A review of the role of apolipoprotein C-II in lipoprotein metabolism and cardiovascular disease

Kei, Anastazia; Filippatos, Theodosios D.; Tsimihodimos, V.; Elisaf, Moses

doi:10.1016/j.metabol.2011.12.002

Cited by 117 publications

(94 citation statements)

References 192 publications

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“…6B). Under zero-order with apoC-II were carried out using Intralipid as substrate, because plasma normally contains sufficient amounts of apoC-II for full activation of LPL (28). The LPL concentration was held constant, while the apoC-II concentration was varied from 0 to 1,000 nM.…”

Section: Itc Can Be Used To Study the Influence Of Added Regulators Omentioning

confidence: 99%

Lipoprotein lipase activity and interactions studied in human plasma by isothermal titration calorimetry

Reimund

Kovrov

Olivecrona

et al. 2017

Journal of Lipid Research

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LPL is produced and secreted from parenchymal cells like adipocytes and myocytes for transport to the luminal side of the endothelium via interaction with the glycosylphosphatidylinositol-anchored high density lipoprotein binding protein 1 (GPIHBP1) (8). Several plasma components have been shown to directly or indirectly modulate the activity of LPL. apoC-II and apoA-V increase the activity of LPL, while apoC-I, apoC-III, angiopoietin-like protein (ANGPTL)3, ANGPTL4, and ANGPTL8 decrease the activity (1, 9). The expression of each of these proteins depends on nutritional and hormonal factors, so that lipid uptake in tissues to a large extent is regulated by posttranslational effects on LPL (1, 9). It is possible that the macromolecular environment in plasma itself may be an influence on the interaction of LPL with its ligands. The protein concentration of plasma (80 g/l) has been shown to cause significant crowding effects (10). It is also possible that some plasma regulators of LPL activity have not been identified yet.LPL activity can be measured in vitro by using artificial, usually emulsified, systems of radiolabeled, fluorogenic, or chromogenic substrates, or isolated triglyceride-rich lipoproteins (TRLs). The reaction products are detected at certain time points by chemical quantification or by determination of radioactivity or fluorescence. These methods have been used to unravel important aspects of the action of LPL and also to quantitate the levels of LPL activity in cells and tissues. Only small amounts of LPL activity are normally present in the circulating blood (11). Therefore, intravenous injections of heparin are made to release LPL from its endothelial binding sites. Determination of LPL activity in postheparin plasma, using artificial substrate systems, is considered to give an estimation of the amount of active LPL at the vascular endothelium (12).Lack of a suitable technique for continuous monitoring of triglyceride hydrolysis in plasma has hampered the understanding of the action of LPL under physiological Abstract LPL hydrolyzes triglycerides in plasma lipoproteins. Due to the complex regulation mechanism, it has been difficult to mimic the physiological conditions under which LPL acts in vitro. We demonstrate that isothermal titration calorimetry (ITC), using human plasma as substrate, overcomes several limitations of previously used techniques. The high sensitivity of ITC allows continuous recording of the heat released during hydrolysis. Both initial rates and kinetics for complete hydrolysis of plasma lipids can be studied. The hydrolytic breakdown of plasma triglycerides by LPL at the capillary endothelium is a crucial event that contributes to control of the levels of triglycerides in plasma (1, 2). Many recent studies support the view that an elevated level of triglycerides in plasma is an independent risk factor for development of atherosclerosis (3-5). Therefore, the LPL system is considered to be an interesting target for drug design (6, 7). Education and Research Grant IUT 19-9,...

