Transmembrane diffusion of fluorescent phospholipids in human erythrocytes

Colleau, Martine; Hervé, P.; Fellmann, Pierre; Devaux, Philippe F.

doi:10.1016/0009-3084(91)90046-e

Cited by 110 publications

(67 citation statements)

References 33 publications

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“…This time depends strongly on the molecular phosphatidylcholine species (Fujii et al, 1986;Middlekoop et al, 1986; Meer et al, 1982) and on the membrane sphingomyelin and cholesterol contents (Bergmann et al, 1984;Morrot et al, 1989). Similar data have been reported in the plasma membranes of erythrocytes belonging to other species Crain and Zilversmit, 1980;Devaux et al, 1988) and with cultured cells (Sandra and Pagano, 1978 Bitbol and Devaux, 1988;Calvez et al, 1988;Morrot et al, 1989 Long-chain, diacyl 8-10 min Huestis, 1985, 1989;Tilley et al, 1986 Fluorescent (NBD) 10-30 min Colleau et al, 1991;Schroit, 1987, 1989 (Venien and Le Grimellec, 1988). Passive diffusion also exists in some intracellular membranes, such as bovine chromaffin granules or inner mitochondrial membranes (Rousselet et al, 1976a).…”

Section: Mechanism Of Transbilayer Migration Passive Diffusionmentioning

confidence: 64%

“…In the case of erythrocytes, whose shape is sensitive to the relative amount of lipid in each of the two membrane leaflets according to the bilayer-couple hypothesis (Deuticke, 1968;Sheetz and Singer, 1974), these changes ( Figure 3) have also been used to follow the transmembrane motion of lipids (Daleke and Huestis, 1985;. All the assays have given comparable results, with the exception of those performed with certain fluorescent short-chain phospholipids which proved to be poor analogues of their endogenous counterparts (Colleau et al, 1991). These measurements have allowed three types of transmembrane movements to be described.…”

Section: Transmembrane Motion Assaysmentioning

confidence: 99%

“…Long-chain lipids (Tilley et al, 1986) and lipids with a short 4-(doxyl)-pentanoyl chain (Morrot et al, 1989) exhibit similar transport kinetics, indicating that the nature of the chain is not very important. However, the presence in sn-2 of a (6-NBD)-caproyl chain decreased the affinity for phosphatidylserine by one order of magnitude and prevented phosphatidylethanolamine from being recognized (Colleau et al, 1991). This abnormal behaviour is no longer found when the fluorescent fatty acid is a dodecanoyl one (Connor et al, 1992 ; as Rh protein does not contain ATPbinding sites, this peptide has to be associated with an ATPutilizing protein (Schroit and Zwaal, 1991).…”

Section: Facilitated Diffusionmentioning

confidence: 99%

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Phospholipids in animal eukaryotic membranes: transverse asymmetry and movement

Zachowski

1993

Biochemical Journal

780

565

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Section: Mechanism Of Transbilayer Migration Passive Diffusionmentioning

confidence: 64%

Section: Transmembrane Motion Assaysmentioning

confidence: 99%

Section: Facilitated Diffusionmentioning

confidence: 99%

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Phospholipids in animal eukaryotic membranes: transverse asymmetry and movement

Zachowski

1993

Biochemical Journal

780

565

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“…The experiments carried out by Tanaka and Schroit in which PS-enriched red cells were recognized by macrophages (22), required on the order of 2% of exogenous phospholipids initially located in the outer leaflet. However, since the fluorescent PS derivatives used in these experiments are substrate of the aminophospholipid translocase (50), the actual number of PS molecules recognized by the macrophages in Tanaka and Schroit's experiment are likely to have been below 2% of the total phospholipids in the outer leaflet.…”

Section: Resultsmentioning

confidence: 97%

Transbilayer mobility and distribution of red cell phospholipids during storage.

Geldwerth¹,

Kuypers²,

Bütikofer³

et al. 1993

J. Clin. Invest.

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We studied phospholipid topology and transbilayer mobility in red cells during blood storage. The distribution of phospholipids was determined by measuring the reactivity of phosphatidylethanolamine with fluorescamine and the degradation of phospholipids by phospholipase A2 and sphingomyelinase C. Phospholipid mobility was measured by determining transbilayer movements of spin-labeled phospholipids. We were unable to detect a change in the distribution of endogenous membrane phospholipids in stored red cells even after 2-mo storage. The rate of inward movement of spin-labeled phosphatidylethanolamine and phosphatidylserine was progressively reduced, whereas that for phosphatidylcholine was increased. These changes in phospholipid translocation correlated with a fall in cellular ATP. However, following restoration of ATP, neither the rate of aminophospholipid translocation nor the transbilayer movement of phosphatidylcholine were completely corrected. Taken together, our findings demonstrate that red cell storage alters the kinetics of transbilayer mobility of phosphatidylserine, phosphatidylethanolamine, and phosphatidylcholine, the activity of the aminophospholipid translocase, but not the asymmetric distribution ofendogenous membrane phospholipids, at least at a level detectable with phospholipases.

