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Volumn 8, Issue 2, 2013, Pages

Adhesion of Annexin 7 Deficient Erythrocytes to Endothelial Cells

Author keywords

[No Author keywords available]

Indexed keywords

ANNEXIN; ANNEXIN 7; IONOMYCIN; PHOSPHATIDYLSERINE; UNCLASSIFIED DRUG;

EID: 84874275868     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0056650     Document Type: Article
Times cited : (10)

References (96)
  • 1
    • 68549097911 scopus 로고    scopus 로고
    • The annexins: spatial and temporal coordination of signaling events during cellular stress
    • Monastyrskaya K, Babiychuk EB, Draeger A, (2009) The annexins: spatial and temporal coordination of signaling events during cellular stress. Cell Mol Life Sci 66: 2623-2642.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 2623-2642
    • Monastyrskaya, K.1    Babiychuk, E.B.2    Draeger, A.3
  • 2
    • 67650532174 scopus 로고    scopus 로고
    • Plasma membrane-associated annexin A6 reduces Ca2+ entry by stabilizing the cortical actin cytoskeleton
    • Monastyrskaya K, Babiychuk EB, Hostettler A, Wood P, Grewal T, et al. (2009) Plasma membrane-associated annexin A6 reduces Ca2+ entry by stabilizing the cortical actin cytoskeleton. J Biol Chem 284: 17227-17242.
    • (2009) J Biol Chem , vol.284 , pp. 17227-17242
    • Monastyrskaya, K.1    Babiychuk, E.B.2    Hostettler, A.3    Wood, P.4    Grewal, T.5
  • 3
    • 0028324464 scopus 로고
    • Annexins: the problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins
    • Raynal P, Pollard HB, (1994) Annexins: the problem of assessing the biological role for a gene family of multifunctional calcium- and phospholipid-binding proteins. Biochim Biophys Acta 1197: 63-93.
    • (1994) Biochim Biophys Acta , vol.1197 , pp. 63-93
    • Raynal, P.1    Pollard, H.B.2
  • 4
    • 0029744441 scopus 로고    scopus 로고
    • Membrane fusion protein synexin (annexin VII) as a Ca2+/GTP sensor in exocytotic secretion
    • Caohuy H, Srivastava M, Pollard HB, (1996) Membrane fusion protein synexin (annexin VII) as a Ca2+/GTP sensor in exocytotic secretion. Proc Natl Acad Sci U S A 93: 10797-10802.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 10797-10802
    • Caohuy, H.1    Srivastava, M.2    Pollard, H.B.3
  • 5
    • 0033374545 scopus 로고    scopus 로고
    • Expression and localisation of annexin VII (synexin) isoforms in differentiating myoblasts
    • Clemen CS, Hofmann A, Zamparelli C, Noegel AA, (1999) Expression and localisation of annexin VII (synexin) isoforms in differentiating myoblasts. J Muscle Res Cell Motil 20: 669-679.
    • (1999) J Muscle Res Cell Motil , vol.20 , pp. 669-679
    • Clemen, C.S.1    Hofmann, A.2    Zamparelli, C.3    Noegel, A.A.4
  • 6
    • 0026653883 scopus 로고
    • Immunolocalization of synexin (annexin VII) in adrenal chromaffin granules and chromaffin cells: evidence for a dynamic role in the secretory process
    • Kuijpers GA, Lee G, Pollard HB, (1992) Immunolocalization of synexin (annexin VII) in adrenal chromaffin granules and chromaffin cells: evidence for a dynamic role in the secretory process. Cell Tissue Res 269: 323-330.
    • (1992) Cell Tissue Res , vol.269 , pp. 323-330
    • Kuijpers, G.A.1    Lee, G.2    Pollard, H.B.3
  • 7
    • 0033598680 scopus 로고    scopus 로고
    • Defects in inositol 1,4,5-trisphosphate receptor expression, Ca(2+) signaling, and insulin secretion in the anx7(+/-) knockout mouse
    • Srivastava M, Atwater I, Glasman M, Leighton X, Goping G, et al. (1999) Defects in inositol 1,4,5-trisphosphate receptor expression, Ca(2+) signaling, and insulin secretion in the anx7(+/-) knockout mouse. Proc Natl Acad Sci U S A 96: 13783-13788.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 13783-13788
    • Srivastava, M.1    Atwater, I.2    Glasman, M.3    Leighton, X.4    Goping, G.5
  • 8
    • 0034967999 scopus 로고    scopus 로고
    • Loss of annexin A7 leads to alterations in frequency-induced shortening of isolated murine cardiomyocytes
    • Herr C, Smyth N, Ullrich S, Yun F, Sasse P, et al. (2001) Loss of annexin A7 leads to alterations in frequency-induced shortening of isolated murine cardiomyocytes. Mol Cell Biol 21: 4119-4128.
    • (2001) Mol Cell Biol , vol.21 , pp. 4119-4128
    • Herr, C.1    Smyth, N.2    Ullrich, S.3    Yun, F.4    Sasse, P.5
  • 9
    • 0344010176 scopus 로고    scopus 로고
    • The lack of annexin A7 affects functions of primary astrocytes
    • Clemen CS, Herr C, Hovelmeyer N, Noegel AA, (2003) The lack of annexin A7 affects functions of primary astrocytes. Exp Cell Res 291: 406-414.
