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Volumn 6, Issue 12, 2014, Pages 3596-3612

Triggering of programmed erythrocyte death by alantolactone

Author keywords

Alantolactone; Cell volume; Ceramide; Eryptosis; Oxidative stress; Phosphatidylserine

Indexed keywords

ALANTOLACTONE; CALCIUM ION; CERAMIDE; PHOSPHATIDYLSERINE; PHOSPHOLIPID; REACTIVE OXYGEN METABOLITE; 2',7'-DICHLORODIHYDROFLUORESCEIN DIACETATE; CALCIUM; FITC-ANNEXIN A5; FLUORESCEIN DERIVATIVE; FLUORESCEIN ISOTHIOCYANATE; LACTONE; LIPOCORTIN 5; PROTEIN BINDING; SESQUITERPENE;

EID: 84919830468     PISSN: None     EISSN: 20726651     Source Type: Journal    
DOI: 10.3390/toxins6123596     Document Type: Article
Times cited : (8)

References (91)
  • 1
    • 84888861862 scopus 로고    scopus 로고
    • Targeting apoptosis pathways in cancer with alantolactone and isoalantolactone
    • Rasul, A.; Khan, M.; Ali, M.; Li, J.; Li, X. Targeting apoptosis pathways in cancer with alantolactone and isoalantolactone. Sci. World J. 2013, 2013, 248-532.
    • (2013) Sci. World J , vol.2013 , pp. 248-532
    • Rasul, A.1    Khan, M.2    Ali, M.3    Li, J.4    Li, X.5
  • 2
    • 0034871746 scopus 로고    scopus 로고
    • Cytotoxic sesquiterpene lactones mediate their death-inducing effect in leukemia T cells by triggering apoptosis
    • Dirsch, V.M.; Stuppner, H.; Vollmar, A.M. Cytotoxic sesquiterpene lactones mediate their death-inducing effect in leukemia T cells by triggering apoptosis. Planta Med. 2001, 67, 557–559.
    • (2001) Planta Med , vol.67 , pp. 557-559
    • Dirsch, V.M.1    Stuppner, H.2    Vollmar, A.M.3
  • 3
    • 84874634964 scopus 로고    scopus 로고
    • Alantolactone induces apoptosis in HepG2 cells through GSH depletion, inhibition of STAT3 activation, and mitochondrial dysfunction
    • Khan, M.; Li, T.; Ahmad Khan, M.K.; Rasul, A.; Nawaz, F.; Sun, M.; Zheng, Y.; Ma, T. Alantolactone induces apoptosis in HepG2 cells through GSH depletion, inhibition of STAT3 activation, and mitochondrial dysfunction. Biomed. Res. Int. 2013, 2013, 719-858.
    • (2013) Biomed. Res. Int. , vol.2013 , pp. 719-858
    • Khan, M.1    Li, T.2    Ahmad Khan, M.K.3    Rasul, A.4    Nawaz, F.5    Sun, M.6    Zheng, Y.7    Ma, T.8
  • 4
    • 84865331826 scopus 로고    scopus 로고
    • Alantolactone induces apoptosis in glioblastoma cells via GSH depletion, ROS generation, and mitochondrial dysfunction
    • Khan, M.; Yi, F.; Rasul, A.; Li, T.; Wang, N.; Gao, H.; Gao, R.; Ma, T. Alantolactone induces apoptosis in glioblastoma cells via GSH depletion, ROS generation, and mitochondrial dysfunction. IUBMB Life 2012, 64, 783–794.
    • (2012) IUBMB Life , vol.64 , pp. 783-794
    • Khan, M.1    Yi, F.2    Rasul, A.3    Li, T.4    Wang, N.5    Gao, H.6    Gao, R.7    Ma, T.8
  • 5
    • 0035847680 scopus 로고    scopus 로고
    • Cytotoxic Michael-type amine adducts of alpha-methylene lactones alantolactone and isoalantolactone
    • Lawrence, N.J.; McGown, A.T.; Nduka, J.; Hadfield, J.A.; Pritchard, R.G. Cytotoxic Michael-type amine adducts of alpha-methylene lactones alantolactone and isoalantolactone. Bioorg. Med. Chem. Lett. 2001, 11, 429–431.
