Surface diffusion in human serum lipoproteins

Cushley, Robert J.; Treleaven, W. Dale; Parmar, Yashpal I.; Chana, Ravinder S.; Fenske, David B.

doi:10.1016/0006-291x(87)90766-2

Cited by 24 publications

(10 citation statements)

References 12 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Equation 6 was listed incorrectly in our previous paper (Cushley et al, 1987), but the diffusion coefficients we reported were correct. Aa is also obtained from a plot of (Aul12 -C ) versus u?.…”

Section: Theorymentioning

confidence: 76%

“…Of particular interest is the value of D, measured for LDL at 25 OC (1.4 X lo4 cm2/s), which is more than an order of magnitude slower than observed in the HDLs or in model systems in the liquid-crystalline phase. In a previous paper, we considered three possible explanations for the slow diffusion observed in LDL, these being (1) the higher SPM content of the LDL monolayer, (2) core-monolayer interactions, and (3) interactions of the phospholipid with apo B-100 (Cushley et al, 1987). Recently, Ibdah et al (1989) demonstrated that LDL surface lipids form a more closepacked monolayer than those of HDL3 due to the higher content of saturated PC and cholesterol in LDL.…”

Section: Discussionmentioning

confidence: 97%

See 1 more Smart Citation

Structure and motion of phospholipids in human plasma lipoproteins. A phosphorus-31 NMR study

Fenske¹,

Chana²,

Parmar³

et al. 1990

Biochemistry

Self Cite

View full text Add to dashboard Cite

The structure and motion of phospholipids in human plasma lipoproteins have been studied by using 31P NMR. Lateral diffusion coefficients, DT, obtained from the viscosity dependence of the 31P NMR line widths, were obtained for very low density lipoprotein (VLDL), low-density lipoprotein (LDL), high-density lipoproteins (HDL2, HDL3), and egg PC/TO microemulsions at 25 degrees C, for VLDL at 40 degrees C, and for LDL at 45 degrees C. At 25 degrees C, the rate of lateral diffusion in LDL (DT = 1.4 x 10(-9) cm2/s) is an order of magnitude slower than in the HDLs (DT = 2 x 10(-8) cm2/s). At 45 degrees C, DT for LDL increases to 1.1 x 10(-8) cm2/s. In contrast, DT for VLDL increases only slightly going from 25 to 40 degrees C. The large increase in diffusion rate observed in LDL occurs over the same temperature range as the smectic to disordered phase transition of the core cholesteryl esters, and provides evidence for direct interactions between the monolayer and core. In order to prove the orientation and/or order of the phospholipid head-group, estimates of the residual chemical shift anistropy, delta sigma, have been obtained for all the lipoproteins and the microemulsions from the viscosity and field dependence of the 31P NMR line widths. For VLDL and LDL, the anisotropy is 47-50 ppm at 25 degrees C, in agreement with data from phospholipid bilayers. For the HDLs, however, significantly larger values of 69-75 ppm (HDL2) and greater than 120 ppm (HDL3) were obtained.(ABSTRACT TRUNCATED AT 250 WORDS)

show abstract

Section: Theorymentioning

confidence: 76%

Section: Discussionmentioning

confidence: 97%

Structure and motion of phospholipids in human plasma lipoproteins. A phosphorus-31 NMR study

Fenske¹,

Chana²,

Parmar³

et al. 1990

Biochemistry

Self Cite

View full text Add to dashboard Cite

show abstract

“…At these temperatures (4°C) the appearance of the lipoprotein changes. It no longer has a fluid-like appearance but rather is more solid or crystallized (2). In effect, by rapidly cooling the plasma, the redistribution of Nys is effectively minimized (data not shown).…”

Section: Methodsmentioning

confidence: 99%

Plasma Lipoprotein Distribution of Liposomal Nystatin Is Influenced by Protein Content of High-Density Lipoproteins