    • (2003) Exp Cell Res , vol.291 , pp. 406-414
    • Clemen, C.S.1    Herr, C.2    Hovelmeyer, N.3    Noegel, A.A.4
  • 10
    • 77955471995 scopus 로고    scopus 로고
    • Enhanced eryptosis of erythrocytes from gene-targeted mice lacking annexin A7
    • Lang E, Lang PA, Shumilina E, Qadri SM, Kucherenko Y, et al. (2010) Enhanced eryptosis of erythrocytes from gene-targeted mice lacking annexin A7. Pflugers Arch 460: 667-676.
    • (2010) Pflugers Arch , vol.460 , pp. 667-676
    • Lang, E.1    Lang, P.A.2    Shumilina, E.3    Qadri, S.M.4    Kucherenko, Y.5
  • 11
    • 70450257793 scopus 로고    scopus 로고
    • Accelerated clearance of Plasmodium-infected erythrocytes in sickle cell trait and annexin-A7 deficiency
    • Lang PA, Kasinathan RS, Brand VB, Duranton C, Lang C, et al. (2009) Accelerated clearance of Plasmodium-infected erythrocytes in sickle cell trait and annexin-A7 deficiency. Cell Physiol Biochem 24: 415-428.
    • (2009) Cell Physiol Biochem , vol.24 , pp. 415-428
    • Lang, P.A.1    Kasinathan, R.S.2    Brand, V.B.3    Duranton, C.4    Lang, C.5
  • 13
    • 34548351248 scopus 로고    scopus 로고
    • Differential effect of HOE642 on two separate monovalent cation transporters in the human red cell membrane
    • Bernhardt I, Weiss E, Robinson HC, Wilkins R, Bennekou P, (2007) Differential effect of HOE642 on two separate monovalent cation transporters in the human red cell membrane. Cell Physiol Biochem 20: 601-606.
    • (2007) Cell Physiol Biochem , vol.20 , pp. 601-606
    • Bernhardt, I.1    Weiss, E.2    Robinson, H.C.3    Wilkins, R.4    Bennekou, P.5
  • 14
    • 0037088836 scopus 로고    scopus 로고
    • Oxidation induces a Cl(-)-dependent cation conductance in human red blood cells
    • Duranton C, Huber SM, Lang F, (2002) Oxidation induces a Cl(-)-dependent cation conductance in human red blood cells. J Physiol 539: 847-855.
    • (2002) J Physiol , vol.539 , pp. 847-855
    • Duranton, C.1    Huber, S.M.2    Lang, F.3
  • 15
    • 0042665846 scopus 로고    scopus 로고
    • Electrophysiological properties of the Plasmodium Falciparum-induced cation conductance of human erythrocytes
    • Duranton C, Huber S, Tanneur V, Lang K, Brand V, et al. (2003) Electrophysiological properties of the Plasmodium Falciparum-induced cation conductance of human erythrocytes. Cell Physiol Biochem 13: 189-198.
    • (2003) Cell Physiol Biochem , vol.13 , pp. 189-198
    • Duranton, C.1    Huber, S.2    Tanneur, V.3    Lang, K.4    Brand, V.5
  • 17
    • 65349138878 scopus 로고    scopus 로고
    • Regulation of erythrocyte survival by AMP-activated protein kinase
    • Foller M, Sopjani M, Koka S, Gu S, Mahmud H, et al. (2009) Regulation of erythrocyte survival by AMP-activated protein kinase. FASEB J 23: 1072-1080.
    • (2009) FASEB J , vol.23 , pp. 1072-1080
    • Foller, M.1    Sopjani, M.2    Koka, S.3    Gu, S.4    Mahmud, H.5
  • 18
    • 0035141179 scopus 로고    scopus 로고
    • Chloride conductance and volume-regulatory nonselective cation conductance in human red blood cell ghosts
    • Huber SM, Gamper N, Lang F, (2001) Chloride conductance and volume-regulatory nonselective cation conductance in human red blood cell ghosts. Pflugers Arch 441: 551-558.
    • (2001) Pflugers Arch , vol.441 , pp. 551-558
    • Huber, S.M.1    Gamper, N.2    Lang, F.3
  • 19
    • 0034565124 scopus 로고    scopus 로고
    • The non-selective voltage-activated cation channel in the human red blood cell membrane: reconciliation between two conflicting reports and further characterisation
    • Kaestner L, Christophersen P, Bernhardt I, Bennekou P, (2000) The non-selective voltage-activated cation channel in the human red blood cell membrane: reconciliation between two conflicting reports and further characterisation. Bioelectrochemistry 52: 117-125.
    • (2000) Bioelectrochemistry , vol.52 , pp. 117-125
    • Kaestner, L.1    Christophersen, P.2    Bernhardt, I.3    Bennekou, P.4
  • 20
    • 0036146457 scopus 로고    scopus 로고
    • Ion channels in the human red blood cell membrane: their further investigation and physiological relevance
    • Kaestner L, Bernhardt I, (2002) Ion channels in the human red blood cell membrane: their further investigation and physiological relevance. Bioelectrochemistry 55: 71-74.