    • (2001) Bioorg. Med. Chem. Lett , vol.11 , pp. 429-431
    • Lawrence, N.J.1    McGown, A.T.2    Nduka, J.3    Hadfield, J.A.4    Pritchard, R.G.5
  • 6
    • 84864144305 scopus 로고    scopus 로고
    • Alantolactone induces activation of apoptosis in human hepatoma cells
    • Lei, J.C.; Yu, J.Q.; Yin, Y.; Liu, Y.W.; Zou, G.L. Alantolactone induces activation of apoptosis in human hepatoma cells. Food Chem. Toxicol. 2012, 50, 3313–3319.
    • (2012) Food Chem. Toxicol , vol.50 , pp. 3313-3319
    • Lei, J.C.1    Yu, J.Q.2    Yin, Y.3    Liu, Y.W.4    Zou, G.L.5
  • 7
    • 84890054965 scopus 로고    scopus 로고
    • Alantolactone induces cell apoptosis partially through down-regulation of testes-specific protease 50 expression
    • Mi, X.G.; Song, Z.B.; Wu, P.; Zhang, Y.W.; Sun, L.G.; Bao, Y.L.; Zhang, Y.; Zheng, L.H.; Sun, Y.; Yu, C.L.; et al. Alantolactone induces cell apoptosis partially through down-regulation of testes-specific protease 50 expression. Toxicol. Lett. 2014, 224, 349–355.
    • (2014) Toxicol. Lett , vol.224 , pp. 349-355
    • Mi, X.G.1    Song, Z.B.2    Wu, P.3    Zhang, Y.W.4    Sun, L.G.5    Bao, Y.L.6    Zhang, Y.7    Zheng, L.H.8    Sun, Y.9    Yu, C.L.10
  • 8
    • 77956172542 scopus 로고    scopus 로고
    • Activation of caspases and poly (ADP-ribose) polymerase cleavage to induce apoptosis in leukemia HL-60 cells by Inula racemosa
    • Pal, H.C.; Sehar, I.; Bhushan, S.; Gupta, B.D.; Saxena, A.K. Activation of caspases and poly (ADP-ribose) polymerase cleavage to induce apoptosis in leukemia HL-60 cells by Inula racemosa. Toxicol. Vitr. 2010, 24, 1599–1609.
    • (2010) Toxicol. Vitr , vol.24 , pp. 1599-1609
    • Pal, H.C.1    Sehar, I.2    Bhushan, S.3    Gupta, B.D.4    Saxena, A.K.5
  • 9
    • 84881476269 scopus 로고    scopus 로고
    • Alantolactone induces apoptosis in chronic myelogenous leukemia sensitive or resistant to imatinib through NF-kappaB inhibition and Bcr/Abl protein deletion
    • Wei, W.; Huang, H.; Zhao, S.; Liu, W.; Liu, C.X.; Chen, L.; Li, J.M.; Wu, Y.L.; Yan, H. Alantolactone induces apoptosis in chronic myelogenous leukemia sensitive or resistant to imatinib through NF-kappaB inhibition and Bcr/Abl protein deletion. Apoptosis 2013, 18, 1060–1070.
    • (2013) Apoptosis , vol.18 , pp. 1060-1070
    • Wei, W.1    Huang, H.2    Zhao, S.3    Liu, W.4    Liu, C.X.5    Chen, L.6    Li, J.M.7    Wu, Y.L.8    Yan, H.9
  • 10
    • 84876936613 scopus 로고    scopus 로고
    • Alantolactone inhibits growth of K562/adriamycin cells by downregulating Bcr/Abl and P-glycoprotein expression
    • Yang, C.; Yang, J.; Sun, M.; Yan, J.; Meng, X.; Ma, T. Alantolactone inhibits growth of K562/adriamycin cells by downregulating Bcr/Abl and P-glycoprotein expression. IUBMB Life 2013, 65, 435–444.
    • (2013) IUBMB Life , vol.65 , pp. 435-444
    • Yang, C.1    Yang, J.2    Sun, M.3    Yan, J.4    Meng, X.5    Ma, T.6
  • 11
    • 84883397220 scopus 로고    scopus 로고
    • Alantolactone induces apoptosis in RKO cells through the generation of reactive oxygen species and the mitochondrial pathway
    • Zhang, Y.; Bao, Y.L.; Wu, Y.; Yu, C.L.; Huang, Y.X.; Sun, Y.; Zheng, L.H.; Li, Y.X. Alantolactone induces apoptosis in RKO cells through the generation of reactive oxygen species and the mitochondrial pathway. Mol. Med. Rep. 2013, 8, 967–972.
