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Sialylated isoforms of apolipoprotein C-III and plasma lipids in subjects with coronary artery disease

  • Oliviero Olivieri EMAIL logo , Carmela Chiariello , Nicola Martinelli , Annalisa Castagna , Giulia Speziali , Domenico Girelli , Francesca Pizzolo , Antonella Bassi , Daniela Cecconi , Elisa Robotti , Marcello Manfredi , Eleonora Conte and Emilio Marengo
Published/Copyright: April 13, 2018

Abstract

Background:

Apolipoprotein C-III (ApoC-III), a key regulator of plasma triglyceride (TG), is present in three isoforms, i.e. non-sialylated (ApoC-III0), monosialylated (ApoC-III1) and disialylated (ApoC-III2). We aimed at quantifying the distribution of the ApoC-III glycoforms in patients with angiographically demonstrated coronary artery disease (CAD) according to levels of total ApoC-III plasma concentration.

Methods:

ApoC-III glycoforms were quantified by a specifically developed, high-resolution, mass spectrometry method in unrelated CAD patients. Lipoprotein lipase (LPL) activity was estimated by a fluorescence-based method.

Results:

In 101 statin-treated CAD patients, the absolute concentrations of the three glycoforms similarly increased across ApoC-III quartiles, but the proportion of ApoC-III1 rose whereas that of ApoC-III0 decreased progressively by increasing total ApoC-III concentrations. The proportion of ApoC-III2 was quite constant throughout the whole range of total ApoC-III. A higher proportion of ApoC-III1 reflected an unfavorable lipid profile characterized by high levels of TG, total and low density lipoprotein cholesterol, ApoE and reduced ApoA-I. The correlations between ApoC-III glycoforms and TG were confirmed in 50 statin-free CAD patients. High concentration of total ApoC-III was associated with low LPL activity, while no correlation was found for the relative proportion of glycoforms.

Conclusions:

Specific patterns of ApoC-III glycoforms are present across different total ApoC-III concentrations in CAD patients. The inhibitory effect of ApoC-III on LPL appears related to total ApoC-III concentration, but not to the relative proportion of ApoC-III glycoforms.


Corresponding author: Oliviero Olivieri, Professor of Internal Medicine, Department of Medicine, Unit of Internal Medicine, University of Verona, Policlinico G.B. Rossi, Piazzale Antonio Scuro 1, 37134 Verona, Italy
aCurrent address: Azienda Socio Sanitaria di Mantova Strada Lago Paiolo, n. 10, Mantova, Italy.

Acknowledgments

The work was performed in part in the LURM (Laboratorio Universitario di Ricerca Medica) Research Center, University of Verona.

  1. Author contributions: All the authors have accepted responsibility for the entire content of this submitted manuscript and approved submission.

  2. Research funding: OO and NM acknowledge the support of Fondazione CariVerona (B36J16002570003, Funder id: 10.13039/501100006747). MM acknowledges the support of Fondazione CRT project Lagrange.

  3. Employment or leadership: None declared.

  4. Honorarium: None declared.

  5. Competing interests: The funding organization(s) played no role in the study design; in the collection, analysis, and interpretation of data; in the writing of the report; or in the decision to submit the report for publication.

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Supplementary Material:

The online version of this article offers supplementary material (https://doi.org/10.1515/cclm-2017-1099).


Received: 2017-11-24
Accepted: 2018-03-09
Published Online: 2018-04-13
Published in Print: 2018-08-28

©2018 Walter de Gruyter GmbH, Berlin/Boston

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