    • (2002) Bioelectrochemistry , vol.55 , pp. 71-74
    • Kaestner, L.1    Bernhardt, I.2
  • 23
    • 0023063572 scopus 로고
    • Activation of calcium-dependent potassium channels in deoxygenated sickled red cells
    • Bookchin RM, Ortiz OE, Lew VL, (1987) Activation of calcium-dependent potassium channels in deoxygenated sickled red cells. Prog Clin Biol Res 240: 193-200.
    • (1987) Prog Clin Biol Res , vol.240 , pp. 193-200
    • Bookchin, R.M.1    Ortiz, O.E.2    Lew, V.L.3
  • 24
    • 0027275040 scopus 로고
    • Inhibition of Ca(2+)-dependent K+ transport and cell dehydration in sickle erythrocytes by clotrimazole and other imidazole derivatives
    • Brugnara C, de Franceschi L, Alper SL, (1993) Inhibition of Ca(2+)-dependent K+ transport and cell dehydration in sickle erythrocytes by clotrimazole and other imidazole derivatives. J Clin Invest 92: 520-526.
    • (1993) J Clin Invest , vol.92 , pp. 520-526
    • Brugnara, C.1    de Franceschi, L.2    Alper, S.L.3
  • 26
    • 0035678259 scopus 로고    scopus 로고
    • Human mature red blood cells express caspase-3 and caspase-8, but are devoid of mitochondrial regulators of apoptosis
    • Berg CP, Engels IH, Rothbart A, Lauber K, Renz A, et al. (2001) Human mature red blood cells express caspase-3 and caspase-8, but are devoid of mitochondrial regulators of apoptosis. Cell Death Differ 8: 1197-1206.
    • (2001) Cell Death Differ , vol.8 , pp. 1197-1206
    • Berg, C.P.1    Engels, I.H.2    Rothbart, A.3    Lauber, K.4    Renz, A.5
  • 27
    • 0344826477 scopus 로고    scopus 로고
    • Dependence of Plasmodium falciparum in vitro growth on the cation permeability of the human host erythrocyte
    • Brand VB, Sandu CD, Duranton C, Tanneur V, Lang KS, et al. (2003) Dependence of Plasmodium falciparum in vitro growth on the cation permeability of the human host erythrocyte. Cell Physiol Biochem 13: 347-356.
    • (2003) Cell Physiol Biochem , vol.13 , pp. 347-356
    • Brand, V.B.1    Sandu, C.D.2    Duranton, C.3    Tanneur, V.4    Lang, K.S.5
  • 28
    • 0035674616 scopus 로고    scopus 로고
    • Programmed cell death in mature erythrocytes: a model for investigating death effector pathways operating in the absence of mitochondria
    • Bratosin D, Estaquier J, Petit F, Arnoult D, Quatannens B, et al. (2001) Programmed cell death in mature erythrocytes: a model for investigating death effector pathways operating in the absence of mitochondria. Cell Death Differ 8: 1143-1156.
    • (2001) Cell Death Differ , vol.8 , pp. 1143-1156
    • Bratosin, D.1    Estaquier, J.2    Petit, F.3    Arnoult, D.4    Quatannens, B.5
  • 30
    • 79959399182 scopus 로고    scopus 로고
    • Janus kinase 3 is expressed in erythrocytes, phosphorylated upon energy depletion and involved in the regulation of suicidal erythrocyte death
    • Bhavsar SK, Gu S, Bobbala D, Lang F, (2011) Janus kinase 3 is expressed in erythrocytes, phosphorylated upon energy depletion and involved in the regulation of suicidal erythrocyte death. Cell Physiol Biochem 27: 547-556.
    • (2011) Cell Physiol Biochem , vol.27 , pp. 547-556
    • Bhavsar, S.K.1    Gu, S.2    Bobbala, D.3    Lang, F.4
  • 31
    • 84864183630 scopus 로고    scopus 로고
    • Effect of casein kinase 1alpha activator pyrvinium pamoate on erythrocyte ion channels
    • Kucherenko Y, Zelenak C, Eberhard M, Qadri SM, Lang F, (2012) Effect of casein kinase 1alpha activator pyrvinium pamoate on erythrocyte ion channels. Cell Physiol Biochem 30: 407-417.
    • (2012) Cell Physiol Biochem , vol.30 , pp. 407-417
    • Kucherenko, Y.1    Zelenak, C.2    Eberhard, M.3    Qadri, S.M.4    Lang, F.5
  • 33
    • 83755206903 scopus 로고    scopus 로고
    • p38 MAPK activation and function following osmotic shock of erythrocytes
    • Gatidis S, Zelenak C, Fajol A, Lang E, Jilani K, et al. (2011) p38 MAPK activation and function following osmotic shock of erythrocytes. Cell Physiol Biochem 28: 1279-1286.
