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Volumn 116, Issue 6, 2015, Pages 460-467

Enhanced Eryptosis Following Juglone Exposure

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CALCIUM ION; CERAMIDE; JUGLONE; LIPOCORTIN 5; PHOSPHATIDYLSERINE; PROTEIN KINASE C; ANTINEOPLASTIC AGENT; CALCIUM; NAPHTHOQUINONE;

EID: 84928726376     PISSN: 17427835     EISSN: 17427843     Source Type: Journal    
DOI: 10.1111/bcpt.12340     Document Type: Article
Times cited : (16)

References (121)
  • 1
    • 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;23:3631-4.
    • (2013) Bioorg Med Chem Lett , vol.23 , pp. 3631-3634
    • Xu, H.1    Yu, X.2    Qu, S.3    Sui, D.4
  • 3
    • 79958800036 scopus 로고    scopus 로고
    • Tumor growth inhibitory effect of juglone and its radiation sensitizing potential: in vivo and in vitro studies
    • Aithal KB, Kumar S, Rao BN, Udupa N, Rao SB. 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
  • 4
    • 33646806762 scopus 로고    scopus 로고
    • Interactions of nitroaromatic compounds with the mammalian selenoprotein thioredoxin reductase and the relation to induction of apoptosis in human cancer cells
    • Cenas N, Prast S, Nivinskas H, Sarlauskas J, Arner ES. Interactions of nitroaromatic compounds with the mammalian selenoprotein thioredoxin reductase and the relation to induction of apoptosis in human cancer cells. J Biol Chem 2006;281:5593-603.
    • (2006) J Biol Chem , vol.281 , pp. 5593-5603
    • Cenas, N.1    Prast, S.2    Nivinskas, H.3    Sarlauskas, J.4    Arner, E.S.5
  • 5
    • 84861465335 scopus 로고    scopus 로고
    • Phosphoinositol 3-kinase, a novel target molecule for the inhibitory effects of juglone on TPA-induced cell transformation
    • Chae JI, Cho JH, Kim DJ, Lee KA, Cho MK, Nam HS et al. 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
  • 6
    • 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 MT, 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
  • 7
    • 77956184488 scopus 로고    scopus 로고
    • Anti-proliferative effect of Juglone from Juglans mandshurica Maxim on human leukemia cell HL-60 by inducing apoptosis through the mitochondria-dependent pathway
    • Xu HL, Yu XF, Qu SC, Zhang R, Qu XR, Chen YP et al. Anti-proliferative effect of Juglone from Juglans mandshurica Maxim on human leukemia cell HL-60 by inducing apoptosis through the mitochondria-dependent pathway. Eur J Pharmacol 2010;645:14-22.
    • (2010) Eur J Pharmacol , vol.645 , pp. 14-22
    • Xu, H.L.1    Yu, X.F.2    Qu, S.C.3    Zhang, R.4    Qu, X.R.5    Chen, Y.P.6
  • 8
    • 84881224985 scopus 로고    scopus 로고
    • The peptidyl-prolyl isomerase Pin1 up-regulation and proapoptotic function in dopaminergic neurons: relevance to the pathogenesis of Parkinson disease
    • Ghosh A, Saminathan H, Kanthasamy A, Anantharam V, Jin H, Sondarva G et al. The peptidyl-prolyl isomerase Pin1 up-regulation and proapoptotic function in dopaminergic neurons: relevance to the pathogenesis of Parkinson disease. J Biol Chem 2013;288:21955-71.
    • (2013) J Biol Chem , vol.288 , pp. 21955-21971
    • Ghosh, A.1    Saminathan, H.2    Kanthasamy, A.3    Anantharam, V.4    Jin, H.5    Sondarva, G.6
  • 9
    • 84888201852 scopus 로고    scopus 로고
    • Essential role of Pin1 via STAT3 signalling and mitochondria-dependent pathways in restenosis in type 2 diabetes
    • Lv L, Zhang J, Zhang L, Xue G, Wang P, Meng Q et al. Essential role of Pin1 via STAT3 signalling and mitochondria-dependent pathways in restenosis in type 2 diabetes. J Cell Mol Med 2013;17:989-1005.
