Kinetics and mechanism of phosphatidylcholine and cholesterol exchange between single bilayer vesicles and bovine serum high-density lipoprotein

Jonas, Ana; Maine, Gregory T.

doi:10.1021/bi00576a014

Cited by 78 publications

(35 citation statements)

References 30 publications

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“…The molecular origin of this effect is in the process of being evaluated via the careful measurement of the functional properties (spin state, rate of autoxidation, uncoupling and product formation) of various CYP3A4 states as a function of substrate loading and various anionic lipid compositions. It is possible there exists a synergy between phospholipids manifested through the increased accessibility of the proteins to the negatively charged head group, as was previously described for the case of blood coagulation factors binding to Nanodisc surfaces (66, 67). …”

Section: Nanodiscs For Analysis Of Lipid-protein Interactionsmentioning

confidence: 75%

“…The binding affinity and stoichiometry for human factor VII and factor X as a function of the PS/(PC+PS) mole percent were readily determined. In another study (67) more complex lipid mixtures were accommodated in the Nanodisc platform to provide for the molecular analysis of the synergies of particular lipids in the coagulation factor activation cascade. This work led to the ABC "anything but choline" hypothesis describing the ability of smaller head group lipids, such as PG, to dramatically accelerate the initiation of the clotting process.…”

Section: Nanodiscs For Analysis Of Lipid-protein Interactionsmentioning

confidence: 99%

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Nanodiscs as a New Tool to Examine Lipid–Protein Interactions

Schuler

Denisov

Sligar

2012

Methods in Molecular Biology

139

131

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Nanodiscs are self-assembled discoidal fragments of lipid bilayers 8 – 16 nm in diameter, stabilized in solution by amphipathic helical scaffold protein. As stable and highly soluble membrane mimetics with controlled lipid composition and ability to add affinity tags to the scaffold protein, Nanodiscs represent an attractive model system for solubilization, isolation, purification, and biophysical and biochemical studies of membrane proteins. We overview various approaches to the structural and functional studies of different classes of integral membrane proteins such as ion channels, transporters, GPCR and other receptors, membrane enzymes, blood coagulation cascade proteins, et cetera incorporated into Nanodiscs with the special focus on the advantages provided by homogeneity, ability to control oligomerization state of the target protein and lipid composition of the bilayer. Special attention is paid to the opportunities provided by Nanodisc system for the detailed studies of the role of different lipid properties and protein – lipid interactions in the functional behavior of membrane proteins.

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Section: Nanodiscs For Analysis Of Lipid-protein Interactionsmentioning

confidence: 75%

Section: Nanodiscs For Analysis Of Lipid-protein Interactionsmentioning

confidence: 99%

Nanodiscs as a New Tool to Examine Lipid–Protein Interactions

Schuler

Denisov

Sligar

2012

Methods in Molecular Biology

139

131

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“…Other studies have demonstrated a dependence of the transfer rate on the concentration of acceptors (Jonas & Maine, 1979;Petrie & Jonas, 1984;Ferrell et al, 1985;Steck et al, 1988;Jones & Thompson, 1989), but in these studies the concentrationdependent rate component was most likely due to differences between the on-rates onto the acceptor and donor bilayers (Nichols & Pagano, 1981), or the component was shown to be sensitive to the aqueous solubility of the ligand (Jones & Thompson, 1990). Thus, it appears that the mechanism of AOffa transfer from A-and H-FABP differs from the aqueous transfer mechanism observed for most lipids in model systems.…”

Section: Discussionmentioning

confidence: 91%

Mechanism of fluorescent fatty acid transfer from adipocyte fatty acid binding protein to membranes

