Effect of cell ageing on Ca2+influx into human red cells

Romero, Pedro; Romero, Eneida A.

doi:10.1054/ceca.1999.0063

Cited by 52 publications

(51 citation statements)

References 23 publications

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“…1 This may be important for erythrocyte ageing, which is paralleled by increase of cytosolic Ca 2+ activity. 21,22 Moreover, according to the present results, oxidative stress or defects of antioxidative defence 23 clearly enhance Ca 2+ entry via the cation channels. This leads to higher intracellular Ca 2+ concentrations and thus accelerates erythrocyte apoptosis and clearance.…”

Section: Discussionsupporting

confidence: 75%

“…The phosphatidylserine exposure at the cell surface is thought to stimulate the uptake by macrophages. 20,21 Thus, to the extent that calcium triggers the breakdown of phosphatidylserine asymmetry, an increase of cytosolic Ca 2+ activity is expected to trigger the clearance of the affected erythrocytes. 1 This may be important for erythrocyte ageing, which is paralleled by increase of cytosolic Ca 2+ activity.…”

Section: Discussionmentioning

confidence: 99%

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Cation channels trigger apoptotic death of erythrocytes

et al. 2003

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Erythrocytes are devoid of mitochondria and nuclei and were considered unable to undergo apoptosis. As shown recently, however, the Ca 2+ -ionophore ionomycin triggers breakdown of phosphatidylserine asymmetry (leading to annexin binding), membrane blebbing and shrinkage of erythrocytes, features typical for apoptosis in nucleated cells. In the present study, the effects of osmotic shrinkage and oxidative stress, well-known triggers of apoptosis in nucleated cells, were studied. Exposure to 850 mOsm for 24 h, to tert-butylhydroperoxide (1 mM) for 15 min, or to glucose-free medium for 48 h, all elicit erythrocyte shrinkage and annexin binding, both sequelae being blunted by removal of extracellular Ca 2+ and mimicked by ionomycin (1 lM). Osmotic shrinkage and oxidative stress activate Ca 2+ -permeable cation channels and increase cytosolic Ca 2+ concentration. The channels are inhibited by amiloride (1 mM), which further blunts annexin binding following osmotic shock, oxidative stress and glucose depletion. In conclusion, osmotic and oxidative stress open Ca 2+ -permeable cation channels in erythrocytes, thus increasing cytosolic Ca 2+ activity and triggering erythrocyte apoptosis.

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Section: Discussionsupporting

confidence: 75%

Section: Discussionmentioning

confidence: 99%

Cation channels trigger apoptotic death of erythrocytes

et al. 2003

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“…The phosphatidylserine exposure at the cell surface is thought to stimulate the uptake by macrophages. 14,44 Moreover, the present study demonstrated Ca 2 þ -ionophore and PGE 2 -triggered proteolysis of ankyrin R (band 2.1), an effect paralleled by the activation of m-calpain and inhibited by calpain inhibitors I/II. These data are consistent with PGE 2 -induced ankyrin R proteolysis by the Ca 2 þ -dependent neutral endopeptidase calpain, which has been shown to degrade ankyrin R (about 215 kDa) in vitro to several cleavage products.…”

Section: -43supporting

confidence: 62%

“…4 This may be also important for erythrocyte aging, which is paralleled by an increase of cytosolic Ca 2 þ activity. 44,49 Moreover, oxidative stress or defects of antioxidative defence 50 clearly enhance Ca 2 þ entry via the cation channels. This in turn leads to higher intracellular Ca 2 þ concentrations and thus accelerates erythrocyte 'apoptosis' and clearance.…”

Section: -43mentioning

confidence: 99%

PGE2 in the regulation of programmed erythrocyte death

et al. 2005

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Hyperosmotic shock, energy depletion, or removal of extracellular Cl À activates Ca 2 þ -permeable cation channels in erythrocyte membranes. Subsequent Ca 2 þ entry induces erythrocyte shrinkage and exposure of phosphatidylserine (PS) at the erythrocyte surface. PS-exposing cells are engulfed by macrophages. The present study explored the signalling involved. Hyperosmotic shock and Cl À removal triggered the release of prostaglandin E 2 (PGE 2 ). In whole-cell recording, activation of the cation channels by Cl À removal was abolished by the cyclooxygenase inhibitor diclophenac. In FACS analysis, phospholipase-A 2 inhibitors quinacrine and palmitoyltrifluoromethyl-ketone, and cyclooxygenase inhibitors acetylsalicylic acid and diclophenac, blunted the increase of PS exposure following Cl À removal. PGE 2 (but not thromboxane) induced cation channel activation, increase in cytosolic Ca 2 þ concentration, cell shrinkage, PS exposure, calpain activation, and ankyrin-R degradation. The latter was attenuated by calpain inhibitors-I/II, while PGE 2 -induced PS exposure was not. In conclusion, hyperosmotic shock or Cl À removal stimulates erythrocyte PS exposure through PGE 2 formation and subsequent activation of Ca 2+ -permeable cation channels.