    • (2013) J Cell Mol Med , vol.17 , pp. 989-1005
    • Lv, L.1    Zhang, J.2    Zhang, L.3    Xue, G.4    Wang, P.5    Meng, Q.6
  • 10
    • 69549105800 scopus 로고    scopus 로고
    • Juglone, a naphthoquinone from walnut, exerts cytotoxic and genotoxic effects against cultured melanoma tumor cells
    • Aithal BK, Kumar MR, Rao BN, Udupa N, Rao BS. Juglone, a naphthoquinone from walnut, exerts cytotoxic and genotoxic effects against cultured melanoma tumor cells. Cell Biol Int 2009;33:1039-49.
    • (2009) Cell Biol Int , vol.33 , pp. 1039-1049
    • Aithal, B.K.1    Kumar, M.R.2    Rao, B.N.3    Udupa, N.4    Rao, B.S.5
  • 11
    • 78650171632 scopus 로고    scopus 로고
    • Juglone-induced apoptosis in human gastric cancer SGC-7901 cells via the mitochondrial pathway
    • Ji YB, Qu ZY, Zou X. Juglone-induced apoptosis in human gastric cancer SGC-7901 cells via the mitochondrial pathway. Exp Toxicol Pathol 2011;63:69-78.
    • (2011) Exp Toxicol Pathol , vol.63 , pp. 69-78
    • Ji, Y.B.1    Qu, Z.Y.2    Zou, X.3
  • 13
    • 80255131064 scopus 로고    scopus 로고
    • Plumbagin and juglone induce caspase-3-dependent apoptosis involving the mitochondria through ROS generation in human peripheral blood lymphocytes
    • Seshadri P, Rajaram A, Rajaram R. Plumbagin and juglone induce caspase-3-dependent apoptosis involving the mitochondria through ROS generation in human peripheral blood lymphocytes. Free Radic Biol Med 2011;51:2090-107.
    • (2011) Free Radic Biol Med , vol.51 , pp. 2090-2107
    • Seshadri, P.1    Rajaram, A.2    Rajaram, R.3
  • 14
    • 84863232732 scopus 로고    scopus 로고
    • Juglone, from Juglans mandshruica Maxim, inhibits growth and induces apoptosis in human leukemia cell HL-60 through a reactive oxygen species-dependent mechanism
    • Xu HL, Yu XF, Qu SC, Qu XR, Jiang YF, Sui da Y. Juglone, from Juglans mandshruica Maxim, inhibits growth and induces apoptosis in human leukemia cell HL-60 through a reactive oxygen species-dependent mechanism. Food Chem Toxicol 2012;50:590-6.
    • (2012) Food Chem Toxicol , vol.50 , pp. 590-596
    • Xu, H.L.1    Yu, X.F.2    Qu, S.C.3    Qu, X.R.4    Jiang, Y.F.5    Sui da, Y.6
  • 15
    • 84855712104 scopus 로고    scopus 로고
    • Pin1 inhibition activates cyclin D and produces neurodegenerative pathology
    • Atabay KD, Karabay A. Pin1 inhibition activates cyclin D and produces neurodegenerative pathology. J Neurochem 2012;120:430-9.
    • (2012) J Neurochem , vol.120 , pp. 430-439
    • Atabay, K.D.1    Karabay, A.2
  • 18
    • 34548490722 scopus 로고    scopus 로고
    • Inhibition of Pin1 reduces glutamate-induced perikaryal accumulation of phosphorylated neurofilament-H in neurons
    • Kesavapany S, Patel V, Zheng YL, Pareek TK, Bjelogrlic M, Albers W et al. Inhibition of Pin1 reduces glutamate-induced perikaryal accumulation of phosphorylated neurofilament-H in neurons. Mol Biol Cell 2007;18:3645-55.