Wootan¹,

Bernlohr²,

Storch³

1993

Biochemistry

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Adipocyte fatty acid binding protein (A-FABP) is a 15-kDa protein found in high abundance in the cytosol of adipose cells. To better understand the role of this protein in intracellular free fatty acid (ffa) transport, the mechanism of ffa transfer from A-FABP to model membranes was examined by monitoring the transfer of fluorescent anthroyloxy ffa (AOffa) to small unilamellar phospholipid vesicles, using a resonance energy transfer assay. Structural features of ffa that increase aqueous solubility, such as shorter chain length and unsaturation, did not increase the AOffa transfer rate. In addition, solution conditions that increase the aqueous solubility of ffa, such as decreasing ionic strength and increasing pH, had little effect on AOffa transfer from A-FABP to membranes. These results suggest that AOffa do not transfer through the aqueous phase. The small entropic contribution to the free energy of the transfer process provides further evidence that AOffa may not travel through the surrounding aqueous environment when transferred from A-FABP to phospholipid membranes. Finally, the rate of AOffa transfer from A-FABP was directly dependent on the concentration of the acceptor membranes. These studies suggest that AOffa transfer from A-FABP to phospholipid vesicles may occur via transient collisional interactions between the protein and membranes.(ABSTRACT TRUNCATED AT 250 WORDS)

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“…For the binding study, we assumed that cholesterol partitioning between the outer and inner monolayer is 70:30 and that only cholesterol in the outer monolayer is subjected to exchange (31,32). The Scatchard plots for cholesterol and PC binding to PLTP were obtained by determining the amounts of PC and cholesterol bound to PLTP obtained by sucrose density gradient centrifugation of the incubation mixtures containing PLTP and vesicles.…”

Section: Cholesterol Transfer From Pc-cholesterol Vesicles To Hdl 3 -mentioning

confidence: 99%

Phospholipid Transfer Protein Mediates Transfer of not Only Phosphatidylcholine but Also Cholesterol from Phosphatidylcholine-Cholesterol Vesicles to High Density Lipoproteins

Nishida

1997

Journal of Biological Chemistry

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Phospholipid transfer protein (PLTP) purified from human plasma was found to enhance the transfer of cholesterol from single bilayer vesicles containing phosphatidylcholine and cholesterol to high density lipoprotein-3. The rate of cholesterol transfer was greatly influenced by the cholesterol content of the donor vesicles. The maximal rate was observed with the vesicles containing 20 -25 mol % cholesterol. This was in contrast to a progressive decline in the rate of phosphatidylcholine transfer with an increase in the cholesterol content. To determine the binding of cholesterol and phosphatidylcholine to PLTP, the mixtures of PLTP and the vesicles containing 3 H-labeled phosphatidylcholine and 14 C-labeled cholesterol were incubated and subjected to sucrose density gradient centrifugation. Determination of the label profiles showed that cholesterol as well as phosphatidylcholine were transferred from the vesicles to PLTP. The reversible nature of the binding was shown by the transfer of labeled cholesterol and phosphatidylcholine bound to PLTP to the acceptor vesicles or low density lipoprotein. Isothermal equilibrium binding of PLTP for cholesterol and phosphatidylcholine showed that PLTP possessed a considerably higher affinity and binding capacity for phosphatidylcholine than for cholesterol. The phosphatidylcholine binding affinity and capacity were greater when PLTP was incubated with phosphatidylcholine vesicles without cholesterol. A possible importance of PLTP-mediated cholesterol transfer in the circulation was described.

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Kinetics and mechanism of phosphatidylcholine and cholesterol exchange between single bilayer vesicles and bovine serum high-density lipoprotein

Cited by 78 publications

References 30 publications

Nanodiscs as a New Tool to Examine Lipid–Protein Interactions

Nanodiscs as a New Tool to Examine Lipid–Protein Interactions

Mechanism of fluorescent fatty acid transfer from adipocyte fatty acid binding protein to membranes

Phospholipid Transfer Protein Mediates Transfer of not Only Phosphatidylcholine but Also Cholesterol from Phosphatidylcholine-Cholesterol Vesicles to High Density Lipoproteins

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