The kinetics of interactions of bilirubin with lipid bilayers and with serum albumin

Noy, Noa; Leonard, Maurice; Zakim, David

doi:10.1016/0301-4622(92)85007-q

Cited by 26 publications

(15 citation statements)

References 23 publications

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“…It has been suggested that uptake of the organic anion bilirubin can be explained simply by its direct interaction with the plasma membrane lipid bilayer (24). The present studies clearly show that in the case of BSP this is not so.…”

Section: Discussioncontrasting

confidence: 43%

Stable Inducible Expression of a Functional Rat Liver Organic Anion Transport Protein in HeLa Cells

Shi

Bai

Ford

et al. 1995

Journal of Biological Chemistry

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Section: Discussioncontrasting

confidence: 43%

Stable Inducible Expression of a Functional Rat Liver Organic Anion Transport Protein in HeLa Cells

Shi

Bai

Ford

et al. 1995

Journal of Biological Chemistry

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“…Bilirubin is poorly soluble in water but readily dissolves in membranes (25). It also associates rapidly with preformed liposomes (26,27). The bilirubin liposome complex is a good substrate for B-UGT (28).…”

Section: Resultsmentioning

confidence: 99%

Discrimination between Crigler-Najjar type I and II by expression of mutant bilirubin uridine diphosphate-glucuronosyltransferase.

Bosma²,

et al. 1994

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Crigler-Najjar (CN) Kinetic constants for the glucuronidation of bilirubin were determined. The affinities for bilirubin of B-UGT1 expressed in COS cells and B-UGT from human liver microsomes were similar with Km of 5.1±0.9 ,uM and 7.9±5.3 ,uM, respectively. B-UGT1 from patient B had a tenfold decreased affinity for bilirubin, Km = 56±23 ,LM.At physiological concentrations of bilirubin both type II patients will have a strongly reduced conjugation capacity, whereas type I patients have no B-UGT activity. We conclude that CN type I is caused by a complete absence of functional B-UGT and that in CN type II B-UGT activity is reduced. (J. Clin. Invest. 1994Invest. .94:2385Invest. -2391

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“…Hydration of the lipophilic CE could represent an important, perhaps rate-limiting, step in selective uptake. By analogy to the transfer of the lipophilic bilirubin from albumin to synthetic phospholipid membranes [46], one could imagine that the overall transfer rate of CE from a donor particle (Pd9 i.e. HDL) to an acceptor particle (Pa9 i.e.…”

Section: Discussionmentioning

confidence: 99%

Greater selective uptake by Hep G2 cells of high-density lipoprotein cholesteryl ester hydroperoxides than of unoxidized cholesteryl esters

Sattler

Stocker

1993

Biochemical Journal

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We have observed recently that high-density lipoproteins (HDL) are the predominant carriers of cholesteryl ester hydroperoxides (CEOOH), the major class of lipid hydroperoxides detectable at nanomolar concentrations in the plasma of healthy fasting humans. The present study investigates the effect of such very low levels of CEOOH in apolipoprotein E-free HDL3 on lipoprotein particle metabolism and 'selective uptake' of its CE by human Hep G2 cells. Minimal oxidation with aqueous peroxyl radicals had a negligible effect on the binding, internalization and degradation of 125I-labelled HDL3. In contrast, with an increasing degree of radical-mediated oxidation of labelled HDL3, [3H]cholesteryl linoleate ([3H]Ch18:2) was taken up at an increasingly greater rate than were 125I-apoproteins. When [3H]cholesteryl linoleate hydroperoxide ([3H]Ch18:2-OOH was incorporated into unoxidized HDL3 by exchange from donor liposomes, it was taken up at a more than 8-fold higher rate than was incorporated [3H]Ch18:2. The same degree of preferential uptake of oxidized CE was observed when HDL3 was used that was doubly labelled with [3H]Ch18:2-OOH and cholesteryl [14C]oleate ([14C]Ch18:1). In both situations, uptake of [3H]Ch18:2-OOH exceeded that of 125I-apolipoprotein A-I some 40-fold. This increased selective uptake of [3H]Ch18:2-OOH from very mildly oxidized HDL3 was accompanied by a parallel increase in the intracellular levels of labelled free cholesterol. In contrast, lipid hydroperoxides were not detectable within Hep G2 cells, suggesting efficient detoxification of CEOOH by these cells. Neither the increased selective uptake of Ch18:2-OOHs nor the levels of intracellular free cholesterol were influenced by the presence of 50 microM chloroquine, suggesting extralysosomal hydrolysis of oxidized CEs. These results show that the selective uptake of HDL CEOOH by Hep G2 cells is more efficient than that of unoxidized CE, and support a protective role for rapid selective uptake in the removal of circulating HDL CEOOH.

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The kinetics of interactions of bilirubin with lipid bilayers and with serum albumin

Cited by 26 publications

References 23 publications

Stable Inducible Expression of a Functional Rat Liver Organic Anion Transport Protein in HeLa Cells

Stable Inducible Expression of a Functional Rat Liver Organic Anion Transport Protein in HeLa Cells

Discrimination between Crigler-Najjar type I and II by expression of mutant bilirubin uridine diphosphate-glucuronosyltransferase.

Greater selective uptake by Hep G2 cells of high-density lipoprotein cholesteryl ester hydroperoxides than of unoxidized cholesteryl esters

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