    • (2007) Mol Biol Cell , vol.18 , pp. 3645-3655
    • Kesavapany, S.1    Patel, V.2    Zheng, Y.L.3    Pareek, T.K.4    Bjelogrlic, M.5    Albers, W.6
  • 19
    • 79951708802 scopus 로고    scopus 로고
    • Peptidyl prolyl isomerase, Pin1 is a potential target for enhancing the therapeutic efficacy of etoposide
    • Mathur R, Chandna S, N Kapoor P, S Dwarakanath B. Peptidyl prolyl isomerase, Pin1 is a potential target for enhancing the therapeutic efficacy of etoposide. Curr Cancer Drug Targets 2011;11:380-92.
    • (2011) Curr Cancer Drug Targets , vol.11 , pp. 380-392
    • Mathur, R.1    Chandna, S.2    Kapoor, P.N.3    Dwarakanath, B.S.4
  • 20
    • 84878425446 scopus 로고    scopus 로고
    • Pin1 is required for ultraviolet A-stimulated cyclooxygenase-2 induction in mouse epidermal cells
    • Quyen BT, Choi HK, Kang KW. Pin1 is required for ultraviolet A-stimulated cyclooxygenase-2 induction in mouse epidermal cells. Cancer Lett 2013;335:31-40.
    • (2013) Cancer Lett , vol.335 , pp. 31-40
    • Quyen, B.T.1    Choi, H.K.2    Kang, K.W.3
  • 21
    • 0033854422 scopus 로고    scopus 로고
    • Phosphorylation-dependent proline isomerization catalyzed by Pin1 is essential for tumor cell survival and entry into mitosis
    • Rippmann JF, Hobbie S, Daiber C, Guilliard B, Bauer M, Birk J et al. Phosphorylation-dependent proline isomerization catalyzed by Pin1 is essential for tumor cell survival and entry into mitosis. Cell Growth Differ 2000;11:409-16.
    • (2000) Cell Growth Differ , vol.11 , pp. 409-416
    • Rippmann, J.F.1    Hobbie, S.2    Daiber, C.3    Guilliard, B.4    Bauer, M.5    Birk, J.6
  • 22
    • 70349112569 scopus 로고    scopus 로고
    • The rotamase Pin1 is up-regulated, hypophosphorylated and required for cell cycle progression in head and neck squamous cell carcinomas
    • Wiegand S, Dakic B, Rath AF, Makarova G, Sterz C, Meissner W et al. The rotamase Pin1 is up-regulated, hypophosphorylated and required for cell cycle progression in head and neck squamous cell carcinomas. Oral Oncol 2009;45:e140-9.
    • (2009) Oral Oncol , vol.45 , pp. e140-e149
    • Wiegand, S.1    Dakic, B.2    Rath, A.F.3    Makarova, G.4    Sterz, C.5    Meissner, W.6
  • 23
    • 72449205615 scopus 로고    scopus 로고
    • Pin1 as an anticancer drug target
    • Xu GG, Etzkorn FA. Pin1 as an anticancer drug target. Drug News Perspect 2009;22:399-407.
    • (2009) Drug News Perspect , vol.22 , pp. 399-407
    • Xu, G.G.1    Etzkorn, F.A.2
  • 24
    • 84861418715 scopus 로고    scopus 로고
    • Killing me softly - suicidal erythrocyte death
    • Lang E, Qadri SM, Lang F. Killing me softly - suicidal erythrocyte death. Int J Biochem Cell Biol 2012;44:1236-43.
    • (2012) Int J Biochem Cell Biol , vol.44 , pp. 1236-1243
    • Lang, E.1    Qadri, S.M.2    Lang, F.3
  • 29
    • 70350236408 scopus 로고    scopus 로고
    • Participation of leukotriene C(4) in the regulation of suicidal erythrocyte death
    • Foller M, Mahmud H, Gu S, Wang K, Floride E, Kucherenko Y et al. Participation of leukotriene C(4) in the regulation of suicidal erythrocyte death. J Physiol Pharmacol 2009;60:135-43.
