The interaction of spectrin · actin and synthetic phospholipids

Mombers, C.; Dijck, P.W.M. Van; Deenen, L.L.M. Van; Gier, J. De; Verkleij, Arie J.

doi:10.1016/0005-2736(77)90096-7

Cited by 62 publications

(25 citation statements)

References 21 publications

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“…In the native membrane an interaction between spectrin and phosphatidylserine may interfere with this lateral separation of lipids which is induced by environmental conditions and may prevent the aggregation of the particles. A clear interaction between spectrin and phosphatidylserine has been shown recently [24], whereas less interaction was detected with phosphatidylcholine [23] and phosphatidylethanolamine (Mombers, C., unpublished results). Phase separations in mixtures of phosphatidylserine and phosphatidylcholine were found to be reduced by the presence of spectrin [24].…”

Section: Discussionmentioning

confidence: 66%

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The lateral distribution of intramembrane particles in the erythrocyte membrane and recombinant vesicles

Gerritsen

Verkleij

Deenen

1979

Biochimica et Biophysica Acta (BBA) - Biomembranes

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SummaryTriton X-100 (in concentrations which did not cause a significant solubilization of membrane material) caused aggregation of the intramembrane particles of human erythrocyte ghosts.Ghosts from which the extrinsic proteins had been removed by alkali treatment showed a temperature-induced aggregation of the particles. With virtually no spectrin present, the particles in these stripped ghosts could still be aggregated by manipulations with ionic strength and pH, or by the addition of calcium.Recombinant vesicles were made from a Triton X-100 extract and a mixture of phospholipids with a composition which resembled that of the inner monolayer of erythrocyte membrane. In these recombinants the same manipulations with ionic strength and pH and the addition of calcium caused a rearrangement of the particles, resulting in the appearance of particle-free areas. In recombinants prepared from a Triton X-100 extract and egg phosphatidylcholine the lateral distribution of the particles was not altered by these manipulations.It is concluded that in the erythrocyte membrane the intramembrane particles can be aggregated by effects of external agents on lipid components. In this light the role of spectrin in stabilizing the membrane by interactions with lipids in the inner monolayer is discussed.

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Section: Discussionmentioning

confidence: 66%

“…Cross-linking studies have suggested a structural linkage between the spectrin-actin network and band 3 [22]. Spectrin-actin was also shown to interact with negatively charged phospholipids [23,24], and perturbation of spectrin by oxidizing agents was correlated with changes in the arrangement of phospholipids in the membrane [ 25].…”

Section: Introductionmentioning

confidence: 99%

The lateral distribution of intramembrane particles in the erythrocyte membrane and recombinant vesicles

Gerritsen

Verkleij

Deenen

1979

Biochimica et Biophysica Acta (BBA) - Biomembranes

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“…The prevention of apparent fusion complexes by the insertion of spectrin into Sph membranes is of considerable interest. Previous studies in liposome model systems have shown similar effects of spectrin (27,43). Perhaps a spectrin meshwork prevents the formation of large protein-free lipid regions, or domains, necessary for fusion.…”

Section: Resultsmentioning

confidence: 74%

“…Because the cells of this mouse are extraordinarily unstable, a membrane-stabilizing role, as well as a shape-control role, has also been proposed for this molecule (26). The demonstration of spectrin-lipid interactions in purified liposome systems (27), of an apparent effect of spectrin in regulating the phospholipid assymetry of the membrane (28), and spectrin's known interactions with actin (29,30), as well as its probable interactions with intermembranous particles and internal membrane proteins (6), all suggest mechanistic possibilities for these roles and lend credence to this view.…”

Section: Introductionmentioning

confidence: 99%

Reconstitution of spectrin-deficient, spherocytic mouse erythrocyte membranes.

Shohet¹

1979

J. Clin. Invest.

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A B S T R A C T To study directly the role of spectrin in erythrocyte membrane function, we have designed a reconstituted membrane system using erythrocyte membranes from spectrin-deficient mice and purified spectrin from normal mice. The normal spectrin is inserted into the spectrin-deficient spherocytes by exchange hemolysis. Thereafter, raising the ionic strength and temperature reseals the cells and, with time, facilitates binding of the spectrin to the spectrindeficient membranes. The binding is apparently specific as shown by its dependence upon the concentration of undenatured spectrin and the concentration of salt used, as well as by the immunofluorescent appearance of the reconstituted cells after treatment with specific antispectrin antibody.In terms of in vitro cellular behavior, the reconstituted preparations show marked changes in comparison to the untreated spherocytes. In particular, membrane stability, as measured by the reduction of myelin figure formation and lipid loss, is considerably enhanced. In addition, membrane fusion, which occurs readily with the untreated spherocytes, is virtually eliminated. Finally, the osmotic behavior of the native spherocytes is appreciably altered, such that the early phase of osmotically induced swelling, as measured in a highspeed stop-flow apparatus, is delayed and modified.Taken together, these findings indicate specific roles for spectrin in the stabilization of the erythrocyte membrane, in the limitation of membrane fusion, and in the modulation of the membrane's response to osmotic stress.

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“…To date, ankyrin-integral membrane protein interactions appear to involve a common site on the ankyrin molecule (since the cytoplasmic domain of Burns, 19881. This emerging class of proteins has been termed "amphitropic proteins" in recognition of their dual (soluble cytoplasmic and membrane bound) nature [Burns, 19881. Erythroid spectrin has been shown to interact directly with phospholipids in vitro [Mombers et al, 1979;Bonnet and Begard, 1984;Sikorski et al, 19871. In several model systems spectrin penetrates both unilamellar and multilamellar liposomes [Sweet and Zull, 1970;Mombers et al, 19801 and specifically interacts with phosphatidylserine and phosphatidylethanol-amine [Cohen et al, 19861. In addition to direct phospholipid interactions with spectrin, spectrin binding proteins may be mediators of spectrin-phospholipid interactions. For example, mammalian erythroid protein 4.1 [Keenan and Heid, 19821 and both avian [Staufenbiel and Lazarides, 19861 and mammalian [Staufenbiel, 19871 erythroid ankyrin have been shown to be fatty acid acylated; this covalently attached fatty acid may permit a direct interaction of ankyrin or protein 4.1 with the membrane.…”

Section: Spectrin-an Kyrin-voltage-dependent Sodium Channelmentioning

confidence: 99%

Functional diversity among spectrin isoforms

Coleman

Fishkind

Mooseker

et al. 1989

Cell Motil. Cytoskeleton

115

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The purpose of this review on spectrin is to examine the functional properties of this ubiquitous family of membrane skeletal proteins. Major topics include spectrin-membrane linkages, spectrin-filament linkages, the subcellular localization of spectrins in various cell types and a discussion of major functional differences between erythroid and nonerythroid spectrins. This includes a summary of studies from our own laboratories on the functional and structural comparison of avian spectrin isoforms which are comprised of a common alpha subunit and a tissue-specific beta subunit. Consequently, the observed differences among these spectrins can be assigned to differences in the properties of the beta subunits.

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The interaction of spectrin · actin and synthetic phospholipids

Cited by 62 publications

References 21 publications

The lateral distribution of intramembrane particles in the erythrocyte membrane and recombinant vesicles

The lateral distribution of intramembrane particles in the erythrocyte membrane and recombinant vesicles

Reconstitution of spectrin-deficient, spherocytic mouse erythrocyte membranes.

Functional diversity among spectrin isoforms

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