    • (2013) Mol. Med. Rep , vol.8 , pp. 967-972
    • Zhang, Y.1    Bao, Y.L.2    Wu, Y.3    Yu, C.L.4    Huang, Y.X.5    Sun, Y.6    Zheng, L.H.7    Li, Y.X.8
  • 12
    • 84861418715 scopus 로고    scopus 로고
    • Killing me softly—Suicidal erythrocyte death
    • Lang, E.; Qadri, S.M.; Lang, F. Killing me softly—Suicidal erythrocyte death. Int. J. Biochem. Cell Biol. 2012, 44, 1236–1243.
    • (2012) Int. J. Biochem. Cell Biol , vol.44 , pp. 1236-1243
    • Lang, E.1    Qadri, S.M.2    Lang, F.3
  • 15
    • 84902186043 scopus 로고    scopus 로고
    • Oxidative stress and suicidal erythrocyte death
    • Lang, F.; Abed, M.; Lang, E.; Foller, M. Oxidative stress and suicidal erythrocyte death. Antioxid. Redox Signal. 2014, 21, 138–153.
    • (2014) Antioxid. Redox Signal , vol.21 , pp. 138-153
    • Lang, F.1    Abed, M.2    Lang, E.3    Foller, M.4
  • 19
    • 84869013866 scopus 로고    scopus 로고
    • In vitro effect of CTAB- and PEG-coated gold nanorods on the induction of eryptosis/erythroptosis in human erythrocytes
    • Lau, I.P.; Chen, H.; Wang, J.; Ong, H.C.; Leung, K.C.; Ho, H.P.; Kong, S.K. In vitro effect of CTAB- and PEG-coated gold nanorods on the induction of eryptosis/erythroptosis in human erythrocytes. Nanotoxicology 2012, 6, 847–856.
    • (2012) Nanotoxicology , vol.6 , pp. 847-856
    • Lau, I.P.1    Chen, H.2    Wang, J.3    Ong, H.C.4    Leung, K.C.5    Ho, H.P.6    Kong, S.K.7
  • 20
    • 84884907779 scopus 로고    scopus 로고
    • Erythrocyte caspase-3 activation and oxidative imbalance in erythrocytes and in plasma of type 2 diabetic patients
    • Maellaro, E.; Leoncini, S.; Moretti, D.; Del Bello, B.; Tanganelli, I.; de Felice, C.; Ciccoli, L. Erythrocyte caspase-3 activation and oxidative imbalance in erythrocytes and in plasma of type 2 diabetic patients. Acta Diabetol. 2013, 50, 489–495.
    • (2013) Acta Diabetol , vol.50 , pp. 489-495
    • Maellaro, E.1    Leoncini, S.2    Moretti, D.3    Del Bello, B.4    Tanganelli, I.5    De Felice, C.6    Ciccoli, L.7
  • 22
    • 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, S.M.; Viollet, B.; Lang, F.; Macek, B. Proteome analysis of erythrocytes lacking AMP-activated protein kinase reveals a role of PAK2 kinase in eryptosis. J. Proteome Res. 2011, 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    Viollet, B.6    Lang, F.7    Macek, B.8
  • 23
    • 84862553285 scopus 로고    scopus 로고
    • Hexavalent chromium-induced erythrocyte membrane phospholipid asymmetry
    • Lupescu, A.; Jilani, K.; Zelenak, C.; Zbidah, M.; Qadri, S.M.; Lang, F. Hexavalent chromium-induced erythrocyte membrane phospholipid asymmetry. Biometals 2012, 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    Lang, F.6
  • 24
    • 84863875401 scopus 로고    scopus 로고
    • Sunitinib-sensitive suicidal erythrocyte death
    • Shaik, N.; Lupescu, A.; Lang, F. Sunitinib-sensitive suicidal erythrocyte death. Cell. Physiol. Biochem. 2012, 30, 512–522.