    • (2009) J Physiol Pharmacol , vol.60 , pp. 135-143
    • Foller, M.1    Mahmud, H.2    Gu, S.3    Wang, K.4    Floride, E.5    Kucherenko, Y.6
  • 30
    • 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 IP, Chen H, Wang J, Ong HC, Leung KC, Ho HP et al. In vitro effect of CTAB- and PEG-coated gold nanorods on the induction of eryptosis/erythroptosis in human erythrocytes. Nanotoxicology 2012;6:847-56.
    • (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
  • 31
    • 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 et al. Erythrocyte caspase-3 activation and oxidative imbalance in erythrocytes and in plasma of type 2 diabetic patients. Acta Diabetol 2013;50:489-95.
    • (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
  • 32
    • 65349138878 scopus 로고    scopus 로고
    • Regulation of erythrocyte survival by AMP-activated protein kinase
    • Foller M, Sopjani M, Koka S, Gu S, Mahmud H, Wang K et al. Regulation of erythrocyte survival by AMP-activated protein kinase. FASEB J 2009;23:1072-80.
    • (2009) FASEB J , vol.23 , pp. 1072-1080
    • Foller, M.1    Sopjani, M.2    Koka, S.3    Gu, S.4    Mahmud, H.5    Wang, K.6
  • 33
    • 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. Effect of casein kinase 1alpha activator pyrvinium pamoate on erythrocyte ion channels. Cell Physiol Biochem 2012;30:407-17.
    • (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
  • 35
    • 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. Janus kinase 3 is expressed in erythrocytes, phosphorylated upon energy depletion and involved in the regulation of suicidal erythrocyte death. Cell Physiol Biochem 2011;27:547-56.
    • (2011) Cell Physiol Biochem , vol.27 , pp. 547-556
    • Bhavsar, S.K.1    Gu, S.2    Bobbala, D.3    Lang, F.4
  • 38
    • 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, Viollet B et al. Proteome analysis of erythrocytes lacking AMP-activated protein kinase reveals a role of PAK2 kinase in eryptosis. J Proteome Res 2011;10:1690-7.
    • (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
  • 39
  • 40
    • 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;30:512-22.
    • (2012) Cell Physiol Biochem , vol.30 , pp. 512-522
    • Shaik, N.1    Lupescu, A.2    Lang, F.3
  • 41
    • 84868445257 scopus 로고    scopus 로고
    • Stimulation of suicidal death of erythrocytes by rifampicin
    • Abed M, Towhid ST, Shaik N, Lang F. Stimulation of suicidal death of erythrocytes by rifampicin. Toxicology 2012;302:123-8.
    • (2012) Toxicology , vol.302 , pp. 123-128
    • Abed, M.1    Towhid, S.T.2    Shaik, N.3    Lang, F.4
  • 42
    • 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. 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 , pp. e33774
    • Bottger, E.1    Multhoff, G.2    Kun, J.F.3    Esen, M.4
  • 43
    • 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, Dal MS et al. Increased caspase-3 immunoreactivity of erythrocytes in STZ diabetic rats. Exp Diabetes Res 2012;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    Dal, M.S.6
  • 44
    • 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. Understanding the mechanisms for metabolism-linked hemolytic toxicity of primaquine against glucose 6-phosphate dehydrogenase deficient human erythrocytes: evaluation of eryptotic pathway. Toxicology 2012;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
  • 45
    • 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, Yu B et al. Polyphyllin D induces apoptosis in human erythrocytes through Ca(2)(+) rise and membrane permeabilization. Arch Toxicol 2012;86:741-52.
    • (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    Yu, B.6
  • 48
    • 84893057981 scopus 로고    scopus 로고
    • Geldanamycin-induced phosphatidylserine translocation in the erythrocyte membrane
    • Jilani K, Qadri SM, Lang F. Geldanamycin-induced phosphatidylserine translocation in the erythrocyte membrane. Cell Physiol Biochem 2013;32:1600-9.
