Spectrin as a stabilizer of the phospholipid asymmetry in the human erythrocyte membrane

Haest, C.W.M.; Plasa, G.; Kamp, D.; Deüticke, B.

doi:10.1016/0005-2736(78)90004-4

Cited by 343 publications

(133 citation statements)

References 31 publications

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“…52 Spectrin plays an important role for the integrity and typical discocyte form of RBCs. 53 Conversely, damage of spectrin and other cytoskeletal proteins has been implicated in the externalization of phosphatidylserine, membrane budding and the characteristic spherical shape of aging erythrocytes. It is interesting to note that calpains but not caspases are also involved in platelet activation which, similar to erythrocyte senescence, displays apoptosis-like morphological alterations including cell shrinkage, microvesiculation and phosphatidylserine exposure.…”

Section: Discussionmentioning

confidence: 99%

Human mature red blood cells express caspase-3 and caspase-8, but are devoid of mitochondrial regulators of apoptosis

et al. 2001

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Although proteases of the caspase family are essential mediators of apoptosis in nucleated cells, in anucleate cells their presence and potential functions are almost completely unknown. Human erythrocytes are a major cell population that does not contain a cell nucleus or other organelles. However, during senescence they undergo certain morphological alterations resembling apoptosis. In the present study, we found that mature erythrocytes contain considerable amounts of caspase-3 and -8, whereas essential components of the mitochondrial apoptotic cascade such as caspase-9, Apaf-1 and cytochrome c were missing. Strikingly, although caspases of erythrocytes were functionally active in vitro, they failed to become activated in intact erythrocytes either during prolonged storage or in response to various proapoptotic stimuli. Following an increase of cytosolic calcium, instead the cysteine protease calpain but not caspases became activated and mediated fodrin cleavage and other morphological alterations such as cell shrinkage. Our results therefore suggest that erythrocytes do not have a functional death system. In addition, because of the presence of procaspases and the absence of a cell nucleus and mitochondria erythrocytes may be an attractive system to dissect the role of certain apoptosis-regulatory pathways. Cell Death and Differentiation (2001) 8, 1197 ± 1206.

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Section: Discussionmentioning

confidence: 99%

Human mature red blood cells express caspase-3 and caspase-8, but are devoid of mitochondrial regulators of apoptosis

et al. 2001

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“…Indeed, in chicken erythrocytes dephosphorylation of membrane proteins, including spectrin, has been correlated with aggregation of the intramembrane particles and with increased exposure of phosphatidylethanolamine at the outer face of the membrane [57]. In human erythrocytes modification of sulfhydryl groups of spectrin has been associated with a movement of phosphatidylethanolamine and phosphatidylserine to the outer layer of the membrane [25]. Both ATP depletion and increased levels of calcium at the inner monolayer have been shown to cause increased fusion [58,59] and the release of vesicles [60--63].…”

Section: Discussionmentioning

confidence: 99%

“…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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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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“…A direct interaction is not out of the question, for spectrin is evidently capable of some association with phospholipids, and in particular the inner leaflet constituent, phosphatidylserine; there are, moreover, indications of a sort that such an interaction in situ may indeed stabilize the bilayer in respect of phospholipid flip-flop and the tendency towards fusion (Haest et al, 1978;Gerritsen et al, 1979).…”

mentioning

confidence: 99%

The red cell membrane and its cytoskeleton

Gratzer¹

1981

Biochemical Journal

127

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Spectrin as a stabilizer of the phospholipid asymmetry in the human erythrocyte membrane

Cited by 343 publications

References 31 publications

Human mature red blood cells express caspase-3 and caspase-8, but are devoid of mitochondrial regulators of apoptosis

Human mature red blood cells express caspase-3 and caspase-8, but are devoid of mitochondrial regulators of apoptosis

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

The red cell membrane and its cytoskeleton

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