    • (2011) Cell Physiol Biochem , vol.28 , pp. 1279-1286
    • Gatidis, S.1    Zelenak, C.2    Fajol, A.3    Lang, E.4    Jilani, K.5
  • 34
    • 79953715199 scopus 로고    scopus 로고
    • Proteome analysis of erythrocytes lacking AMP-activated protein kinase reveals a role of PAK2 kinase in eryptosis
    • Zelenak C, Foller M, Velic A, Krug K, Qadri SM, et al. (2011) Proteome analysis of erythrocytes lacking AMP-activated protein kinase reveals a role of PAK2 kinase in eryptosis. J Proteome Res 10: 1690-1697.
    • (2011) J Proteome Res , vol.10 , pp. 1690-1697
    • Zelenak, C.1    Foller, M.2    Velic, A.3    Krug, K.4    Qadri, S.M.5
  • 35
    • 84865058970 scopus 로고    scopus 로고
    • Enhanced Erythrocyte Membrane Exposure of Phosphatidylserine Following Sorafenib Treatment: An in vivo and in vitro Study
    • Lupescu A, Shaik N, Jilani K, Zelenak C, Lang E, et al. (2012) Enhanced Erythrocyte Membrane Exposure of Phosphatidylserine Following Sorafenib Treatment: An in vivo and in vitro Study. Cell Physiol Biochem 30: 876-888.
    • (2012) Cell Physiol Biochem , vol.30 , pp. 876-888
    • Lupescu, A.1    Shaik, N.2    Jilani, K.3    Zelenak, C.4    Lang, E.5
  • 36
    • 84863875401 scopus 로고    scopus 로고
    • Sunitinib-sensitive suicidal erythrocyte death
    • Shaik N, Lupescu A, Lang F, (2012) Sunitinib-sensitive suicidal erythrocyte death. Cell Physiol Biochem 30: 512-522.
    • (2012) Cell Physiol Biochem , vol.30 , pp. 512-522
    • Shaik, N.1    Lupescu, A.2    Lang, F.3
  • 37
  • 38
    • 0032811978 scopus 로고    scopus 로고
    • Role of red blood cells in thrombosis
    • Andrews DA, Low PS, (1999) Role of red blood cells in thrombosis. Curr Opin Hematol 6: 76-82.
    • (1999) Curr Opin Hematol , vol.6 , pp. 76-82
    • Andrews, D.A.1    Low, P.S.2
  • 39
    • 0032748399 scopus 로고    scopus 로고
    • Phosphatidylserine-related adhesion of human erythrocytes to vascular endothelium
    • Closse C, Dachary-Prigent J, Boisseau MR, (1999) Phosphatidylserine-related adhesion of human erythrocytes to vascular endothelium. Br J Haematol 107: 300-302.
    • (1999) Br J Haematol , vol.107 , pp. 300-302
    • Closse, C.1    Dachary-Prigent, J.2    Boisseau, M.R.3
  • 40
    • 0038481238 scopus 로고    scopus 로고
    • Altered erythrocyte endothelial adherence and membrane phospholipid asymmetry in hereditary hydrocytosis
    • Gallagher PG, Chang SH, Rettig MP, Neely JE, Hillery CA, et al. (2003) Altered erythrocyte endothelial adherence and membrane phospholipid asymmetry in hereditary hydrocytosis. Blood 101: 4625-4627.
    • (2003) Blood , vol.101 , pp. 4625-4627
    • Gallagher, P.G.1    Chang, S.H.2    Rettig, M.P.3    Neely, J.E.4    Hillery, C.A.5
  • 41
    • 35848958833 scopus 로고    scopus 로고
    • Mechanisms of uremic erythrocyte-induced adhesion of human monocytes to cultured endothelial cells
    • Pandolfi A, Di Pietro N, Sirolli V, Giardinelli A, Di Silvestre S, et al. (2007) Mechanisms of uremic erythrocyte-induced adhesion of human monocytes to cultured endothelial cells. J Cell Physiol 213: 699-709.
    • (2007) J Cell Physiol , vol.213 , pp. 699-709
    • Pandolfi, A.1    Di Pietro, N.2    Sirolli, V.3    Giardinelli, A.4    Di Silvestre, S.5
  • 42
    • 0029817966 scopus 로고    scopus 로고
    • Increased erythrocyte phosphatidylserine exposure in sickle cell disease: flow-cytometric measurement and clinical associations
    • Wood BL, Gibson DF, Tait JF, (1996) Increased erythrocyte phosphatidylserine exposure in sickle cell disease: flow-cytometric measurement and clinical associations. Blood 88: 1873-1880.
    • (1996) Blood , vol.88 , pp. 1873-1880
    • Wood, B.L.1    Gibson, D.F.2    Tait, J.F.3
  • 44
    • 33846188964 scopus 로고    scopus 로고
    • Use of a hanging-weight system for isolated renal artery occlusion during ischemic preconditioning in mice
    • Grenz A, Eckle T, Zhang H, Huang DY, Wehrmann M, et al. (2007) Use of a hanging-weight system for isolated renal artery occlusion during ischemic preconditioning in mice. Am J Physiol Renal Physiol 292: F475-F485.