    • (2013) Cell Physiol Biochem , vol.32 , pp. 1600-1609
    • Jilani, K.1    Qadri, S.M.2    Lang, F.3
  • 49
    • 84865056373 scopus 로고    scopus 로고
    • Inhibitory Effect of Furosemide on Non-Selective Voltage-Independent Cation Channels in Human Erythrocytes
    • Kucherenko YV, Lang F. Inhibitory Effect of Furosemide on Non-Selective Voltage-Independent Cation Channels in Human Erythrocytes. Cell Physiol Biochem 2012;30:863-75.
    • (2012) Cell Physiol Biochem , vol.30 , pp. 863-875
    • Kucherenko, Y.V.1    Lang, F.2
  • 50
    • 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. Enhanced ca(2 + ) entry, ceramide formation, and apoptotic death of erythrocytes triggered by plumbagin. J Nat Prod 2012;75:1956-61.
    • (2012) J Nat Prod , vol.75 , pp. 1956-1961
    • Lupescu, A.1    Jilani, K.2    Zbidah, M.3    Lang, E.4    Lang, F.5
  • 51
    • 84864070776 scopus 로고    scopus 로고
    • Induction of apoptotic erythrocyte death by rotenone
    • Lupescu A, Jilani K, Zbidah M, Lang F. Induction of apoptotic erythrocyte death by rotenone. Toxicology 2012;300:132-7.
    • (2012) Toxicology , vol.300 , pp. 132-137
    • Lupescu, A.1    Jilani, K.2    Zbidah, M.3    Lang, F.4
  • 52
    • 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;34:209-10.
    • (2012) Blood Purif , vol.34 , pp. 209-210
    • Polak-Jonkisz, D.1    Purzyc, L.2
  • 53
    • 84860322995 scopus 로고    scopus 로고
    • Salidroside protects human erythrocytes against hydrogen peroxide-induced apoptosis
    • Qian EW, Ge DT, Kong SK. Salidroside protects human erythrocytes against hydrogen peroxide-induced apoptosis. J Nat Prod 2012;75:531-7.
    • (2012) J Nat Prod , vol.75 , pp. 531-537
    • Qian, E.W.1    Ge, D.T.2    Kong, S.K.3
  • 54
    • 84864397354 scopus 로고    scopus 로고
    • Inhibition of Ca(2 + ) entry and suicidal erythrocyte death by naringin
    • Shaik N, Zbidah M, Lang F. Inhibition of Ca(2 + ) entry and suicidal erythrocyte death by naringin. Cell Physiol Biochem 2012;30:678-86.
    • (2012) Cell Physiol Biochem , vol.30 , pp. 678-686
    • Shaik, N.1    Zbidah, M.2    Lang, F.3
  • 56
    • 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. Deoxygenation-induced and Ca(2 + ) dependent phosphatidylserine externalisation in red blood cells from normal individuals and sickle cell patients. Cell Calcium 2012;51:51-6.
    • (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
  • 57
    • 45149094904 scopus 로고    scopus 로고
    • Environmental stress, erythrocyte dysfunctions, inflammation, and the metabolic syndrome: adaptations to CO2 increases?
    • Zappulla D. Environmental stress, erythrocyte dysfunctions, inflammation, and the metabolic syndrome: adaptations to CO2 increases? J Cardiometab Syndr 2008;3:30-4.
    • (2008) J Cardiometab Syndr , vol.3 , pp. 30-34
    • Zappulla, D.1
  • 59
    • 84868496151 scopus 로고    scopus 로고
    • Gossypol-induced suicidal erythrocyte death
    • Zbidah M, Lupescu A, Shaik N, Lang F. Gossypol-induced suicidal erythrocyte death. Toxicology 2012;302:101-5.
    • (2012) Toxicology , vol.302 , pp. 101-105
    • Zbidah, M.1    Lupescu, A.2    Shaik, N.3    Lang, F.4
  • 63
    • 84888182490 scopus 로고    scopus 로고
    • Age Sensitivity of NFkappaB Abundance and Programmed Cell Death in Erythrocytes Induced by NFkappaB Inhibitors
    • Ghashghaeinia M, Cluitmans JC, Toulany M, Saki M, Koberle M, Lang E et al. Age Sensitivity of NFkappaB Abundance and Programmed Cell Death in Erythrocytes Induced by NFkappaB Inhibitors. Cell Physiol Biochem 2013;32:801-13.
