Suicidal Death of Erythrocytes Due to Selenium-Compounds

Sopjani, Mentor; Föller, Michael; Gulbins, Erich; Läng, Florian

doi:10.1159/000185452

Cited by 43 publications

(21 citation statements)

References 95 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Some of these diseases may cause eryptosis by stimulating the formation of hemin. Furthermore, several eryptosis-triggering xenobiotics and endogeneous substances have been identified, such as cordycepin [50], methylglyoxal [54], amyloid peptides [53], lipopetides [71] retinoic acid [55], paclitaxel [44], amantadine [23], chlorpromazine [1], ciglitazone [58], cyclosporine [56], Bay-5884 [65], curcumin [4], valinomycin [64], listeriolysin [25], aluminum [57], copper [46], bismuth [13], tin [52], cadmium [68], selenium [67], vanadate [27], gold [69], and arsenic [51]. At least in theory, some of those substances may be effective through stimulation of hemin formation.…”

Section: Discussionmentioning

confidence: 99%

Hemin-induced suicidal erythrocyte death

2009

Self Cite

View full text Add to dashboard Cite

Several diseases, such as malaria, sickle cell disease, and ischemia/reperfusion may cause excessive formation of hemin, which may in turn trigger hemolysis. A variety of drugs and diseases leading to hemolysis triggers suicidal erythrocyte death or eryptosis, i.e., cell membrane scrambling and cell shrinkage. Eryptosis is elicited by increased cytosolic Ca 2+ activity and by ceramide. The present study explored whether hemin stimulates eryptosis. Cell membrane scrambling was estimated from annexin Vbinding to phosphatidylserine exposed at the cell surface, cell shrinkage from forward scatter in fluorescence-activated cell sorter analysis, cytosolic Ca 2+ activity from Fluo3 fluorescence and ceramide formation from fluorescencelabeled antibody binding. Exposure to hemin (1-10 μM) within 48 h significantly increased annexin V-binding, decreased forward scatter, increased cytosolic Ca 2+ activity, and stimulated ceramide formation. In conclusion, hemin stimulates suicidal cell death, which may in turn contribute to the clearance of circulating erythrocytes and thus to anemia.

show abstract

Section: Discussionmentioning

confidence: 99%

Hemin-induced suicidal erythrocyte death

2009

Self Cite

View full text Add to dashboard Cite

show abstract

“…Eryptosis may further be stimulated by ceramide (acylsphingosine) [76], prostaglandin E 2 [64], platelet activating factor [92], anti-A IgG antibodies [93], hemolysin from Vibrio parahaemolyticus [94], listeriolysin [95], paclitaxel [96], amantadine [97], azathioprine [98], amiodarone [99], retinoic acid [100], ciglitazone [101], chlorpromazine [58], peptidoglycan [102], cyclosporine [60], methylglyoxal [59], amyloid peptides [103], anandamide [104], Bay-Y5884 [105], curcumin [106], arsenic [107], methyldopa [108], valinomycin [109], aluminium [110], mercury [111], lead [112], gold [113], selenium [114], vanadium [115], cadmium [116], tin [117], and copper [118].…”

Section: Suicidal Erythrocyte Deathmentioning

confidence: 99%

Suicide for Survival - Death of Infected Erythrocytes as a Host Mechanism to Survive Malaria