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“…PC is a cylindrical lipid with a low tendency to flip across membranes, with a half-time of days in model membranes. Indeed, using natural PC (7)(8)(9) or spin-labeled and fluorescent (C 6 -NBD-) short chain PCs (10,11), typical half-times for inward translocation have been reported of hours (as compared with minutes for PS) in the erythrocyte membrane as a model plasma membrane. Still, in some cells the short chain PCs displayed rapid inward translocation (12) in an ATP-dependent and N-ethylmaleimide-sensitive manner (13), as they do in yeast (4,14).…”

mentioning

confidence: 99%

Natural Phosphatidylcholine Is Actively Translocated across the Plasma Membrane to the Surface of Mammalian Cells

Kälin

Fernandes

Hrafnsdóttir

et al. 2004

Journal of Biological Chemistry

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The cell surface of eukaryotic cells is enriched in choline phospholipids, whereas the aminophospholipids are concentrated at the cytosolic side of the plasma membrane by the activity of one or more P-type ATPases. Lipid translocation has been investigated mostly by using short chain lipid analogs because assays for endogenous lipids are inherently complicated. In the present paper, we optimized two independent assays for the translocation of natural phosphatidylcholine (PC) to the cell surface based on the hydrolysis of outer leaflet phosphoglycerolipids by exogenous phospholipase A 2 and the exchange of outer leaflet PC by a transfer protein. We report that PC reached the cell surface in the absence of vesicular traffic by a pathway that involved translocation across the plasma membrane. In erythrocytes, PC that was labeled at the inside of the plasma membrane was translocated to the cell surface with a half-time of 30 min. This translocation was probably mediated by an ATPase, because it required ATP and was vanadate-sensitive. The inhibition of PC translocation by glibenclamide, an inhibitor of various ATP binding cassette transporters, and its reduction in erythrocytes from both Abcb1a/1b and Abcb4 knockout mice, suggest the involvement of ATP binding cassette transporters in natural PC cell surface translocation. The relative importance of the outward translocation of PC as compared with the well characterized fast inward translocation of phosphatidylserine for the overall asymmetric phospholipid organization in plasma membranes remains to be established.The distribution of lipids across the eukaryotic plasma membrane bilayer is asymmetric with the choline phospholipids sphingomyelin and phosphatidylcholine (PC) 1 at the cell surface and the aminophospholipids phosphatidylserine (PS) and phosphatidylethanolamine (PE) at the inside (1, 2). PS and PE are continuously translocated from the exoplasmic to the cytoplasmic leaflet of cellular membranes by proteins belonging to a subfamily of P-type ATPases (3, 4). Inward translocation of PS is essential to prevent PS cell surface signaling, which induces blood coagulation and serves as a signal for cell-cell recognition, e.g. the removal of apoptotic cells by macrophages. An additional function of lipid translocation has emerged recently. Evidence from mammalian and yeast cells suggests that ATP-dependent inward translocation of phospholipids by the aminophospholipid translocase affects membrane curvature and is a, or the, driving force for the formation of endocytic vesicles at the plasma membrane (4 -6). The fact that yeast expresses five P-type ATPase family members in different compartments of the exocytic and endocytic transport pathways suggests the possibility that all membrane budding from sphingolipid-and cholesterol-rich membranes depends on the mass translocation of membrane phospholipids.The bulk membrane phospholipid in mammalian cells is PC, which constitutes 25-50 mol % of the membrane lipids. However, it is unclear if cells possess mechanisms for ...

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Transmembrane diffusion of fluorescent phospholipids in human erythrocytes

Cited by 110 publications

References 33 publications

Phospholipids in animal eukaryotic membranes: transverse asymmetry and movement

Phospholipids in animal eukaryotic membranes: transverse asymmetry and movement

Transbilayer mobility and distribution of red cell phospholipids during storage.

Natural Phosphatidylcholine Is Actively Translocated across the Plasma Membrane to the Surface of Mammalian Cells

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