    • (2013) Cell Physiol Biochem , vol.32 , pp. 801-813
    • Ghashghaeinia, M.1    Cluitmans, J.C.2    Toulany, M.3    Saki, M.4    Koberle, M.5    Lang, E.6
  • 65
    • 84891361707 scopus 로고    scopus 로고
    • Triggering of Suicidal Erythrocyte Death by Penta-O-galloyl-beta-d-glucose
    • Alzoubi K, Honisch S, Abed M, Lang F. Triggering of Suicidal Erythrocyte Death by Penta-O-galloyl-beta-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
  • 66
    • 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;5:703-16.
    • (2013) Toxins (Basel) , vol.5 , pp. 703-716
    • Jilani, K.1    Lang, F.2
  • 68
    • 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;5:1543-54.
    • (2013) Toxins (Basel) , vol.5 , pp. 1543-1554
    • Lupescu, A.1    Bissinger, R.2    Jilani, K.3    Lang, F.4
  • 78
    • 84869396808 scopus 로고    scopus 로고
    • Withaferin A-stimulated Ca2 +  entry, ceramide formation and suicidal death of erythrocytes
    • Jilani K, Lupescu A, Zbidah M, Shaik N, Lang F. Withaferin A-stimulated Ca2 +  entry, ceramide formation and suicidal death of erythrocytes. Toxicol In Vitro 2013;27:52-8.
    • (2013) Toxicol In Vitro , vol.27 , pp. 52-58
    • Jilani, K.1    Lupescu, A.2    Zbidah, M.3    Shaik, N.4    Lang, F.5
  • 80
    • 80055099463 scopus 로고    scopus 로고
    • Triggering of erythrocyte cell membrane scrambling by ursolic acid
    • Jilani K, Abed M, Zelenak C, Lang E, Qadri SM, Lang F. Triggering of erythrocyte cell membrane scrambling by ursolic acid. J Nat Prod 2011;74:2181-6.
    • (2011) J Nat Prod , vol.74 , pp. 2181-2186
    • Jilani, K.1    Abed, M.2    Zelenak, C.3    Lang, E.4    Qadri, S.M.5    Lang, F.6
  • 84
    • 84895665358 scopus 로고    scopus 로고
    • Stimulation of suicidal erythrocyte death by increased extracellular phosphate concentrations
    • Voelkl J, Alzoubi K, Mamar AK, Ahmed MS, 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
  • 91
    • 0035469888 scopus 로고    scopus 로고
    • Short survival of phosphatidylserine-exposing red blood cells in murine sickle cell anemia
    • de Jong K, Emerson RK, Butler J, Bastacky J, Mohandas N, Kuypers FA. Short survival of phosphatidylserine-exposing red blood cells in murine sickle cell anemia. Blood 2001;98:1577-84.
    • (2001) Blood , vol.98 , pp. 1577-1584
    • de Jong, K.1    Emerson, R.K.2    Butler, J.3    Bastacky, J.4    Mohandas, N.5    Kuypers, F.A.6
  • 92
    • 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, Lang F. Suicide for survival-death of infected erythrocytes as a host mechanism to survive malaria. Cell Physiol Biochem 2009;24:133-40.
    • (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
  • 93
    • 0036265634 scopus 로고    scopus 로고
    • Comparison of mechanisms of anemia in mice with sickle cell disease and beta-thalassemia: peripheral destruction, ineffective erythropoiesis, and phospholipid scramblase-mediated phosphatidylserine exposure
    • Kean LS, Brown LE, Nichols JW, Mohandas N, Archer DR, Hsu LL. Comparison of mechanisms of anemia in mice with sickle cell disease and beta-thalassemia: peripheral destruction, ineffective erythropoiesis, and phospholipid scramblase-mediated phosphatidylserine exposure. Exp Hematol 2002;30:394-402.