    • (2007) Am J Physiol Renal Physiol , vol.292
    • Grenz, A.1    Eckle, T.2    Zhang, H.3    Huang, D.Y.4    Wehrmann, M.5
  • 45
    • 1542724429 scopus 로고    scopus 로고
    • A disintegrin and metalloproteinase 10-mediated cleavage and shedding regulates the cell surface expression of CXC chemokine ligand 16
    • Gough PJ, Garton KJ, Wille PT, Rychlewski M, Dempsey PJ, et al. (2004) A disintegrin and metalloproteinase 10-mediated cleavage and shedding regulates the cell surface expression of CXC chemokine ligand 16. J Immunol 172: 3678-3685.
    • (2004) J Immunol , vol.172 , pp. 3678-3685
    • Gough, P.J.1    Garton, K.J.2    Wille, P.T.3    Rychlewski, M.4    Dempsey, P.J.5
  • 46
    • 40049104573 scopus 로고    scopus 로고
    • Critical role for CXC chemokine ligand 16 (SR-PSOX) in Th1 response mediated by NKT cells
    • Shimaoka T, Seino K, Kume N, Minami M, Nishime C, et al. (2007) Critical role for CXC chemokine ligand 16 (SR-PSOX) in Th1 response mediated by NKT cells. J Immunol 179: 8172-8179.
    • (2007) J Immunol , vol.179 , pp. 8172-8179
    • Shimaoka, T.1    Seino, K.2    Kume, N.3    Minami, M.4    Nishime, C.5
  • 47
    • 33644891025 scopus 로고    scopus 로고
    • Enhanced programmed cell death of iron-deficient erythrocytes
    • Kempe DS, Lang PA, Duranton C, Akel A, Lang KS, et al. (2006) Enhanced programmed cell death of iron-deficient erythrocytes. FASEB J 20: 368-370.
    • (2006) FASEB J , vol.20 , pp. 368-370
    • Kempe, D.S.1    Lang, P.A.2    Duranton, C.3    Akel, A.4    Lang, K.S.5
  • 48
    • 4344698212 scopus 로고    scopus 로고
    • Enhanced susceptibility to erythrocyte "apoptosis" following phosphate depletion
    • Birka C, Lang PA, Kempe DS, Hoefling L, Tanneur V, et al. (2004) Enhanced susceptibility to erythrocyte "apoptosis" following phosphate depletion. Pflugers Arch 448: 471-477.
    • (2004) Pflugers Arch , vol.448 , pp. 471-477
    • Birka, C.1    Lang, P.A.2    Kempe, D.S.3    Hoefling, L.4    Tanneur, V.5
  • 49
    • 33646337960 scopus 로고    scopus 로고
    • Suicidal death of erythrocytes in recurrent hemolytic uremic syndrome
    • Lang PA, Beringer O, Nicolay JP, Amon O, Kempe DS, et al. (2006) Suicidal death of erythrocytes in recurrent hemolytic uremic syndrome. J Mol Med 84: 378-388.
    • (2006) J Mol Med , vol.84 , pp. 378-388
    • Lang, P.A.1    Beringer, O.2    Nicolay, J.P.3    Amon, O.4    Kempe, D.S.5
  • 52
    • 60549101348 scopus 로고    scopus 로고
    • Influence of paclitaxel on parasitemia and survival of Plasmodium berghei infected mice
    • Koka S, Bobbala D, Lang C, Boini KM, Huber SM, et al. (2009) Influence of paclitaxel on parasitemia and survival of Plasmodium berghei infected mice. Cell Physiol Biochem 23: 191-198.
    • (2009) Cell Physiol Biochem , vol.23 , pp. 191-198
    • Koka, S.1    Bobbala, D.2    Lang, C.3    Boini, K.M.4    Huber, S.M.5
  • 53
    • 68349127308 scopus 로고    scopus 로고
    • Suicide for survival-death of infected erythrocytes as a host mechanism to survive malaria
    • Foller M, Bobbala D, Koka S, Huber SM, Gulbins E, et al. (2009) Suicide for survival-death of infected erythrocytes as a host mechanism to survive malaria. Cell Physiol Biochem 24: 133-140.
    • (2009) Cell Physiol Biochem , vol.24 , pp. 133-140
    • Foller, M.1    Bobbala, D.2    Koka, S.3    Huber, S.M.4    Gulbins, E.5
  • 54
    • 78650011787 scopus 로고    scopus 로고
    • Effect of amphotericin B on parasitemia and survival of plasmodium berghei-infected mice
    • Siraskar B, Ballal A, Bobbala D, Foller M, Lang F, (2010) Effect of amphotericin B on parasitemia and survival of plasmodium berghei-infected mice. Cell Physiol Biochem 26: 347-354.
    • (2010) Cell Physiol Biochem , vol.26 , pp. 347-354
    • Siraskar, B.1    Ballal, A.2    Bobbala, D.3    Foller, M.4    Lang, F.5
  • 55
    • 33846985938 scopus 로고    scopus 로고
    • Liver cell death and anemia in Wilson disease involve acid sphingomyelinase and ceramide
    • Lang PA, Schenck M, Nicolay JP, Becker JU, Kempe DS, et al. (2007) Liver cell death and anemia in Wilson disease involve acid sphingomyelinase and ceramide. Nat Med 13: 164-170.