    • (2012) Cell. Physiol. Biochem , vol.30 , pp. 512-522
    • Shaik, N.1    Lupescu, A.2    Lang, F.3
  • 25
    • 84864183630 scopus 로고    scopus 로고
    • Effect of casein kinase 1alpha activator pyrvinium pamoate on erythrocyte ion channels
    • Kucherenko, Y.; Zelenak, C.; Eberhard, M.; Qadri, S.M.; Lang, F. Effect of casein kinase 1alpha activator pyrvinium pamoate on erythrocyte ion channels. Cell. Physiol. Biochem. 2012, 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
  • 27
    • 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, S.K.; Gu, S.; Bobbala, D.; Lang, F. Janus kinase 3 is expressed in erythrocytes, phosphorylated upon energy depletion and involved in the regulation of suicidal erythrocyte death. Cell. Physiol. Biochem. 2011, 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
  • 33
    • 79958800036 scopus 로고    scopus 로고
    • Tumor growth inhibitory effect of juglone and its radiation sensitizing potential: In vivo and in vitro studies
    • Aithal, K.B.; Kumar, S.; Rao, B.N.; Udupa, N.; Rao, S.B. Tumor growth inhibitory effect of juglone and its radiation sensitizing potential: In vivo and in vitro studies. Integr. Cancer Ther. 2012, 11, 68–80.
    • (2012) Integr. Cancer Ther , vol.11 , pp. 68-80
    • Aithal, K.B.1    Kumar, S.2    Rao, B.N.3    Udupa, N.4    Rao, S.B.5
  • 34
    • 84891361707 scopus 로고    scopus 로고
    • Triggering of suicidal erythrocyte death by penta-O-galloyl-β-D-glucose
    • Alzoubi, K.; Honisch, S.; Abed, M.; Lang, F. Triggering of suicidal erythrocyte death by penta-O-galloyl-β-D-glucose. Toxins (Basel) 2014, 6, 54–65.
    • (2014) Toxins (Basel) , vol.6 , pp. 54-65
    • Alzoubi, K.1    Honisch, S.2    Abed, M.3    Lang, F.4
  • 35
    • 84912135458 scopus 로고    scopus 로고
    • Mitoxantrone-Induced suicidal erythrocyte death
    • Arnold, M.; Bissinger, R.; Lang, F. Mitoxantrone-Induced suicidal erythrocyte death. Cell. Physiol. Biochem. 2014, 34, 1756–1767.
    • (2014) Cell. Physiol. Biochem , vol.34 , pp. 1756-1767
    • Arnold, M.1    Bissinger, R.2    Lang, F.3
  • 37
    • 84858211907 scopus 로고    scopus 로고
    • Plasmodium falciparum-infected erythrocytes induce granzyme B by NK cells through expression of host-Hsp70
    • e33774
    • Bottger, E.; Multhoff, G.; Kun, J.F.; Esen, M. Plasmodium falciparum-infected erythrocytes induce granzyme B by NK cells through expression of host-Hsp70. PLoS One 2012, 7, e33774.
    • (2012) Plos One , vol.7
    • Bottger, E.1    Multhoff, G.2    Kun, J.F.3    Esen, M.4
  • 38
    • 84861465335 scopus 로고    scopus 로고
    • Phosphoinositol 3-kinase, a novel target molecule for the inhibitory effects of juglone on TPA-induced cell transformation
    • Chae, J.I.; Cho, J.H.; Kim, D.J.; Lee, K.A.; Cho, M.K.; Nam, H.S.; Woo, K.M.; Lee, S.H.; Shim, J.H. Phosphoinositol 3-kinase, a novel target molecule for the inhibitory effects of juglone on TPA-induced cell transformation. Int. J. Mol. Med. 2012, 30, 8–14.
    • (2012) Int. J. Mol. Med , vol.30 , pp. 8-14
    • Chae, J.I.1    Cho, J.H.2    Kim, D.J.3    Lee, K.A.4    Cho, M.K.5    Nam, H.S.6    Woo, K.M.7    Lee, S.H.8    Shim, J.H.9
  • 45
    • 84877270091 scopus 로고    scopus 로고
    • Carmustine-induced phosphatidylserine translocation in the erythrocyte membrane
    • Jilani, K.; Lang, F. Carmustine-induced phosphatidylserine translocation in the erythrocyte membrane. Toxins (Basel) 2013, 5, 703–716.