Cassidy

Strobel

1998

Antimicrob Agents Chemother

View full text Add to dashboard Cite

The plasma lipoprotein distribution of free nystatin (Nys) and liposomal nystatin (L-Nys) in human plasma samples with various lipoprotein lipid and protein concentrations and compositions was investigated. To assess the lipoprotein distributions of Nys and L-Nys, human plasma was incubated with Nys and L-Nys (equivalent to 20 μg/ml) for 5 min at 37°C. The plasma was subsequently partitioned into its lipoprotein and lipoprotein-deficient plasma fractions by step-gradient ultracentrifugation, and each fraction was analyzed for Nys content by high-pressure liquid chromatography. The lipid and protein contents and compositions of each fraction were determined with enzymatic kits. Following the incubation of Nys and L-Nys in human plasma the majority of Nys recovered within the lipoprotein fractions was recovered from the high-density lipoprotein (HDL) fraction. Incorporation of Nys into liposomes consisting of dimyristoylphosphatidylcholine and dimyristoylphosphatidylglycerol significantly increased the percentage of drug recovered within the HDL fraction. Furthermore, it was observed that as the amount of HDL protein decreased the amounts of Nys and L-Nys recovered within this fraction decreased. These findings suggest that the preferential distribution of Nys and L-Nys into plasma HDL may be a function of the HDL protein concentration.

show abstract

“…99 Changes in serum distribution of AmpB at 37°C compared to 25°C appear to be related to the transition temperature (between 27 and 34°C ) of lipoproteins. 126 During the transition, esterified cholesterol within the lipoprotein core exists as a disordered isotropic solution, whereas below this temperature it forms more ordered liquid crystals. 126 The core of HDL becomes less ordered at the higher temperature, thus making it easier for the AmpB molecule to associate with it.…”

Section: Amphotericinmentioning

confidence: 99%

“…126 During the transition, esterified cholesterol within the lipoprotein core exists as a disordered isotropic solution, whereas below this temperature it forms more ordered liquid crystals. 126 The core of HDL becomes less ordered at the higher temperature, thus making it easier for the AmpB molecule to associate with it. We hypothesize that the binding of AmpB to lipoproteins may have a major impact on the safety of this drug since AmpB is often administered to patients with abnormal serum cholesterol and triglyceride metabolism.…”

Section: Amphotericinmentioning

confidence: 99%

Role of Plasma Lipoproteins in Modifying the Biological Activity of Hydrophobic Drugs

Wasan

Cassidy

1998

Journal of Pharmaceutical Sciences

130

101

View full text Add to dashboard Cite

The plasma lipoprotein distribution of potential drug candidates is not commonly studied. For some hydrophobic drug candidates, attainment of similar plasma free drug levels has not been associated with uniform production of pharmacological activity in different animal species. It is well-known that plasma lipoprotein lipid profiles vary considerably between different animal species. In addition, human disease states can significantly influence plasma lipoprotein profiles, resulting in altered therapeutic outcomes. Current research has shown that lipoprotein binding of drug compounds can significantly influence not only the pharmacological and pharmacokinetic properties of the drug, but the relative toxicity as well. Elucidation of drug distribution among plasma lipoproteins is expected to yield valuable insight into factors governing the pharmacological activity and potential toxicity of the drug. This paper will present an historical perspective and summarize the latest research in the area of lipoprotein-drug interactions.

show abstract

Surface diffusion in human serum lipoproteins

Cited by 24 publications

References 12 publications

Structure and motion of phospholipids in human plasma lipoproteins. A phosphorus-31 NMR study

Structure and motion of phospholipids in human plasma lipoproteins. A phosphorus-31 NMR study

Plasma Lipoprotein Distribution of Liposomal Nystatin Is Influenced by Protein Content of High-Density Lipoproteins

Role of Plasma Lipoproteins in Modifying the Biological Activity of Hydrophobic Drugs

Contact Info

Product

Resources

About