    • (2007) Nat Med , vol.13 , pp. 164-170
    • Lang, P.A.1    Schenck, M.2    Nicolay, J.P.3    Becker, J.U.4    Kempe, D.S.5
  • 56
    • 45149094904 scopus 로고    scopus 로고
    • Environmental stress, erythrocyte dysfunctions, inflammation, and the metabolic syndrome: adaptations to CO2 increases?
    • Zappulla D, (2008) Environmental stress, erythrocyte dysfunctions, inflammation, and the metabolic syndrome: adaptations to CO2 increases? J Cardiometab Syndr 3: 30-34.
    • (2008) J Cardiometab Syndr , vol.3 , pp. 30-34
    • Zappulla, D.1
  • 57
    • 84868445257 scopus 로고    scopus 로고
    • Stimulation of suicidal death of erythrocytes by rifampicin
    • Abed M, Towhid ST, Shaik N, Lang F, (2012) Stimulation of suicidal death of erythrocytes by rifampicin. Toxicology 302: 123-128.
    • (2012) Toxicology , vol.302 , pp. 123-128
    • Abed, M.1    Towhid, S.T.2    Shaik, N.3    Lang, F.4
  • 58
  • 59
    • 84858211907 scopus 로고    scopus 로고
    • Plasmodium falciparum-infected erythrocytes induce granzyme B by NK cells through expression of host-Hsp70
    • Bottger E, Multhoff G, Kun JF, Esen M, (2012) Plasmodium falciparum-infected erythrocytes induce granzyme B by NK cells through expression of host-Hsp70. PLoS One 7: e33774.
    • (2012) PLoS One , vol.7
    • Bottger, E.1    Multhoff, G.2    Kun, J.F.3    Esen, M.4
  • 61
    • 84861017791 scopus 로고    scopus 로고
    • Increased caspase-3 immunoreactivity of erythrocytes in STZ diabetic rats
    • Firat U, Kaya S, Cim A, Buyukbayram H, Gokalp O, et al. (2012) Increased caspase-3 immunoreactivity of erythrocytes in STZ diabetic rats. Exp Diabetes Res 2012: 316384.
    • (2012) Exp Diabetes Res , vol.2012 , pp. 316384
    • Firat, U.1    Kaya, S.2    Cim, A.3    Buyukbayram, H.4    Gokalp, O.5
  • 62
    • 84857798694 scopus 로고    scopus 로고
    • Understanding the mechanisms for metabolism-linked hemolytic toxicity of primaquine against glucose 6-phosphate dehydrogenase deficient human erythrocytes: evaluation of eryptotic pathway
    • Ganesan S, Chaurasiya ND, Sahu R, Walker LA, Tekwani BL, (2012) Understanding the mechanisms for metabolism-linked hemolytic toxicity of primaquine against glucose 6-phosphate dehydrogenase deficient human erythrocytes: evaluation of eryptotic pathway. Toxicology 294: 54-60.
    • (2012) Toxicology , vol.294 , pp. 54-60
    • Ganesan, S.1    Chaurasiya, N.D.2    Sahu, R.3    Walker, L.A.4    Tekwani, B.L.5
  • 63
    • 84862871418 scopus 로고    scopus 로고
    • Polyphyllin D induces apoptosis in human erythrocytes through Ca(2)(+) rise and membrane permeabilization
    • Gao M, Cheung KL, Lau IP, Yu WS, Fung KP, et al. (2012) Polyphyllin D induces apoptosis in human erythrocytes through Ca(2)(+) rise and membrane permeabilization. Arch Toxicol 86: 741-752.
    • (2012) Arch Toxicol , vol.86 , pp. 741-752
    • Gao, M.1    Cheung, K.L.2    Lau, I.P.3    Yu, W.S.4    Fung, K.P.5
  • 64
    • 79951601376 scopus 로고    scopus 로고
    • The NFkB pathway inhibitors Bay 11-7082 and parthenolide induce programmed cell death in anucleated Erythrocytes
    • Ghashghaeinia M, Toulany M, Saki M, Bobbala D, Fehrenbacher B, et al. (2011) The NFkB pathway inhibitors Bay 11-7082 and parthenolide induce programmed cell death in anucleated Erythrocytes. Cell Physiol Biochem 27: 45-54.
    • (2011) Cell Physiol Biochem , vol.27 , pp. 45-54
    • Ghashghaeinia, M.1    Toulany, M.2    Saki, M.3    Bobbala, D.4    Fehrenbacher, B.5
  • 66
    • 84867690450 scopus 로고    scopus 로고
    • Enhanced Apoptotic Death of Erythrocytes Induced by the Mycotoxin Ochratoxin A
    • Jilani K, Lupescu A, Zbidah M, Abed M, Shaik N, et al. (2012) Enhanced Apoptotic Death of Erythrocytes Induced by the Mycotoxin Ochratoxin A. Kidney Blood Press Res. 36: 107-118.
    • (2012) Kidney Blood Press Res , vol.36 , pp. 107-118
    • Jilani, K.1    Lupescu, A.2    Zbidah, M.3    Abed, M.4    Shaik, N.5
  • 67
    • 84869396808 scopus 로고    scopus 로고
    • Withaferin A-stimulated Ca(2+) entry, ceramide formation and suicidal death of erythrocytes
    • Jilani K, Lupescu A, Zbidah M, Shaik N, Lang F, (2013) Withaferin A-stimulated Ca(2+) entry, ceramide formation and suicidal death of erythrocytes. Toxicol In Vitro 27: 52-58.