    • (2013) Toxins (Basel) , vol.5 , pp. 703-716
    • Jilani, K.1    Lang, F.2
  • 46
    • 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.; Lang, F. Enhanced apoptotic death of erythrocytes induced by the mycotoxin ochratoxin A. Kidney Blood Press. Res. 2012, 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    Lang, F.6
  • 47
    • 84893057981 scopus 로고    scopus 로고
    • Geldanamycin-induced phosphatidylserine translocation in the erythrocyte membrane
    • Jilani, K.; Qadri, S.M.; Lang, F. Geldanamycin-induced phosphatidylserine translocation in the erythrocyte membrane. Cell. Physiol. Biochem. 2013, 32, 1600–1609.
    • (2013) Cell. Physiol. Biochem , vol.32 , pp. 1600-1609
    • Jilani, K.1    Qadri, S.M.2    Lang, F.3
  • 48
    • 84865056373 scopus 로고    scopus 로고
    • Inhibitory effect of furosemide on non-selective voltage-independent cation channels in human erythrocytes
    • Kucherenko, Y.V.; Lang, F. Inhibitory effect of furosemide on non-selective voltage-independent cation channels in human erythrocytes. Cell. Physiol. Biochem. 2012, 30, 863–875.
    • (2012) Cell. Physiol. Biochem , vol.30 , pp. 863-875
    • Kucherenko, Y.V.1    Lang, F.2
  • 52
    • 84884162145 scopus 로고    scopus 로고
    • Triggering of suicidal erythrocyte death by celecoxib
    • Lupescu, A.; Bissinger, R.; Jilani, K.; Lang, F. Triggering of suicidal erythrocyte death by celecoxib. Toxins (Basel) 2013, 5, 1543–1554.
    • (2013) Toxins (Basel) , vol.5 , pp. 1543-1554
    • Lupescu, A.1    Bissinger, R.2    Jilani, K.3    Lang, F.4
  • 55
    • 27544443196 scopus 로고    scopus 로고
    • The natural toxin juglone causes degradation of p53 and induces rapid H2AX phosphorylation and cell death in human fibroblasts
    • Paulsen, M.T.; Ljungman, M. The natural toxin juglone causes degradation of p53 and induces rapid H2AX phosphorylation and cell death in human fibroblasts. Toxicol. Appl. Pharmacol. 2005, 209, 1–9.
    • (2005) Toxicol. Appl. Pharmacol , vol.209 , pp. 1-9
    • Paulsen, M.T.1    Ljungman, M.2
  • 56
    • 84874680927 scopus 로고    scopus 로고
    • Ca influx versus efflux during eryptosis in uremic erythrocytes
    • Polak-Jonkisz, D.; Purzyc, L. Ca influx versus efflux during eryptosis in uremic erythrocytes. Blood Purif. 2012, 34, 209–210.
    • (2012) Blood Purif , vol.34 , pp. 209-210
    • Polak-Jonkisz, D.1    Purzyc, L.2
  • 57
    • 84860322995 scopus 로고    scopus 로고
    • Salidroside protects human erythrocytes against hydrogen peroxide-induced apoptosis
    • Qian, E.W.; Ge, D.T.; Kong, S.K. Salidroside protects human erythrocytes against hydrogen peroxide-induced apoptosis. J. Nat. Prod. 2012, 75, 531–537.
    • (2012) J. Nat. Prod , vol.75 , pp. 531-537
    • Qian, E.W.1    Ge, D.T.2    Kong, S.K.3
  • 59
    • 84908609487 scopus 로고    scopus 로고
    • Oxysterol mixture in hypercholesterolemia-relevant proportion causes oxidative stress-dependent eryptosis
    • Tesoriere, L.; Attanzio, A.; Allegra, M.; Cilla, A.; Gentile, C.; Livrea, M.A. Oxysterol mixture in hypercholesterolemia-relevant proportion causes oxidative stress-dependent eryptosis. Cell. Physiol. Biochem. 2014, 34, 1075–1089.
    • (2014) Cell. Physiol. Biochem , vol.34 , pp. 1075-1089
    • Tesoriere, L.1    Attanzio, A.2    Allegra, M.3    Cilla, A.4    Gentile, C.5    Livrea, M.A.6
  • 60
    • 84874232618 scopus 로고    scopus 로고
    • Differential erythropoietin action upon cells induced to eryptosis by different agents
    • Vota, D.M.; Maltaneri, R.E.; Wenker, S.D.; Nesse, A.B.; Vittori, D.C. Differential erythropoietin action upon cells induced to eryptosis by different agents. Cell. Biochem. Biophys. 2013, 65, 145–157.