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Section: Itc Can Be Used To Study the Influence Of Added Regulators Omentioning

confidence: 99%

Lipoprotein lipase activity and interactions studied in human plasma by isothermal titration calorimetry

Reimund

Kovrov

Olivecrona

et al. 2017

Journal of Lipid Research

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“…The main causes of extreme hypercholesterolemia or hypertriglyceridemia are homozygous familial hypercholesterolemia, familial chylomicronemia, familial lipoprotein lipase deficiency, and familial apo C-II deficiency [8][9][10].…”

Section: Extreme Hypercholesterolemiamentioning

confidence: 99%

Microsomal Transfer Protein Inhibitors, New Approach for Treatment of Familial Hypercholesterolemia, Review of the Literature, Original Findings, and Clinical Significance

Kolovou

Vasiliadis

Gontoras

et al. 2015

Cardiovascular Therapeutics

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SUMMARYThe genetic causes of cholesterol metabolism disorders usually lead to premature atherosclerosis. The most well recognized genetically caused hypercholesterolemia is familial hypercholesterolemia. Although the disease is well known, as the discovery of low-density lipoprotein receptor, the classical treatment with lipid-lowering drugs (statins, fibrates, ezetimibe, colesevelam) is still not adequate and new options are seeking. This review is an attempt to analyze the microsomal transfer protein (MTP) inhibitors as a new approach for treatment of familial hypercholesterolemia, to reviews the literature according to MTP inhibitors and finally to provide original findings.

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“…Apolipoproteins are centrally involved in lipid metabolism and atherosclerotic processes and fulfill an important role as biomarkers for cardiovascular disease (CVD) 5 risk. Apolipoprotein B-100 (apoB-100), for example, accurately reflects the number of potentially atherogenic LDL particles, whereas apoA-I reflects atheroprotective HDL particles.…”

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confidence: 99%

Automated Multiplex LC-MS/MS Assay for Quantifying Serum Apolipoproteins A-I, B, C-I, C-II, C-III, and E with Qualitative Apolipoprotein E Phenotyping

Broek¹,

Romijn²,

Nouta³

et al. 2016

Clinical Chemistry

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BACKGROUND Direct and calculated measures of lipoprotein fractions for cardiovascular risk assessment suffer from analytical inaccuracy in certain dyslipidemic and pathological states, most commonly hypertriglyceridemia. LC-MS/MS has proven suitable for multiplexed quantification and phenotyping of apolipoproteins. We developed and provisionally validated an automated assay for quantification of apolipoprotein (apo) A-I, B, C-I, C-II, C-III, and E and simultaneous qualitative assessment of apoE phenotypes. METHODS We used 5 value-assigned human serum pools for external calibration. Serum proteins were denatured, reduced, and alkylated according to standard mass spectrometry–based proteomics procedures. After trypsin digestion, peptides were analyzed by LC-MS/MS. For each peptide, we measured 2 transitions. We compared LC-MS/MS results to those obtained by an immunoturbidimetric assay or ELISA. RESULTS Intraassay CVs were 2.3%–5.5%, and total CVs were 2.5%–5.9%. The LC-MS/MS assay correlated (R = 0.975–0.995) with immunoturbidimetric assays with Conformité Européenne marking for apoA-I, apoB, apoC-II, apoC-III, and apoE in normotriglyceridemic (n = 54) and hypertriglyceridemic (n = 46) sera. Results were interchangeable for apoA-I ≤3.0 g/L (Deming slope 1.014) and for apoB-100 ≤1.8 g/L (Deming slope 1.016) and were traceable to higher-order standards. CONCLUSIONS The multiplex format provides an opportunity for new diagnostic and pathophysiologic insights into types of dyslipidemia and allows a more personalized approach for diagnosis and treatment of lipid abnormalities.

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A review of the role of apolipoprotein C-II in lipoprotein metabolism and cardiovascular disease

Cited by 117 publications

References 192 publications

Lipoprotein lipase activity and interactions studied in human plasma by isothermal titration calorimetry

Lipoprotein lipase activity and interactions studied in human plasma by isothermal titration calorimetry

Microsomal Transfer Protein Inhibitors, New Approach for Treatment of Familial Hypercholesterolemia, Review of the Literature, Original Findings, and Clinical Significance

Automated Multiplex LC-MS/MS Assay for Quantifying Serum Apolipoproteins A-I, B, C-I, C-II, C-III, and E with Qualitative Apolipoprotein E Phenotyping

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