Distribution and Functions of Lecithin: Cholesterol Acyltransferase and Cholesteryl Ester Transfer Protein in Plasma Lipoproteins

Francone, O. L.; Gürakar, Arzu R.; Fielding, C J

doi:10.1016/s0021-9258(18)83541-4

Cited by 256 publications

(53 citation statements)

References 40 publications

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“…Reference Collection 6 (Fielding and Fielding, 1980;Morton and Zilversmit, 1981;Mahadevan and Soloff, 1983;Steyrer and Kostner, 1988;Camato et al, 1989;Francone et al, 1989;Holmquist, 1989;Sánchez et al, 1992a). Reference Collection 7 (Utermann et al, 1980;Camato et al, 1989;Yang et al, 1990Yang et al, , 1994Blanco-Vaca et al, 1992;Liu et al, 2001;Jin et al, 2006;Najyb et al, 2015;Lai et al, 2017).…”

Section: Apod Systematic Review Reference Collectionsmentioning

confidence: 99%

The Lipocalin Apolipoprotein D Functional Portrait: A Systematic Review

Sánchez

Ganfornina

2021

Front. Physiol.

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Apolipoprotein D is a chordate gene early originated in the Lipocalin protein family. Among other features, regulation of its expression in a wide variety of disease conditions in humans, as apparently unrelated as neurodegeneration or breast cancer, have called for attention on this gene. Also, its presence in different tissues, from blood to brain, and different subcellular locations, from HDL lipoparticles to the interior of lysosomes or the surface of extracellular vesicles, poses an interesting challenge in deciphering its physiological function: Is ApoD a moonlighting protein, serving different roles in different cellular compartments, tissues, or organisms? Or does it have a unique biochemical mechanism of action that accounts for such apparently diverse roles in different physiological situations? To answer these questions, we have performed a systematic review of all primary publications where ApoD properties have been investigated in chordates. We conclude that ApoD ligand binding in the Lipocalin pocket, combined with an antioxidant activity performed at the rim of the pocket are properties sufficient to explain ApoD association with different lipid-based structures, where its physiological function is better described as lipid-management than by long-range lipid-transport. Controlling the redox state of these lipid structures in particular subcellular locations or extracellular structures, ApoD is able to modulate an enormous array of apparently diverse processes in the organism, both in health and disease. The new picture emerging from these data should help to put the physiological role of ApoD in new contexts and to inspire well-focused future research.

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Section: Apod Systematic Review Reference Collectionsmentioning

confidence: 99%

The Lipocalin Apolipoprotein D Functional Portrait: A Systematic Review

Sánchez

Ganfornina

2021

Front. Physiol.

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“…Cholesterol present in different HDL subfractions originates from the de novo secretion of lipoproteins as well as from transfer from cell membranes and from apoB-containing lipoproteins (LDL) (1)(2)(3)(4)(5). Recent studies by Fielding and colleagues indicate that cellular cholesterol may first transfer to a small pre-f31-HDL and then be transferred to larger pre-f3 2 -and pre-f33-HDL, where the esterification of cholesterol occurs (6,7). The same group has also reported that LDL-cholesterol is transferred to and esterified in a-HDL 3 (8,9).…”

Section: Effect Of Lpai Composition and Structure On Cholesterol Transfer Between Lipoproteins*mentioning

confidence: 99%

Effect of LpA-I Composition and Structure on Cholesterol Transfer between Lipoproteins