    • (2002) Exp Hematol , vol.30 , pp. 394-402
    • Kean, L.S.1    Brown, L.E.2    Nichols, J.W.3    Mohandas, N.4    Archer, D.R.5    Hsu, L.L.6
  • 94
    • 51149091241 scopus 로고    scopus 로고
    • Influence of chlorpromazine on eryptosis, parasitemia and survival of Plasmodium berghei infected mice
    • Koka S, Lang C, Boini KM, Bobbala D, Huber SM, Lang F. Influence of chlorpromazine on eryptosis, parasitemia and survival of Plasmodium berghei infected mice. Cell Physiol Biochem 2008;22:261-8.
    • (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
  • 95
    • 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 OM, Boini KM, Nicolay JP, Huber SM et al. Influence of NO synthase inhibitor L-NAME on parasitemia and survival of Plasmodium berghei infected mice. Cell Physiol Biochem 2008;21:481-8.
    • (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
  • 96
    • 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;104:3364-71.
    • (2004) Blood , vol.104 , pp. 3364-3371
    • Ayi, K.1    Turrini, F.2    Piga, A.3    Arese, P.4
  • 97
    • 33847026927 scopus 로고    scopus 로고
    • Deoxygenation-induced non-electrolyte pathway in red cells from sickle cell patients
    • Browning JA, Robinson HC, Ellory JC, Gibson JS. Deoxygenation-induced non-electrolyte pathway in red cells from sickle cell patients. Cell Physiol Biochem 2007;19:165-74.
    • (2007) Cell Physiol Biochem , vol.19 , pp. 165-174
    • Browning, J.A.1    Robinson, H.C.2    Ellory, J.C.3    Gibson, J.S.4
  • 98
    • 69249169929 scopus 로고    scopus 로고
    • Delayed hemolytic transfusion reaction in sickle cell disease patients: evidence of an emerging syndrome with suicidal red blood cell death
    • Chadebech P, Habibi A, Nzouakou R, Bachir D, Meunier-Costes N, Bonin P et al. Delayed hemolytic transfusion reaction in sickle cell disease patients: evidence of an emerging syndrome with suicidal red blood cell death. Transfusion 2009;49:1785-92.
    • (2009) Transfusion , vol.49 , pp. 1785-1792
    • Chadebech, P.1    Habibi, A.2    Nzouakou, R.3    Bachir, D.4    Meunier-Costes, N.5    Bonin, P.6
  • 99
    • 0036432879 scopus 로고    scopus 로고
    • Enhanced erythrocyte apoptosis in sickle cell anemia, thalassemia and glucose-6-phosphate dehydrogenase deficiency
    • Lang KS, Roll B, Myssina S, Schittenhelm M, Scheel-Walter HG, Kanz L et al. Enhanced erythrocyte apoptosis in sickle cell anemia, thalassemia and glucose-6-phosphate dehydrogenase deficiency. Cell Physiol Biochem 2002;12:365-72.
    • (2002) Cell Physiol Biochem , vol.12 , pp. 365-372
    • Lang, K.S.1    Roll, B.2    Myssina, S.3    Schittenhelm, M.4    Scheel-Walter, H.G.5    Kanz, L.6
  • 100
    • 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. Increased erythrocyte phosphatidylserine exposure in sickle cell disease: flow-cytometric measurement and clinical associations. Blood 1996;88:1873-80.
    • (1996) Blood , vol.88 , pp. 1873-1880
    • Wood, B.L.1    Gibson, D.F.2    Tait, J.F.3
  • 101
    • 78651259720 scopus 로고    scopus 로고
    • Eryptosis in hereditary spherocytosis and thalassemia: role of glycoconjugates
    • Basu S, Banerjee D, Chandra S, Chakrabarti A. Eryptosis in hereditary spherocytosis and thalassemia: role of glycoconjugates. Glycoconj J 2010;27:717-22.
