Dependence on heparin chain-length of the interaction of heparin with human plasma low density lipoproteins

Cardin, Alan D.; Jackson, Richard L.; Elledge, Barry; Feldhake, David

doi:10.1016/0141-8130(89)90042-1

Cited by 8 publications

(5 citation statements)

References 22 publications

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“…No relevant change is detected for the intensity of the 2'-0-sulfated iduronyl residue (=60% of total iduronic acid content). These results are consistent with the general trend reported in former studies on high LDL affinity fractions of heparin (Cardin et al, 1989;Srinivasan et al, 1991).…”

Section: Resultssupporting

confidence: 93%

“…Our data cannot rule out such a hypothesis, but strongly disfavor it. In agreement with our findings, former observations (Fransson & Havsmark, 1981;Cardin et al, 1989;Srinivasan et al, 1991) reported that high LDL affinity fractions of heparin have a higher sulfation degree and moleclar weight than the starting material. More significantly, our systematic study with wellcharacterized heparin fractions and derivatives indicates a regular dependence of LDL affinity on the heparin molecular weight and on the degree of sulfation.…”

Section: Discussionsupporting

confidence: 94%

“…The association of LDL and heparin is highly sensitive to salt concentration (Iverius, 1972) as a consequence of its electrostatic nature. This property is also exploited in the purification of heparin fractions with high LDL affinity (Cardin et al, 1989;Srinivasan et al, 1991). When the salt concentration is progressively increased in a solution with constant LDL and FRH concentrations, the fluorescence anisotropy gradually decreases (Figure 3) as a result of the dissociation of bound heparin.…”

Section: Resultsmentioning

confidence: 99%

“…In an attempt to elucidate the structural parameters which are most relevant to the LDL-heparin interaction, recent studies have focused on the isolation of high LDL affinity fractions from native heparin samples (Cardin et al, 1987(Cardin et al, , 1989Srinivasan et al, 1991). These investigations have not succeeded at identifying a well-defined, highly specific molecular structure, but have indicated a general trend of increasing affinity with increasing heparin chain length and sulfation degree.…”

mentioning

confidence: 99%

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Heparin binding to human plasma low-density lipoproteins: dependence on heparin sulfation degree and chain length

Gigli¹,

Consonni²,

Ghiselli³

et al. 1992

Biochemistry

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Binding between low-density lipoproteins (LDL) and fluorescein-labeled heparin was studied quantitatively with a modified form of a published procedure [Cardin, A. D., Randall, C. I., Hirose, N., & Jackson, R. L. (1987) Biochemistry 26, 5513-5518], using fluorescence anisotropy titrations. Assumption of binding site equivalence satisfactorily interpreted experimental data. Accordingly, the apparent total capacity, n, and the average dissociation constant, Kd, were estimated as n approximately 24 disaccharides per LDL particle and Kd approximately 4 microM in 0.05 M HEPES/0.1 M NaCl, pH 7.4, 22 degrees C. Competition experiments with unlabeled heparins were exploited for the quantitative study of Kd as a function of heparin chain length and sulfation degree (ns = sulfate groups per disaccharide). The former parameter was investigated with a series of bovine lung heparin fractions with Mw ranging from 1,800 to 21,000 and constant sulfation degree (ns = 2.8 +/- 0.1). A series of physically fractionated or chemically modified heparins having 1.2 less than ns less than 3.5 were used to explore the dependence on sulfation degree. LDL affinity was found to increase with increasing both ns and Mw: an empirical Mw-1.6 dependence represented very well the chain length data set; a linear dependence was observed for log Kd as a function of ns, after appropriate allowance was made for chain length differences among samples. This regularity confirmed that LDL-heparin binding is mainly driven by electrostatic forces.(ABSTRACT TRUNCATED AT 250 WORDS)

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Section: Resultssupporting

confidence: 93%

Section: Discussionsupporting

confidence: 94%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

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Heparin binding to human plasma low-density lipoproteins: dependence on heparin sulfation degree and chain length

Gigli¹,

Consonni²,

Ghiselli³

et al. 1992

Biochemistry

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“…An antilipemic activity of heparins has been known for long and is attributed to its ability to competes with proteoglycans on the arterial walls [29] for LDL uptake [30]. Our data show that a single injection of 5 mg/kg of SSLMWH-19 caused a minor nonsignificant decrease in the triglycerides levels of the mice.…”

Section: Sslmwh-19 Reduces Triglyceride Levels In Micementioning

confidence: 63%

Oversulfated heparins with low anticoagulant activity are strong and fast inhibitors of hepcidin expression in vitro and in vivo

Poli¹,

Asperti²,

Ruzzenenti³

et al. 2014

Biochemical Pharmacology

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Ca2+-Mediated Interaction between Dextran Sulfate and Dimyristoyl-sn-Glycero-3-Phosphocholine Surfaces Studied by 2H Nuclear Magnetic Resonance

Huster

Arnold

1998

Biophysical Journal

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The binding of dextran sulfates (DSs) with varying chain lengths to phosphatidylcholine multilamellar vesicles was investigated as a function of polyelectrolyte, NaCl, and Ca2+ concentration. Attractive forces between negatively charged polyelectrolytes and zwitterionic phospholipids arise from the assembly of calcium bridges. The formation of calcium bridges between the sulfate groups on the dextran sulfate and the phosphate group of the lipid results in increased calcium binding in mixtures of DS and 1, 2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC). At high NaCl concentration, the plateau adsorption of DS 500 is increased. The strength of dextran sulfate binding to DMPC is reflected in the changes of the 2H NMR quadrupolar splittings of the headgroup methylenes. Association forces increase with the number of calcium bridges formed. Low-molecular-weight DS does not bind to DMPC surfaces whereas longer-chain DSs strongly influence headgroup structure as a result of strong association. DS binding increases with increasing concentration; however, further association of the polyelectrolyte can be promoted only if negative charges are sufficiently screened. DS binding to lipid bilayers is a complicated balance of calcium bridging and charge screening. From our data we postulate that the structure of the adsorbed layer resembles a lattice of DS strands sandwiched between the bilayer lamellae.

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Dependence on heparin chain-length of the interaction of heparin with human plasma low density lipoproteins

Cited by 8 publications

References 22 publications

Heparin binding to human plasma low-density lipoproteins: dependence on heparin sulfation degree and chain length

Heparin binding to human plasma low-density lipoproteins: dependence on heparin sulfation degree and chain length

Oversulfated heparins with low anticoagulant activity are strong and fast inhibitors of hepcidin expression in vitro and in vivo

Ca2+-Mediated Interaction between Dextran Sulfate and Dimyristoyl-sn-Glycero-3-Phosphocholine Surfaces Studied by 2H Nuclear Magnetic Resonance

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