[15] Oil-drop tensiometer: Applications for studying the kinetics of lipase action

Labourdenne, S.; Cagna, Alain; Delorme, B.; Esposito, George G.; Verger, Robert; Rivière, C.

doi:10.1016/s0076-6879(97)86017-x

Cited by 16 publications

(14 citation statements)

References 37 publications

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“…An oil-drop tensiometer designed by Teclis Instruments (Longessaigne, France) was used to measure the interfacial tension () of lipid/water interfaces (40,41,43).  is the energy required to create one new cm 2 of surface (i.e.,  = ergs/cm 2 or mN/m) (41,50).…”

Section: Interfacial Tension and Surface Pressure Measurementsmentioning

confidence: 99%

“…Lipid-free apoC-III has little -helical content, but apoC-III acquires 50-70% helical content on binding to lipid (33)(34)(35)(36). NMR structures of apoC-III:sodium dodecyl sulfate complexes showed helix formation in the protein's N-terminal (residues , central (resides [34][35][36][37][38][39][40][41][42][43], and C-terminal (resides 47-65) regions ( Fig. 1) (36).…”

mentioning

confidence: 99%

“…We used oil-drop tensiometry to characterize the behavior of each peptide at triolein/water (TO/W) and POPC/ triolein/water (POPC/TO/W) interfaces (40,41). The TO/W interface provides a model for protein interactions with a TG core, a component of all TG-rich lipoproteins, whereas POPC/TO/W interfaces more closely mimic the surface of nascent, cholesterol-poor lipoproteins (42).…”

mentioning

confidence: 99%

“…The TO/W interface provides a model for protein interactions with a TG core, a component of all TG-rich lipoproteins, whereas POPC/TO/W interfaces more closely mimic the surface of nascent, cholesterol-poor lipoproteins (42). The oil-drop tensiometer measures the surface tension of lipid/ water interfaces, which is high at hydrophobic surfaces (40,41,43). Peptide adsorption to these interfaces decreases surface tension, and the magnitude of this change reflects the peptide's ability to remodel the surface (41,(44)(45)(46).…”

mentioning

confidence: 99%

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Aromatic residues in the C terminus of apolipoprotein C-III mediate lipid binding and LPL inhibition

Meyers

Larsson

Vorrsjö

et al. 2017

Journal of Lipid Research

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This article is available online at http://www.jlr.org triglyceride (TG)-rich lipoproteins (i.e., VLDLs and chylomicrons) (2-4). In normolipidemic individuals, plasma concentrations of apoC-III are 80-100 g/ml, with approximately 60% of apoC-III associated with HDL, 20% with LDL, 20% with the TG-rich lipoproteins, and very little free in plasma (5). In the hypertriglyceridemic state, plasma apoC3 levels increase to >300 g/ml, and the percentage on TG-rich lipoproteins increases from 20% to upward of 60% (5-7). In fact, animal and human studies have established a strong, positive correlation between elevated plasma apoC-III levels and TG levels, which are an independent risk factor for atherosclerotic CVD (1, 8). The overexpression of human apoC-III in mice promoted the development of atherosclerosis and was associated with elevated TG levels, but low HDL cholesterol levels, in plasma (9). In contrast, targeted disruption of apoC-III in mice was associated with the rapid catabolism of TG-rich lipoproteins and a 70% decrease in fasting TG levels (10).Beyond these mouse models, clinical studies established the importance of apoC-III as a predictor of CVD outcomes. Increased serum apoC-III levels were associated with elevated serum TG and, in turn, insulin resistance, CVD, and type II diabetes (11-13). Plasma levels of apoC-III independently predicted risk for coronary heart disease, even after control for blood lipids (12,14). Further indicating a crucial role of apoC-III in regulating lipid metabolism, subjects with gain-of-function mutations in the apoC-III gene exhibited hypertriglyceridemia that was associated with elevated plasma apoC-III protein levels (15, 16). In contrast, subjects with loss-of-function mutations in the apoC-III gene exhibited reduced TG and apoC-III levels (17-21), which had a cardioprotective effect. apoC-III is a small (79 amino acid), O-glycosylated, secretory protein that is synthesized in the liver and intestine (1). ApoC-III is the most abundant apoC in humans and circulates in plasma as a component of HDLs and the Abstract

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Section: Interfacial Tension and Surface Pressure Measurementsmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Aromatic residues in the C terminus of apolipoprotein C-III mediate lipid binding and LPL inhibition

Meyers

Larsson

Vorrsjö

et al. 2017

Journal of Lipid Research

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“…To probe the relation between apoC-II and lipoprotein surface pressure, we used oil-drop tensiometry (30,35) to characterize the behavior of human apoC-II at triolein/water (TO/W) and 1-palmitoyl-2-oleoyl-phosphatidylcholine/triolein/water (POPC/TO/W) interfaces. TO is a common TG, and POPC is the most abundant phospholipid on lipoproteins.…”

Section: Human Apolipoprotein C-ii (Apoc-ii)mentioning

confidence: 99%

A Pressure-dependent Model for the Regulation of Lipoprotein Lipase by Apolipoprotein C-II

Meyers

Larsson

Olivecrona

et al. 2015

Journal of Biological Chemistry

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Background: Apolipoprotein C-II (apoC-II) is the cofactor for lipoprotein lipase (LPL), the central enzyme for plasma triglyceride metabolism. Results: ApoC-II adopts two conformations at lipid surfaces that are favored at different surface pressures. Conclusion: Conformational rearrangement of apoC-II at lipoprotein surfaces promotes interaction with LPL. Significance: Our mechanism explains how apoC-II withstands increases in surface pressure during LPL-mediated lipoprotein metabolism.

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Methods for lipase detection and assay: a critical review

Beisson¹,

Tiss

Rivière

et al. 2000

Eur. J. Lipid Sci. Technol.

333

169

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[15] Oil-drop tensiometer: Applications for studying the kinetics of lipase action

Cited by 16 publications

References 37 publications

Aromatic residues in the C terminus of apolipoprotein C-III mediate lipid binding and LPL inhibition

Aromatic residues in the C terminus of apolipoprotein C-III mediate lipid binding and LPL inhibition

A Pressure-dependent Model for the Regulation of Lipoprotein Lipase by Apolipoprotein C-II

Methods for lipase detection and assay: a critical review

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