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“…However, it is well established that there is an association of increased levels of intracellular calcium with the events surrounding PS translocation in mature erythrocytes. [17][18][19] The original hypothesis by Raff et al 20 that all nucleated cells require survival signals to be maintained has been well supported Reprints: Rosemary O'Connor, Department of Biochemistry, Lee Maltings, National University of Ireland, Cork, Ireland; e-mail: r.oconnor@ucc.ie.The publication costs of this article were defrayed in part by page charge payment. Therefore, and solely to indicate this fact, this article is hereby marked ''advertisement'' in accordance with 18 U.S.C.…”

mentioning

confidence: 99%

Erythrocyte survival is promoted by plasma and suppressed by a Bak-derived BH3 peptide that interacts with membrane-associated Bcl-XL

Walsh

Lutz

Cotter

et al. 2002

Blood

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Erythrocytes have a defined lifespan in vivo, and the signals that maintain their survival in circulation or trigger their death are unknown. Here, we investigated the control of erythrocyte survival and death in an in vitro culture system where erythrocytes survived for 10 days in serumfree medium in the presence or absence of bovine serum. Death of the cells in culture was correlated with increased exposure of phosphatidylserine and increased levels of intracellular calcium. Cell death could be suppressed by supplementing the medium with human plasma or serum, resulting in a doubling of the lifespan to 20 days. Freshly isolated erythrocytes and cultured erythrocytes were both found to express Bcl-X L and, to a lesser extent, Bak in membrane protein extracts. Treatment of the cells with a Bak-derived BH3 peptide fused to the internalization sequence of the antennapedia protein, which has previously been shown to enter cells by diffusion and antagonize Bcl-X L , resulted in substantial cell death in erythrocyte cultures. BH3-induced death was accompanied by an immediate increase in accumulation of intracellular calcium and could be suppressed by plasma, but not by the caspase inhibitor zVAD. A BH3 peptide mutated at amino acid 78 of full-length Bak required for heterodimerization with Bcl-X L had no effect on cell viability or calcium levels. We conclude that the BH3 peptide accelerates erythrocyte death through antagonization of Bcl-X L . The data suggest that erythrocyte survival is promoted by survival factors in plasma and by membrane- IntroductionCell death and survival in hematopoietic cells is regulated by signals from cell-surface receptors that either promote apoptosis, such as Fas and tumor necrosis factor (TNF), or repress cell death, such as receptors for cytokines and survival factors such as erythropoietin (EPO), interleukin 3, and insulinlike growth factor I (IGF-I). [1][2][3] Ligation of the receptors for Fas/TNF can lead directly to activation of caspases, which can act as effectors of cell death by catalyzing structural changes associated with apoptosis, including cytoskeletal reorganization and DNA fragmentation. Survival factors mediate signals through several kinases, such as phosphoinositol 3 kinase and AKT, ultimately leading to transcriptional events or to regulation of Bcl-2 family proteins. 4 The Bcl-2 family acts as central regulators of cell death in many cells [5][6][7] and is divided into 2 main groups consisting of suppressors of apoptosis, including Bcl-2, Bcl-X L , Bcl-w, and Mcl-1, and potent apoptosis promoters, including Bax, Bak, Bad, and Bid. Bcl-2 and Bcl-X L survival activity can be antagonized by heterodimerization with proteins containing a BH3 domain, which is the essential domain for the binding and proapoptotic activity of Bak, Bax, Bik, and Bid. 8 Bcl-2 and Bcl-X L are expressed in outer mitochondrial membranes where antagonization of their function is associated with rupture of the membrane, release of the proapoptotic factors cytochrome c, and activation of caspas...

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Effect of cell ageing on Ca2+influx into human red cells

Cited by 52 publications

References 23 publications

Cation channels trigger apoptotic death of erythrocytes

Cation channels trigger apoptotic death of erythrocytes

PGE2 in the regulation of programmed erythrocyte death

Erythrocyte survival is promoted by plasma and suppressed by a Bak-derived BH3 peptide that interacts with membrane-associated Bcl-XL

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