    • (2013) Cell. Biochem. Biophys , vol.65 , pp. 145-157
    • Vota, D.M.1    Maltaneri, R.E.2    Wenker, S.D.3    Nesse, A.B.4    Vittori, D.C.5
  • 61
    • 84856108016 scopus 로고    scopus 로고
    • 2+ dependent phosphatidylserine externalisation in red blood cells from normal individuals and sickle cell patients
    • 2+ dependent phosphatidylserine externalisation in red blood cells from normal individuals and sickle cell patients. Cell Calcium 2012, 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
  • 62
    • 84878107433 scopus 로고    scopus 로고
    • Juglone, isolated from Juglans mandshurica Maxim, induces apoptosis via down-regulation of AR expression in human prostate cancer LNCaP cells
    • Xu, H.; Yu, X.; Qu, S.; Sui, D. Juglone, isolated from Juglans mandshurica Maxim, induces apoptosis via down-regulation of AR expression in human prostate cancer LNCaP cells. Bioorg. Med. Chem. Lett. 2013, 23, 3631–3634.
    • (2013) Bioorg. Med. Chem. Lett , vol.23 , pp. 3631-3634
    • Xu, H.1    Yu, X.2    Qu, S.3    Sui, D.4
  • 65
    • 84912091297 scopus 로고    scopus 로고
    • Involvement of calcium, reactive oxygen species, and ATP in hexavalent chromium-induced damage in red blood cells
    • Zhang, R.; Xiang, Y.; Ran, Q.; Deng, X.; Xiao, Y.; Xiang, L.; Li, Z. Involvement of calcium, reactive oxygen species, and ATP in hexavalent chromium-induced damage in red blood cells. Cell. Physiol. Biochem. 2014, 34, 1780–1791.
    • (2014) Cell. Physiol. Biochem , vol.34 , pp. 1780-1791
    • Zhang, R.1    Xiang, Y.2    Ran, Q.3    Deng, X.4    Xiao, Y.5    Xiang, L.6    Li, Z.7
  • 66
    • 84895665358 scopus 로고    scopus 로고
    • Stimulation of suicidal erythrocyte death by increased extracellular phosphate concentrations
    • Voelkl, J.; Alzoubi, K.; Mamar, A.K.; Ahmed, M.S.; Abed, M.; Lang, F. Stimulation of suicidal erythrocyte death by increased extracellular phosphate concentrations. Kidney Blood Press. Res. 2013, 38, 42–51.
    • (2013) Kidney Blood Press. Res , vol.38 , pp. 42-51
    • Voelkl, J.1    Alzoubi, K.2    Mamar, A.K.3    Ahmed, M.S.4    Abed, M.5    Lang, F.6
  • 68
    • 1842661170 scopus 로고
    • The pathogenesis of the renal injury produced in the dog by hemoglobin or methemoglobin
    • Harrison, H.E.; Bunting, H.; Ordway, N.K.; Albrink, W.S. The pathogenesis of the renal injury produced in the dog by hemoglobin or methemoglobin. J. Exp. Med. 1947, 86, 339–356.
    • (1947) J. Exp. Med , vol.86 , pp. 339-356
    • Harrison, H.E.1    Bunting, H.2    Ordway, N.K.3    Albrink, W.S.4
  • 69
    • 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, S.M.; Gulbins, E.; Lang, F. Suicide for survival—Death of infected erythrocytes as a host mechanism to survive malaria. Cell. Physiol. Biochem. 2009, 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    Lang, F.6
  • 70
    • 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.; Sandu, C.; Lang, F. Electrophysiological properties of the Plasmodium Falciparum-induced cation conductance of human erythrocytes. Cell. Physiol. Biochem. 2003, 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    Sandu, C.6    Lang, F.7
  • 71
    • 0035069258 scopus 로고    scopus 로고
    • Membrane transport in the malaria-infected erythrocyte
    • Kirk, K. Membrane transport in the malaria-infected erythrocyte. Physiol. Rev. 2001, 81, 495–537.