Meng¹,

Sparks²,

Marcel³

1995

Journal of Biological Chemistry

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The effect of high density lipoprotein composition on the rates of unesterified cholesterol exchange between low density lipoproteins (LDL) and well-defined homogeneous discoidal lipoproteins (LpA-I) reconstituted with phosphatidylcholine, cholesterol, and apolipoprotein A-I (apoA-I) has been investigated. LpA-I containing cholesterol and 2, 3, and 4 apoA-I molecules per particle differed in their ability to accept or donate cholesterol. A significant cholesterol exchange occurs between LDL and Lp2A-I (7.8 and 9.6 nm), while there is little or no cholesterol exchange detectable between LDL and Lp3A-I (10.8 and 13.4 nm) and Lp4A-I (17.0 nm) complexes. The cholesterol transfer from LDL to the cholesterol-free Lp2A-I (9.6 nm), Lp3A-I (13.4 nm), and Lp4A-I (17.0 nm) particles also shows significant cholesterol transfer to Lp2A-I, while there is no detectable transfer to Lp3- and 4A-I particles. The rates of cholesterol transfer to cholesterol-free and cholesterol-containing Lp2A-I appear to differ significantly. Cholesterol transfer from LDL to cholesterol-free Lp2A-I is zero order with respect to acceptor concentrations when the Lp2A-I/LDL ratio is above 10. Transfer rates from LDL to cholesterol-free Lp2A-I are faster for the smaller Lp2A-I (8.5 nm) than to the larger Lp2A-I (9.7 nm) and exhibit half-times (t1/2) at 25 degrees C of 4.0 and 5.3 h, respectively. In contrast, cholesterol transfer from LDL to cholesterol-containing Lp2A-I remains dependent upon acceptor concentrations to an acceptor/donor particle ratio of 80. In addition, transfer from LDL to cholesterol-containing Lp2A-I is faster to the 9.6 nm than to 7.8 nm particles, with t1/2 of 1.4 and 2.3 h, respectively. The rates of cholesterol transfer from Lp2A-I to LDL are higher than in the opposite direction, in particular for the small Lp2A-I (7.8 nm), which has a t1/2 of approximately 50 min. The results show that changes in the composition and structure of apoA-I-containing particles have a significant effect on inter-lipoprotein exchange of cholesterol. This suggests that the kinetics of cholesterol transfer to and from reconstituted discoidal LpA-I particles cannot be fully explained by passive aqueous diffusion.

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“…One occurs inside cells , via acyl-CoA cholesterol acyltransferase (ACAT) to esterify cholesterol. The other occurs in extracellular spaces such as the bloodstream, where high density lipoprotein (HDL) reverse cholesterol transport catalyzed by lecithin cholesterol acyl transferase (LCAT) . The hydrolysis of CEs requires cholesterol ester hydrolases, especially neutral cholesterol ester hydrolase (NCEH) and lysosomal acidic lipase (LAL).…”

mentioning

confidence: 99%

“…The other occurs in extracellular spaces such as the bloodstream, where high density lipoprotein (HDL) reverse cholesterol transport catalyzed by lecithin cholesterol acyl transferase (LCAT). 6 The hydrolysis of CEs requires cholesterol ester hydrolases, 7 especially neutral cholesterol ester hydrolase (NCEH) and lysosomal acidic lipase (LAL). LAL is the primary enzyme responsible for the hydrolysis of cholesteryl esters in low density lipoprotein (LDL).…”

mentioning

confidence: 99%

Mathematical Model-Assisted UHPLC-MS/MS Method for Global Profiling and Quantification of Cholesteryl Esters in Hyperlipidemic Golden Hamsters

Wang

et al. 2019

Anal. Chem.

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Cholesteryl esters (CEs) are formed by the 3-hydroxyl group of cholesterol and a fatty acyl chain through an ester bond and function as a biologically inert storage form of cholesterol. Abnormal CE levels are often related to various diseases, particularly hyperlipidemia and atherosclerosis. Herein, we developed a mathematical model-assisted ultrahigh performance liquid chromatography–mass spectrometry (UHPLC-MS) method for the untargeted identification to targeted quantification of CEs in plasma, different density lipoprotein samples from humans, rats, and golden hamsters. Using UHPLC-quadrupole-time-of-flight mass spectrometry (UHPLC-QTOF-MS), 81 CE candidates were detected in the above samples, of which 24 CEs were reported in the Human Metabolome Database and 57 CEs were newly identified based on an in-house database of theoretically possible CEs, including the computationally generated precursor ion m/z mass of CE, carbon number and double bond numbers of the fatty acyl chain. Then three mathematical models based on the characteristic chromatographic retention behavior related to structural features were established and validated using commercial and synthetic CE standards. The mathematical model-assisted UHPLC-MS/MS strategy was proposed to provide a global profiling and identification of CEs, especially unknown CEs. With the efficient strategy, 74 CEs in the plasma of golden hamsters were identified and then quantified in normal and hyperlipidemic golden hamsters by dynamic multiple reaction monitoring (dMRM). A total of 21 CEs among 35 shared potential biomarkers were newly found for hyperlipidemia. Our work will contribute to the in-depth study of the functions of CEs and the discovery of disease biomarkers.

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Distribution and Functions of Lecithin: Cholesterol Acyltransferase and Cholesteryl Ester Transfer Protein in Plasma Lipoproteins

Cited by 256 publications

References 40 publications

The Lipocalin Apolipoprotein D Functional Portrait: A Systematic Review

The Lipocalin Apolipoprotein D Functional Portrait: A Systematic Review

Effect of LpA-I Composition and Structure on Cholesterol Transfer between Lipoproteins

Mathematical Model-Assisted UHPLC-MS/MS Method for Global Profiling and Quantification of Cholesteryl Esters in Hyperlipidemic Golden Hamsters

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