Eryptosis in hereditary spherocytosis and thalassemia: role of glycoconjugates

Basu, Sumanta; Banerjee, Debasis; Chandra, Sarmila; Chakrabarti, Abhijit

doi:10.1007/s10719-009-9257-6

Cited by 32 publications

(17 citation statements)

References 31 publications

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“…Eryptosis is accelerated in sickle cell anemia [3,35], thalassemia [36], G6PD deficiency [3,37], defective anion exchanger 1 (AE1) [3], in a GLUT1 mutation turning this carrier into a Ca 2+ channel [3], and hereditary spherocytosis [36]. Enhanced eryptosis is further observed in Wilson's disease [3], paroxysmal nocturnal hemoglobinuria [37], and myelodysplastic syndrome [38].…”

Section: Disclosure Statementmentioning

confidence: 99%

Physiology and Pathophysiology of Eryptosis

Läng

Lang

Föller³

2012

Transfus Med Hemother

145

106

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Suicidal erythrocyte death (eryptosis) is characterized by cell shrinkage, cell membrane blebbing, and cell membrane phospholipid scrambling with phosphatidylserine exposure at the cell surface. Eryptotic cells adhere to the vascular wall and are rapidly cleared from circulating blood. Eryptosis is stimulated by an increase in cytosolic Ca²⁺ activity, ceramide, hyperosmotic shock, oxidative stress, energy depletion, hyperthermia, and a wide variety of xenobiotics and endogenous substances. Inhibitors of eryptosis include erythropoietin and nitric oxide. Enhanced eryptosis is observed in diabetes, renal insufficiency, hemolytic uremic syndrome, sepsis, mycoplasma infection, malaria, iron deficiency, sickle cell anemia, beta-thalassemia, glucose-6-phosphate dehydrogenase-(G6PD) deficiency, hereditary spherocytosis, paroxysmal nocturnal hemoglobinuria, Wilson’s disease, myelodysplastic syndrome, and phosphate depletion. Eryptosis is further enhanced in gene-targeted mice with deficient annexin 7, cGMP-dependent protein kinase type I (cGKI), AMP-activated protein kinase (AMPK), anion exchanger 1 (AE1), adenomatous polyposis coli (APC), and Klotho, as well as in mouse models of sickle cell anemia and thalassemia. Decreased eryptosis is observed in mice with deficient phosphoinositide-dependent kinase 1 (PDK1), platelet activating factor (PAF) receptor, transient receptor potential channel 6 (TRPC6), janus kinase 3 (JAK3), and taurine transporter (TAUT). Eryptosis may be a useful mechanism to remove defective erythrocytes prior to hemolysis. Excessive eryptosis may, however, compromise microcirculation and lead to anemia.

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Section: Disclosure Statementmentioning

confidence: 99%

Physiology and Pathophysiology of Eryptosis

Läng

Lang

Föller³

2012

Transfus Med Hemother

145

106

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“…Eryptosis is to be considered a physiological event, leading to disposal of aged RBCs by macrophages, however growing evidences suggest that this process may contribute to the patho-physiology of various clinical disorders. Enhanced eryptosis is observed in chronic uremia [19], sickle cell disease [20], thalassemia [21] and diabetes [22]. Externalization of PS at the RBC surface may activate coagulant enzymes [23] and thus cause thrombosis and thrombo-occlusive disease [20,23,24,25,26].…”

Section: Introductionmentioning

confidence: 99%

Oxysterol Mixture in Hypercholesterolemia-Relevant Proportion Causes Oxidative Stress-Dependent Eryptosis

Tesoriere

Attanzio

Allegra

et al. 2014

Cell Physiol Biochem

109

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Background/Aims: Oxysterol activity on the erythrocyte (RBC) programmed cell death (eryptosis) had not been studied yet. Effects of an oxysterol mixture in hyper-cholesterolemic-relevant proportion, and of individual compounds, were investigated on RBCs from healthy humans. Methods: Membrane phosphatidylserine (PS) externalization, calcium entry, ROS production, amino-phospholipid translocase (APLT) activity were evaluated by cytofluorimetric assays, cell volume from forward scatter. Prostaglandin PGE2 was measured by ELISA; GSH-adducts and lipoperoxides by spectrophotometry. Involvement of protein kinase C and caspase was investigated by inhibitors staurosporin, calphostin C, and Z-DEVD-FMK, respectively. Results: Oxysterols caused PS externalization and cell shrinkage, associated with PGE2release, opening of PGE2-dependent calcium channels, ROS production, GSH depletion, membrane lipid oxidation. Addition of antioxidants prevented Ca²⁺ influx and eryptosis. Calcium removal prevented cell shrinkage, with small effect (-20%) on the PS exposure, whereas ROS generation was unaltered. Either in the presence or absence of calcium i) oxysterols inhibited APLT, ii) staurosporin, calphostin C, Z-DEVD-FMK blunted and iii) antioxidants fully prevented the oxysterol-induced PS externalization. Only 7-ketocholesterol and cholestan-3β,5α,6β-triol were individually active. Eryptosis was observed in RBCs isolated after ex vivo spiking of human whole blood with the oxysterol mixture. Conclusions: Oxysterols induce an oxidative stress-dependent eryptosis, involving calcium-independent mechanisms. Eryptotic activity of oxysterols may be relevant in vivo.

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“…4 The relevance of eryptosis in RBCs is indicated by its association with a growing number of diseases, for example, diabetes, heart failure, sickle cell disease, or thalassemia. [5][6][7][8][9][10] In addition, a growing number of chemicals or pharmacologic substances have been associated with eryptosis. 11 The mechanisms leading to eryptosis may be shared with those resulting in normal RBC senescence, such as loss of ATP or accumulation of intracellular Ca 21 concentration ([Ca 21 ]i), but may also be somewhat different.…”

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confidence: 99%