    • (2001) Physiol. Rev , vol.81 , pp. 495-537
    • Kirk, K.1
  • 73
    • 0036771811 scopus 로고    scopus 로고
    • 16alpha-bromoepiandrosterone, an antimalarial analogue of the hormone dehydroepiandrosterone, enhances phagocytosis of ring stage parasitized erythrocytes: A novel mechanism for antimalarial activity
    • Ayi, K.; Giribaldi, G.; Skorokhod, A.; Schwarzer, E.; Prendergast, P.T.; Arese, P. 16alpha-bromoepiandrosterone, an antimalarial analogue of the hormone dehydroepiandrosterone, enhances phagocytosis of ring stage parasitized erythrocytes: A novel mechanism for antimalarial activity. Antimicrob. Agents Chemother. 2002, 46, 3180–3184.
    • (2002) Antimicrob. Agents Chemother , vol.46 , pp. 3180-3184
    • Ayi, K.1    Giribaldi, G.2    Skorokhod, A.3    Schwarzer, E.4    Prendergast, P.T.5    Arese, P.6
  • 74
    • 8644226200 scopus 로고    scopus 로고
    • Enhanced phagocytosis of ring-parasitized mutant erythrocytes: A common mechanism that may explain protection against falciparum malaria in sickle trait and beta-thalassemia trait
    • Ayi, K.; Turrini, F.; Piga, A.; Arese, P. Enhanced phagocytosis of ring-parasitized mutant erythrocytes: A common mechanism that may explain protection against falciparum malaria in sickle trait and beta-thalassemia trait. Blood 2004, 104, 3364–3371.
    • (2004) Blood , vol.104 , pp. 3364-3371
    • Ayi, K.1    Turrini, F.2    Piga, A.3    Arese, P.4
  • 75
    • 0032189018 scopus 로고    scopus 로고
    • Early phagocytosis of glucose-6-phosphate dehydrogenase (G6PD)-deficient erythrocytes parasitized by Plasmodium falciparum may explain malaria protection in G6PD deficiency
    • Cappadoro, M.; Giribaldi, G.; O’Brien, E.; Turrini, F.; Mannu, F.; Ulliers, D.; Simula, G.; Luzzatto, L.; Arese, P. Early phagocytosis of glucose-6-phosphate dehydrogenase (G6PD)-deficient erythrocytes parasitized by Plasmodium falciparum may explain malaria protection in G6PD deficiency. Blood 1998, 92, 2527–2534.
    • (1998) Blood , vol.92 , pp. 2527-2534
    • Cappadoro, M.1    Giribaldi, G.2    O’Brien, E.3    Turrini, F.4    Mannu, F.5    Ulliers, D.6    Simula, G.7    Luzzatto, L.8    Arese, P.9
  • 76
  • 77
    • 51149091241 scopus 로고    scopus 로고
    • Influence of chlorpromazine on eryptosis, parasitemia and survival of Plasmodium berghe infected mice
    • Koka, S.; Lang, C.; Boini, K.M.; Bobbala, D.; Huber, S.M.; Lang, F. Influence of chlorpromazine on eryptosis, parasitemia and survival of Plasmodium berghe infected mice. Cell. Physiol. Biochem. 2008, 22, 261–268.
    • (2008) Cell. Physiol. Biochem , vol.22 , pp. 261-268
    • Koka, S.1    Lang, C.2    Boini, K.M.3    Bobbala, D.4    Huber, S.M.5    Lang, F.6
  • 78
    • 42949111588 scopus 로고    scopus 로고
    • Influence of NO synthase inhibitor L-NAME on parasitemia and survival of Plasmodium berghei infected mice
    • Koka, S.; Lang, C.; Niemoeller, O.M.; Boini, K.M.; Nicolay, J.P.; Huber, S.M.; Lang, F. Influence of NO synthase inhibitor L-NAME on parasitemia and survival of Plasmodium berghei infected mice. Cell. Physiol. Biochem. 2008, 21, 481–488.
    • (2008) Cell. Physiol. Biochem , vol.21 , pp. 481-488
    • Koka, S.1    Lang, C.2    Niemoeller, O.M.3    Boini, K.M.4    Nicolay, J.P.5    Huber, S.M.6    Lang, F.7
  • 79
    • 55349114724 scopus 로고    scopus 로고
    • Role of lactadherin in the clearance of phosphatidylserine-expressing red blood cells
    • Dasgupta, S.K.; Abdel-Monem, H.; Guchhait, P.; Nagata, S.; Thiagarajan, P. Role of lactadherin in the clearance of phosphatidylserine-expressing red blood cells. Transfusion 2008, 48, 2370–2376.