Föller

Bobbala²,

Koka³

et al. 2009

Cell Physiol Biochem

Self Cite

154

161

View full text Add to dashboard Cite

The pathogen of malaria, Plasmodium, enters erythrocytes and thus escapes recognition by the immune system. The pathogen induces oxidative stress to the host erythrocyte, which triggers eryptosis, the suicidal death of erythrocytes. Eryptosis is characterized by cell shrinkage, membrane blebbing and cell membrane phospholipid scrambling with phosphatidylserine exposure at the cell surface. Phosphatidylserine-exposing erythrocytes are identified by macrophages which engulf and degrade the eryptotic cells. To the extent that infected erythrocytes undergo eryptosis prior to exit of Plasmodiaand subsequent infection of other erythrocytes, the premature eryptosis may protect against malaria. Accordingly, any therapeutical intervention accelerating suicidal death of infected erythrocytes has the potential to foster elimination of infected erythrocytes, delay the development of parasitemia and favorably influence the course of malaria. Eryptosis is stimulated by a wide variety of triggers including osmotic shock, oxidative stress, energy depletion and a wide variety of xenobiotics. Diseases associated with accelerated eryptosis include sepsis, haemolytic uremic syndrome, malaria, sickle-cell anemia, beta-thalassemia, glucose-6-phosphate dehydrogenase (G6PD)-deficiency, phosphate depletion, iron deficiency and Wilson’s disease. Among the known stimulators of eryptosis, paclitaxel, chlorpromazine, cyclosporine, curcumin, PGE₂ and lead have indeed been shown to favourably influence the course of malaria. Moreover, sickle-cell trait, beta-thalassemia trait, glucose-6-phosphate dehydrogenase (G6PD)-deficiency and iron deficiency confer some protection against a severe course of malaria. Importantly, counteracting Plasmodia by inducing eryptosis is not expected to generate resistance of the pathogen, as the proteins involved in suicidal death of the host cell are not encoded by the pathogen and thus cannot be modified by mutations of its genes.

show abstract

“…Moreover, eryptosis may be triggered by a wide variety of endogeneous substances and xenobiotics, such as antiA IgG antibodies [24], cordycepin [25], hemin [26], amiodarone [27], methylglyoxal [28], amyloid peptides [29], anandamide [30], lipopetides [31] retinoic acid [32], paclitaxel [33], amantadine [34], chlorpromazine [35], ciglitazone [36]. cyclosporine [37], Bay-5884 [38], curcumin [39], valinomycin [40], listeriolysin [41], aluminium [42], bismuth [43], mercury [44], copper [23], cadmium [45], selenium [46], vanadate [47], gold [48] and arsenic [49]. Inhibitors of eryptosis include caffeine [50].…”

Section: Introductionmentioning

confidence: 99%

Inhibitory Effect of Thymol on Suicidal Erythrocyte Death

Mahmud

Mauro²,

Föller

et al. 2009

Cell Physiol Biochem

Self Cite

View full text Add to dashboard Cite

The antibacterial plant component thymol has antioxidant activity. Oxidative stress is known to activate Ca²⁺-permeable cation channels with subsequent Ca²⁺ entry, activation of Ca²⁺-sensitive K⁺ channels, cell shrinkage, cell membrane scrambling and phosphatidylserine exposure at the erythrocyte surface. Cell shrinkage and phosphatidylserine exposure are typical features of suicidal erythrocyte death or eryptosis. Eryptotic cells are cleared from circulating blood thus causing anemia and may adhere to the vascular wall thus interfering with the microcirculation. The present experiments explored whether thymol interacts with eryptosis. Annexin V-binding was utilized to determine phosphatidylserine exposure, forward scatter to detect alterations of cell volume and Fluo3 fluorescence to depict changes of the cytosolic Ca²⁺ activity. Oxidative stress (30 min. 0.3 mM tert-butylhydroperoxide), energy depletion (48 h glucose removal) and isotonic cell shrinkage (48 h replacement of extracellular Cl^- with gluconate) significantly increased annexin V-binding and decreased the forward scatter, effects significantly blunted in the presence of thymol 2.5 - 20 μg/ml. Thymol is a potent inhibitor of suicidal erythrocyte death particularly following oxidative stress. In conclusion, thymol may be useful incounteracting anemia and impairment of microcirculation.

show abstract

Suicidal Death of Erythrocytes Due to Selenium-Compounds

Cited by 43 publications

References 95 publications

Hemin-induced suicidal erythrocyte death

Hemin-induced suicidal erythrocyte death

Suicide for Survival - Death of Infected Erythrocytes as a Host Mechanism to Survive Malaria

Inhibitory Effect of Thymol on Suicidal Erythrocyte Death

Contact Info

Product

Resources

About