MS in this study were identical to those measured with the conventional GC/MS method and were in the same range as those reported previously by others using similar stable isotope protocols and the GC/MS method for ApoA-I ( 15,26 ) and ApoB100 ( 20,27 ). Similar results have been also reported for ApoA-II ( 21,26 ), ApoE ( 19,20 ), and ApoC-III ( 20,28 ).…”

Section: Discussionsupporting

confidence: 88%

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Multiplexed peptide analysis for kinetic measurements of major human apolipoproteins by LC/MS/MS

Croyal

Fall

Ferchaud‐Roucher

et al. 2016

Journal of Lipid Research

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those of the entire lipoprotein metabolism ( 1, 3 ). The incorporation of a labeled amino acid into the protein during its synthesis is subsequently measured over time and analyzed with a compartmental model to obtain the kinetic data ( 4, 5 ). The reference method to measure tracer enrichments involves isolation of the Apos by gel electrophoresis followed by acid hydrolysis to obtain unlabeled and labeled amino acids. Then, the amino acids are derivatized for GC/ MS analysis ( 3 ). These approaches are limited to one or a small number of relatively abundant Apos and remain a timeconsuming process. Kinetic studies are therefore mainly focused on the most abundant structural Apos (ApoA-I and ApoB100) and less on others, although they have a central role in lipid metabolism (ApoC-II, ApoC-III and ApoE) ( 6 ).The combination of proteomic tools, such as enzymatic proteolysis and liquid LC/MS/MS, has appeared recently to be a powerful tool to study plasma proteins ( 7-11 ). Although promising, one analytical challenge is to use this method in a single run analysis for the determination of concentrations and tracer enrichments of a signifi cant set of plasma proteins with large differences in molecular mass or abundances ( 6, 11 ).We recently published an LC/MS/MS method to simultaneously measure the concentration, tracer enrichment, and average size of Apo(a) ( 9, 12 ). In the present study, we aimed to describe the development and the validation of a multiplexed LC/MS/MS method, performing in a single run the enrichment measurements and the quantifi cation of six major human Apos (ApoA-I, ApoA-II, ApoB100, ApoC-II, ApoC-III, and ApoE) in plasma samples obtained from a stable isotope kinetic study in humans. Lipoprotein kinetic studies using radioactive or stable isotope tracers have been performed for years in humans to gain a better understanding of the mechanisms involved in lipid metabolism disturbances and related diseases ( 1, 2 ). Endogenous labeling with an amino acid tracer of Apo, a main component of lipoproteins, is commonly used, assuming the kinetics of Apos represent a good estimate of This work was supported by the Biogenouest CORSAIRE core facility.

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Section: Discussionsupporting

confidence: 88%

“…We found similar data for ApoC-II but, to our knowledge, no previous work can support this fi nding. Despite the lack of direct comparisons in our study with [18][19][20][21][22][26][27][28]. In addition, ApoA-I/ApoA-II and ApoC-III/ApoC-II concentration ratios were also in the reported ranges ( 6,11,19,21,26 ).…”

Section: Discussionmentioning

confidence: 55%

Multiplexed peptide analysis for kinetic measurements of major human apolipoproteins by LC/MS/MS

Croyal

Fall

Ferchaud‐Roucher

et al. 2016

Journal of Lipid Research

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“…Interestingly, in contrast to the concentrations of the major apoB-containing Lp, LDL, the plasma levels of Lp(a) correlated highly significantly with the rate of biosynthesis, whereas there was no correlation with the fractional catabolic rate (FCR) (49). These results have been confirmed by several other groups using radioactive or stable isotope labeling techniques (50,51).We have also been interested in the mechanism of Lp(a) catabolism via specific cell surface receptors. In order to study this, binding studies of LDL and Lp(a) to cultured human fibroblasts were performed.…”

Section: Pioneers In Lp(a) Researchsupporting

confidence: 60%

Lipoprotein (a): a historical appraisal

Kostner

2017

Journal of Lipid Research

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“…The metabolic data accumulating in this study after appropriate modeling present a scenario of virtually complete intracellular assembly of Lp(a) [43].…”

Section: In Vivo Metabolism Of Lp(a) and Ldl In Healthy Subjectsmentioning

confidence: 99%

New Insights into the Assembly and Metabolism of ApoB-Containing Lipoproteins from in vivo Kinetic Studies: Results on Healthy Subjects and Patients with Chronic Kidney Disease

Dieplinger¹,

Dieplinger²

2012

Lipoproteins - Role in Health and Diseases

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In vivo stable-isotope kinetic study suggests intracellular assembly of lipoprotein(a)

Cited by 58 publications

References 42 publications

Multiplexed peptide analysis for kinetic measurements of major human apolipoproteins by LC/MS/MS

Multiplexed peptide analysis for kinetic measurements of major human apolipoproteins by LC/MS/MS

Lipoprotein (a): a historical appraisal

New Insights into the Assembly and Metabolism of ApoB-Containing Lipoproteins from in vivo Kinetic Studies: Results on Healthy Subjects and Patients with Chronic Kidney Disease

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