    • (2013) Toxicol In Vitro , vol.27 , pp. 52-58
    • Jilani, K.1    Lupescu, A.2    Zbidah, M.3    Shaik, N.4    Lang, F.5
  • 68
    • 84865056373 scopus 로고    scopus 로고
    • Inhibitory Effect of Furosemide on Non-Selective Voltage-Independent Cation Channels in Human Erythrocytes
    • Kucherenko YV, Lang F, (2012) Inhibitory Effect of Furosemide on Non-Selective Voltage-Independent Cation Channels in Human Erythrocytes. Cell Physiol Biochem 30: 863-875.
    • (2012) Cell Physiol Biochem , vol.30 , pp. 863-875
    • Kucherenko, Y.V.1    Lang, F.2
  • 71
    • 84861418715 scopus 로고    scopus 로고
    • Killing me softly - suicidal erythrocyte death
    • Lang E, Qadri SM, Lang F, (2012) Killing me softly- suicidal erythrocyte death. Int J Biochem Cell Biol 44: 1236-1243.
    • (2012) Int J Biochem Cell Biol , vol.44 , pp. 1236-1243
    • Lang, E.1    Qadri, S.M.2    Lang, F.3
  • 72
    • 84856052014 scopus 로고    scopus 로고
    • Mechanisms and significance of eryptosis, the suicidal death of erythrocytes
    • Lang F, Qadri SM, (2012) Mechanisms and significance of eryptosis, the suicidal death of erythrocytes. Blood Purif 33: 125-130.
    • (2012) Blood Purif , vol.33 , pp. 125-130
    • Lang, F.1    Qadri, S.M.2
  • 73
    • 84862553285 scopus 로고    scopus 로고
    • Hexavalent chromium-induced erythrocyte membrane phospholipid asymmetry
    • Lupescu A, Jilani K, Zelenak C, Zbidah M, Qadri SM, et al. (2012) Hexavalent chromium-induced erythrocyte membrane phospholipid asymmetry. Biometals 25: 309-318.
    • (2012) Biometals , vol.25 , pp. 309-318
    • Lupescu, A.1    Jilani, K.2    Zelenak, C.3    Zbidah, M.4    Qadri, S.M.5
  • 75
    • 84870207315 scopus 로고    scopus 로고
    • Enhanced Ca(2+) Entry, Ceramide Formation, and Apoptotic Death of Erythrocytes Triggered by Plumbagin
    • Lupescu A, Jilani K, Zbidah M, Lang E, Lang F (2012) Enhanced Ca(2+) Entry, Ceramide Formation, and Apoptotic Death of Erythrocytes Triggered by Plumbagin. J Nat Prod.
    • (2012) J Nat Prod.
    • Lupescu, A.1    Jilani, K.2    Zbidah, M.3    Lang, E.4    Lang, F.5
  • 76
    • 84874680927 scopus 로고    scopus 로고
    • Ca Influx versus Efflux during Eryptosis in Uremic Erythrocytes
    • Polak-Jonkisz D, Purzyc L, (2012) Ca Influx versus Efflux during Eryptosis in Uremic Erythrocytes. Blood Purif 34: 209-210.
    • (2012) Blood Purif , vol.34 , pp. 209-210
    • Polak-Jonkisz, D.1    Purzyc, L.2
  • 77
    • 79953089426 scopus 로고    scopus 로고
    • Beauvericin induced erythrocyte cell membrane scrambling
    • Qadri SM, Kucherenko Y, Lang F, (2011) Beauvericin induced erythrocyte cell membrane scrambling. Toxicology 283: 24-31.
    • (2011) Toxicology , vol.283 , pp. 24-31
    • Qadri, S.M.1    Kucherenko, Y.2    Lang, F.3
  • 78
    • 83755178192 scopus 로고    scopus 로고
    • Dicoumarol activates Ca2+-permeable cation channels triggering erythrocyte cell membrane scrambling
    • Qadri SM, Kucherenko Y, Zelenak C, Jilani K, Lang E, et al. (2011) Dicoumarol activates Ca2+-permeable cation channels triggering erythrocyte cell membrane scrambling. Cell Physiol Biochem 28: 857-864.
    • (2011) Cell Physiol Biochem , vol.28 , pp. 857-864
    • Qadri, S.M.1    Kucherenko, Y.2    Zelenak, C.3    Jilani, K.4    Lang, E.5
  • 79
    • 80052077564 scopus 로고    scopus 로고
    • Sphingosine but not sphingosine-1-phosphate stimulates suicidal erythrocyte death
    • Qadri SM, Bauer J, Zelenak C, Mahmud H, Kucherenko Y, et al. (2011) Sphingosine but not sphingosine-1-phosphate stimulates suicidal erythrocyte death. Cell Physiol Biochem 28: 339-346.