    • (2010) Glycoconj J , vol.27 , pp. 717-722
    • Basu, S.1    Banerjee, D.2    Chandra, S.3    Chakrabarti, A.4
  • 103
    • 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, Lupescu A et al. Liver cell death and anemia in Wilson disease involve acid sphingomyelinase and ceramide. Nat Med 2007;13:164-70.
    • (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    Lupescu, A.6
  • 105
    • 84860348582 scopus 로고    scopus 로고
    • Enhanced suicidal erythrocyte death in mice carrying a loss-of-function mutation of the adenomatous polyposis coli gene
    • Qadri SM, Mahmud H, Lang E, Gu S, Bobbala D, Zelenak C et al. Enhanced suicidal erythrocyte death in mice carrying a loss-of-function mutation of the adenomatous polyposis coli gene. J Cell Mol Med 2012;16:1085-93.
    • (2012) J Cell Mol Med , vol.16 , pp. 1085-1093
    • Qadri, S.M.1    Mahmud, H.2    Lang, E.3    Gu, S.4    Bobbala, D.5    Zelenak, C.6
  • 108
    • 1842661170 scopus 로고
    • The pathogenesis of the renal injury produced in the dog by hemoglobin or methemoglobin
    • Harrison HE, Bunting H, Ordway NK, Albrink WS. The pathogenesis of the renal injury produced in the dog by hemoglobin or methemoglobin. J Exp Med 1947;86:339-56.
    • (1947) J Exp Med , vol.86 , pp. 339-356
    • Harrison, H.E.1    Bunting, H.2    Ordway, N.K.3    Albrink, W.S.4
  • 109
    • 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 et al. Electrophysiological properties of the Plasmodium Falciparum-induced cation conductance of human erythrocytes. Cell Physiol Biochem 2003;13:189-98.
    • (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
  • 110
    • 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
  • 111
    • 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 PT, 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;46:3180-4.
    • (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
  • 112
    • 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 et al. Early phagocytosis of glucose-6-phosphate dehydrogenase (G6PD)-deficient erythrocytes parasitized by Plasmodium falciparum may explain malaria protection in G6PD deficiency. Blood 1998;92:2527-34.
    • (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
  • 116
    • 0032811978 scopus 로고    scopus 로고
    • Role of red blood cells in thrombosis
    • Andrews DA, Low PS. 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
  • 117
    • 33846444733 scopus 로고    scopus 로고
    • Lysophosphatidic acid induces thrombogenic activity through phosphatidylserine exposure and procoagulant microvesicle generation in human erythrocytes
    • Chung SM, Bae ON, Lim KM, Noh JY, Lee MY, Jung YS et al. Lysophosphatidic acid induces thrombogenic activity through phosphatidylserine exposure and procoagulant microvesicle generation in human erythrocytes. Arterioscler Thromb Vasc Biol 2007;27:414-21.
    • (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
  • 118
    • 18544381354 scopus 로고    scopus 로고
    • Surface exposure of phosphatidylserine in pathological cells
    • Zwaal RF, Comfurius P, Bevers EM. Surface exposure of phosphatidylserine in pathological cells. Cell Mol Life Sci 2005;62:971-88.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 971-988
    • Zwaal, R.F.1    Comfurius, P.2    Bevers, E.M.3
  • 119
    • 0032748399 scopus 로고    scopus 로고
    • Phosphatidylserine-related adhesion of human erythrocytes to vascular endothelium
    • Closse C, Dachary-Prigent J, Boisseau MR. Phosphatidylserine-related adhesion of human erythrocytes to vascular endothelium. Br J Haematol 1999;107:300-2.
    • (1999) Br J Haematol , vol.107 , pp. 300-302
    • Closse, C.1    Dachary-Prigent, J.2    Boisseau, M.R.3
  • 120
    • 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, Smith BD et al. Altered erythrocyte endothelial adherence and membrane phospholipid asymmetry in hereditary hydrocytosis. Blood 2003;101:4625-7.
    • (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
  • 121


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