Surface-core correlations in serum lipoproteins

Herak, Janko N.; Pifat, Greta; Brnjas-Kraljević, Jasminka; Knipping, Gabriele; Jürgens, Günther

doi:10.1007/bf01121912

Cited by 10 publications

(3 citation statements)

References 17 publications

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“…These studies, however, do not rule out a minor role for acidic groups on LDL participating with acidic groups on heparin bridged through Ca2+. This mechanism would be consistent with reports that calcium and other ions bind to the LDL surface (Herak et al, 1984) and to heparin (Lerner & Torchia, 1986) . In addition to heparin neutralizing protein positive charges, Ca2+ may neutralize negative charges on LDL and bound heparin, resulting in a complex with reduced surface charge.…”

Section: Discussionsupporting

confidence: 93%

Physical-chemical interaction of heparin and human plasma low-density lipoproteins

Cardin¹,

Randall²,

Hirose³

et al. 1987

Biochemistry

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This study characterizes the physical-chemical interactions of heparin with human plasma low-density lipoproteins (LDL). A high reactive heparin (HRH) specific for the surface determinants of LDL was isolated by chromatography of commercial bovine lung heparin on LDL immobilized to AffiGel-10. HRH was derivatized with fluoresceinamine and repurified by affinity chromatography, and its interaction with LDL in solution was monitored by steady-state fluorescence polarization. Binding of LDL to fluoresceinamine-labeled HRH (FL . HRH) was saturable, reversible, and specific; HRH stoichiometrically displaced FL . HRH from the soluble complex, and acetylation of lysine residues on LDL blocked heparin binding. Titration of FL.HRH with excess LDL yielded soluble complexes with two LDL molecules per heparin chain (Mr 13,000) characterized by an apparent Kd of 1 microM. Titration of LDL with excess HRH resulted in two classes of heparin binding with two and five heparin molecules bound per LDL and apparent Kd values of 1 and 10 microM, respectively. At physiological pH and ionic strength, the soluble HRH-LDL complexes were maximally precipitated with 20-50 mM Ca2+. Insoluble complexes contained 2-10 HRH molecules per LDL with the final product stoichiometry dependent on the ratio of the reactants. The affinity of HRH for LDL in the insoluble complexes was estimated between 1 and 10 microM. Insoluble LDL-heparin complexes were readily dissociated with 1.0 M NaCl, and their formation was prevented by acetylation of the lysine residues on LDL.

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Section: Discussionsupporting

confidence: 93%

Physical-chemical interaction of heparin and human plasma low-density lipoproteins

Cardin¹,

Randall²,

Hirose³

et al. 1987

Biochemistry

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“…The substrate specificity of human LDL and pig LDL-1 was comparable. This is not astonishing, since both fractions have many characteristics in common (Jackson et al, 1976;Jurgens et al, 1981;Herak et al, 1984). In contrast, pig LDL-2 produced slightly, but significantly, higher esterification rates than LDL-1.…”

Section: Discussionmentioning

confidence: 92%

Studies on the substrate specificity of human and pig lecithin:cholesterol acyltransferase: role of low-density lipoproteins

Knipping¹,

Birchbauer²,

Steyrer³

et al. 1986

Biochemistry

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The substrate properties of low-density lipoprotein (LDL) fractions from human and pig plasma and of lipoprotein a [Lp(a)] upon incubation with either pig or human lecithin:cholesterol acyltransferase (LCAT, EC 2.3.1.43) were investigated and compared with those of pig high-density lipoproteins (HDL) or human HDL-3. The cholesterol esterification using purified native pig LDL-1, human LDL, or Lp(a) as a substrate was approximately 36-42% that of pig HDL or human HDL-3, while cholesteryl ester formation with pig LDL-2 was 41-47%. No significant difference was found in the substrate activity between pig HDL and human HDL-3, and between human LDL and Lp(a), respectively. After depletion of pig LDL-1, pig LDL-2, and human LDL from apolipoprotein A-I (apoA-I), cholesteryl ester formation decreased to about 22-28% of the value found with pig HDL. Depletion of human LDL from apolipoprotein E (apoE) did not result in significantly different esterification rates in comparison to native LDL. Total removal of non-apoB proteins from human LDL resulted in esterification rates of approximately 10-15% that of HDL. Readdition of apoA-I to all these LDL fractions produced solely in apoA-I-depleted LDL fractions an increase of cholesteryl ester formation, whereas in those LDL fractions that were additionally depleted from apoE and/or from apoC polypeptides, a further decrease in the esterification rate occurred.(ABSTRACT TRUNCATED AT 250 WORDS)

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“…= 0.5–1.1 kcal/mol) 15. No phase transitions in the range 10–40°C were recorded in HDL core 15, 42, 43.…”

Section: Discussionmentioning

confidence: 87%

Anomalous change of viscosity and conductivity in blood plasma lipoproteins in the physiological temperature range

Kunitsyn¹,

Панин²,

Polyakov³

2001

Int. J. Quantum Chem.

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Study on temperature dependencies of viscosity (η) and conductivity (σ) of blood lipoproteins [high‐density lipoprotein (HDL), low‐density lipoprotein (LDL), and very low density lipoprotein (VLDL)] and A‐I apolipoprotein (human and rats) has revealed the presence of the anomalous region at temperature 35–38±0.5°C (Tc). Transition width is 2°C. Viscous flow enthalpy, activation energy (ΔH), and transition enthalpy (ΔHtrans.) as well as thermal coefficients Δη/ΔT and Δσ/ΔT on either side of Tc have been calculated. Transition heat is very low in human HDL, VLDL and apoA‐I, and in LDL it is higher by a factor of 4–5. Some mechanisms of the cortisol interaction with HDL and apoA‐I have been studied by infrared (IR) spectroscopy and conductometry. The hormone has been found to strengthen the tangle → α‐helixes and tangle → β‐structures transitions and increase the ordering of lipids. Therewith, ΔHtrans. rises markedly (13 and more times), and at the same time the anomalous region is shifted by 1–2°C in apoA‐I. The anomalous change of viscosity and conductivity in the physiological temperature range for all lipoprotein fractions and apoA‐I seems to be due to the structural phase transition in both proteins and lipids. In view of the heat capacity jump and a low value of ΔHtrans. in human HDL, one may assume the phospholipids of these particles to exhibit the orientation transition of smectic A↔C type, which is assigned to the second type of phase transition. The structural transition into apoA‐I is likely to contain the elements of phase transition of the first and second types. In human and rat VLDL, the smectic → cholesteric phase transition seems to occur. Enthalpy of viscous flow and structural transition in VLDL is higher for rats than for human. The pH shift of the medium to the neutral region (pH 6.1) results in shifting the anomalous region by 1–2°C. © 2001 John Wiley & Sons, Inc. Int J Quant Chem 81: 348–369, 2001

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Surface-core correlations in serum lipoproteins

Cited by 10 publications

References 17 publications

Physical-chemical interaction of heparin and human plasma low-density lipoproteins

Physical-chemical interaction of heparin and human plasma low-density lipoproteins

Studies on the substrate specificity of human and pig lecithin:cholesterol acyltransferase: role of low-density lipoproteins

Anomalous change of viscosity and conductivity in blood plasma lipoproteins in the physiological temperature range

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