    • (2011) Cell Physiol Biochem , vol.28 , pp. 339-346
    • Qadri, S.M.1    Bauer, J.2    Zelenak, C.3    Mahmud, H.4    Kucherenko, Y.5
  • 80
    • 84860322995 scopus 로고    scopus 로고
    • Salidroside protects human erythrocytes against hydrogen peroxide-induced apoptosis
    • Qian EW, Ge DT, Kong SK, (2012) Salidroside protects human erythrocytes against hydrogen peroxide-induced apoptosis. J Nat Prod 75: 531-537.
    • (2012) J Nat Prod , vol.75 , pp. 531-537
    • Qian, E.W.1    Ge, D.T.2    Kong, S.K.3
  • 81
    • 84864397354 scopus 로고    scopus 로고
    • Inhibition of Ca(2+) entry and suicidal erythrocyte death by naringin
    • Shaik N, Zbidah M, Lang F, (2012) Inhibition of Ca(2+) entry and suicidal erythrocyte death by naringin. Cell Physiol Biochem 30: 678-686.
    • (2012) Cell Physiol Biochem , vol.30 , pp. 678-686
    • Shaik, N.1    Zbidah, M.2    Lang, F.3
  • 83
    • 84856108016 scopus 로고    scopus 로고
    • Deoxygenation-induced and Ca(2+) dependent phosphatidylserine externalisation in red blood cells from normal individuals and sickle cell patients
    • Weiss E, Cytlak UM, Rees DC, Osei A, Gibson JS, (2012) Deoxygenation-induced and Ca(2+) dependent phosphatidylserine externalisation in red blood cells from normal individuals and sickle cell patients. Cell Calcium 51: 51-56.
    • (2012) Cell Calcium , vol.51 , pp. 51-56
    • Weiss, E.1    Cytlak, U.M.2    Rees, D.C.3    Osei, A.4    Gibson, J.S.5
  • 85
    • 84868496151 scopus 로고    scopus 로고
    • Gossypol-induced suicidal erythrocyte death
    • Zbidah M, Lupescu A, Shaik N, Lang F, (2012) Gossypol-induced suicidal erythrocyte death. Toxicology 302: 101-105.
    • (2012) Toxicology , vol.302 , pp. 101-105
    • Zbidah, M.1    Lupescu, A.2    Shaik, N.3    Lang, F.4
  • 88
    • 84939666375 scopus 로고
    • The pathophysiology of ischaemic acute renal failure. A new hypothesis about the initiation phase
    • Mason J, (1986) The pathophysiology of ischaemic acute renal failure. A new hypothesis about the initiation phase. Ren Physiol 9: 129-147.
    • (1986) Ren Physiol , vol.9 , pp. 129-147
    • Mason, J.1
  • 89
    • 79958794987 scopus 로고    scopus 로고
    • Apoptosis and acute kidney injury
    • Havasi A, Borkan SC, (2011) Apoptosis and acute kidney injury. Kidney Int 80: 29-40.
    • (2011) Kidney Int , vol.80 , pp. 29-40
    • Havasi, A.1    Borkan, S.C.2
  • 90
    • 79551489395 scopus 로고    scopus 로고
    • Acute kidney injury: lessons from experimental models
    • Heyman SN, Rosenberger C, Rosen S, (2011) Acute kidney injury: lessons from experimental models. Contrib Nephrol 169: 286-296.
    • (2011) Contrib Nephrol , vol.169 , pp. 286-296
    • Heyman, S.N.1    Rosenberger, C.2    Rosen, S.3
  • 93
    • 84859827339 scopus 로고    scopus 로고
    • Granulocyte colony stimulating factor prevents kidney infarction and attenuates renovascular hypertension
    • Nogueira BV, Palomino Z, Porto ML, Balarini CM, Pereira TM, et al. (2012) Granulocyte colony stimulating factor prevents kidney infarction and attenuates renovascular hypertension. Cell Physiol Biochem 29: 143-152.
    • (2012) Cell Physiol Biochem , vol.29 , pp. 143-152
    • Nogueira, B.V.1    Palomino, Z.2    Porto, M.L.3    Balarini, C.M.4    Pereira, T.M.5
  • 95
    • 70450252193 scopus 로고    scopus 로고
    • Implementation of an in vitro model system for investigation of reperfusion damage after renal ischemia
    • Sauvant C, Schneider R, Holzinger H, Renker S, Wanner C, et al. (2009) Implementation of an in vitro model system for investigation of reperfusion damage after renal ischemia. Cell Physiol Biochem 24: 567-576.
    • (2009) Cell Physiol Biochem , vol.24 , pp. 567-576
    • Sauvant, C.1    Schneider, R.2    Holzinger, H.3    Renker, S.4    Wanner, C.5
  • 96
    • 84859413982 scopus 로고    scopus 로고
    • Metabolomic changes and protective effect of (L)-carnitine in rat kidney ischemia/reperfusion injury
    • Liu Y, Yan S, Ji C, Dai W, Hu W, et al. (2012) Metabolomic changes and protective effect of (L)-carnitine in rat kidney ischemia/reperfusion injury. Kidney Blood Press Res 35: 373-381.
    • (2012) Kidney Blood Press Res , vol.35 , pp. 373-381
    • Liu, Y.1    Yan, S.2    Ji, C.3    Dai, W.4    Hu, W.5


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