    • (2008) Transfusion , vol.48 , pp. 2370-2376
    • Dasgupta, S.K.1    Abdel-Monem, H.2    Guchhait, P.3    Nagata, S.4    Thiagarajan, P.5
  • 81
    • 47749112789 scopus 로고    scopus 로고
    • A role of phosphatidylserine externalization in clearance of erythrocytes exposed to stress but not in eliminating aging populations of erythrocyte in mice
    • Khandelwal, S.; Saxena, R.K. A role of phosphatidylserine externalization in clearance of erythrocytes exposed to stress but not in eliminating aging populations of erythrocyte in mice. Exp. Gerontol. 2008, 43, 764–770.
    • (2008) Exp. Gerontol , vol.43 , pp. 764-770
    • Khandelwal, S.1    Saxena, R.K.2
  • 84
    • 0032811978 scopus 로고    scopus 로고
    • Role of red blood cells in thrombosis
    • Andrews, D.A.; Low, P.S. Role of red blood cells in thrombosis. Curr. Opin. Hematol. 1999, 6, 76–82.
    • (1999) Curr. Opin. Hematol , vol.6 , pp. 76-82
    • Andrews, D.A.1    Low, P.S.2
  • 85
    • 33846444733 scopus 로고    scopus 로고
    • Lysophosphatidic acid induces thrombogenic activity through phosphatidylserine exposure and procoagulant microvesicle generation in human erythrocytes
    • Chung, S.M.; Bae, O.N.; Lim, K.M.; Noh, J.Y.; Lee, M.Y.; Jung, Y.S.; Chung, J.H. Lysophosphatidic acid induces thrombogenic activity through phosphatidylserine exposure and procoagulant microvesicle generation in human erythrocytes. Arterioscler. Thromb. Vasc. Biol. 2007, 27, 414–421.
    • (2007) Arterioscler. Thromb. Vasc. Biol , vol.27 , pp. 414-421
    • Chung, S.M.1    Bae, O.N.2    Lim, K.M.3    Noh, J.Y.4    Lee, M.Y.5    Jung, Y.S.6    Chung, J.H.7
  • 86
    • 18544381354 scopus 로고    scopus 로고
    • Surface exposure of phosphatidylserine in pathological cells
    • Zwaal, R.F.; Comfurius, P.; Bevers, E.M. Surface exposure of phosphatidylserine in pathological cells. Cell. Mol. Life Sci. 2005, 62, 971–988.
    • (2005) Cell. Mol. Life Sci , vol.62 , pp. 971-988
    • Zwaal, R.F.1    Comfurius, P.2    Bevers, E.M.3
  • 87
    • 0032748399 scopus 로고    scopus 로고
    • Phosphatidylserine-related adhesion of human erythrocytes to vascular endothelium
    • Closse, C.; Dachary-Prigent, J.; Boisseau, M.R. Phosphatidylserine-related adhesion of human erythrocytes to vascular endothelium. Br. J. Haematol. 1999, 107, 300–302.
    • (1999) Br. J. Haematol , vol.107 , pp. 300-302
    • Closse, C.1    Dachary-Prigent, J.2    Boisseau, M.R.3
  • 88
    • 0038481238 scopus 로고    scopus 로고
    • Altered erythrocyte endothelial adherence and membrane phospholipid asymmetry in hereditary hydrocytosis
    • Gallagher, P.G.; Chang, S.H.; Rettig, M.P.; Neely, J.E.; Hillery, C.A.; Smith, B.D.; Low, P.S. Altered erythrocyte endothelial adherence and membrane phospholipid asymmetry in hereditary hydrocytosis. Blood 2003, 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    Smith, B.D.6    Low, P.S.7
  • 90
    • 0029817966 scopus 로고    scopus 로고
    • Increased erythrocyte phosphatidylserine exposure in sickle cell disease: Flow-cytometric measurement and clinical associations
    • Wood, B.L.; Gibson, D.F.; Tait, J.F. Increased erythrocyte phosphatidylserine exposure in sickle cell disease: Flow-cytometric measurement and clinical associations. Blood 1996, 88, 1873–1880.
    • (1996) Blood , vol.88 , pp. 1873-1880
    • Wood, B.L.1    Gibson, D.F.2    Tait, J.F.3


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