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Volumn 195, Issue 2, 2004, Pages 182-193

Plant-derived abrin-a induces apoptosis in cultured leukemic cell lines by different mechanisms

Author keywords

Abrin a; Acute lymphoblastic leukemia; ALL; Apoptosis; Caspase activity; DNA fragmentation; FITC; Fluorescein isothiocyanate; PBS ( ); Phosphatidylserine translocation

Indexed keywords

ABRIN; CASPASE 3; CASPASE 8; CASPASE 9; PHOSPHATIDYLSERINE;

EID: 1442348468     PISSN: 0041008X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.taap.2003.11.018     Document Type: Article
Times cited : (32)

References (37)
  • 1
    • 0036899079 scopus 로고    scopus 로고
    • Apoptosomes: Engines for caspase activation
    • Adams J.M., Cory S. Apoptosomes: engines for caspase activation. Curr. Opin. Cell Biol. 14:2002;715-720.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 715-720
    • Adams, J.M.1    Cory, S.2
  • 3
    • 0037344678 scopus 로고    scopus 로고
    • Therapeutic activation of caspases in cancer: A question of selectivity
    • Beauparlant P., Shore G.C. Therapeutic activation of caspases in cancer: a question of selectivity. Curr. Opin. Drug Discovery Dev. 6:2003;179-187.
    • (2003) Curr. Opin. Drug Discovery Dev. , vol.6 , pp. 179-187
    • Beauparlant, P.1    Shore, G.C.2
  • 4
    • 0029944848 scopus 로고    scopus 로고
    • Effect of membrane potential on phosphatidylserine synthesis and calcium movements in control and CD3-activated Jurkat T cells
    • Breintmayer J.P., Pelassy C., Aussel C. Effect of membrane potential on phosphatidylserine synthesis and calcium movements in control and CD3-activated Jurkat T cells. J. Lipid Mediators Cell Signalling. 13:1996;151-161.
    • (1996) J. Lipid Mediators Cell Signalling , vol.13 , pp. 151-161
    • Breintmayer, J.P.1    Pelassy, C.2    Aussel, C.3
  • 6
    • 0027499070 scopus 로고
    • The use of ATP bioluminescence as a measure of cell proliferation and cytotoxicity
    • Crouch S.P.M. The use of ATP bioluminescence as a measure of cell proliferation and cytotoxicity. J. Immunol. Methods. 160:1993;81-88.
    • (1993) J. Immunol. Methods , vol.160 , pp. 81-88
    • Crouch, S.P.M.1
  • 8
    • 0023664263 scopus 로고
    • The mechanism of action of ricin and related toxic lectins on eukaryotic ribosomes. The site and the characteristics of the modification in 28 S ribosomal RNA caused by the toxins
    • Endo Y., Mitsui K., Motizuki M., Tsurugi K. The mechanism of action of ricin and related toxic lectins on eukaryotic ribosomes. The site and the characteristics of the modification in 28 S ribosomal RNA caused by the toxins. J. Biol. Chem. 262:1987;5908-5912.
    • (1987) J. Biol. Chem. , vol.262 , pp. 5908-5912
    • Endo, Y.1    Mitsui, K.2    Motizuki, M.3    Tsurugi, K.4
  • 10
    • 0025886113 scopus 로고
    • Single-chain ribosome inactivating proteins from plants depurinate Escherichia coli 23S ribosomal RNA
    • Hartley M.R., Legname G., Osborn R., Chen Z., Lord J.M. Single-chain ribosome inactivating proteins from plants depurinate Escherichia coli 23S ribosomal RNA. FEBS Lett. 290(1-2):1991;65-68.
    • (1991) FEBS Lett. , vol.290 , Issue.12 , pp. 65-68
    • Hartley, M.R.1    Legname, G.2    Osborn, R.3    Chen, Z.4    Lord, J.M.5
  • 11
    • 0031213763 scopus 로고    scopus 로고
    • A- and B-subunit variant distribution in the holoprotein variants of protein toxin abrin: Variants of abrins I and III have constant toxic a subunits and variant lectin B subunits
    • Hegde R., Podder S.K. A- and B-subunit variant distribution in the holoprotein variants of protein toxin abrin: variants of abrins I and III have constant toxic A subunits and variant lectin B subunits. Arch. Biochem. Biophys. 344(1):1997;75-84.
    • (1997) Arch. Biochem. Biophys. , vol.344 , Issue.1 , pp. 75-84
    • Hegde, R.1    Podder, S.K.2
  • 12
    • 0027320749 scopus 로고
    • The variants of the protein toxins abrin and ricin. A useful guide to understanding the processing events in the toxin transport
    • Hegde R., Karande A.A., Podder S.K. The variants of the protein toxins abrin and ricin. A useful guide to understanding the processing events in the toxin transport. Eur. J. Biochem. 215(2):1993;411-419.
    • (1993) Eur. J. Biochem. , vol.215 , Issue.2 , pp. 411-419
    • Hegde, R.1    Karande, A.A.2    Podder, S.K.3
  • 13
    • 0032478614 scopus 로고    scopus 로고
    • Blk, a BH3-containing mouse protein that interacts with Bcl-2 and Bcl-xL, is a potent death agonist
    • Hegde R., Srinivasula S.M., Ahmad M., Fernandes-Alnemri T., Alnemri E.S. Blk, a BH3-containing mouse protein that interacts with Bcl-2 and Bcl-xL, is a potent death agonist. J. Biol. Chem. 273:1998;7783-7786.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7783-7786
    • Hegde, R.1    Srinivasula, S.M.2    Ahmad, M.3    Fernandes-Alnemri, T.4    Alnemri, E.S.5
  • 14
    • 0035010412 scopus 로고    scopus 로고
    • An insight into the mechanism of cytotoxicity of ricin to hepatoma cell: Roles of Bcl-2 family proteins, caspases, Ca(2+)-dependent proteases and protein kinase C
    • Hu R., Zhai Q., Liu W., Liu X. An insight into the mechanism of cytotoxicity of ricin to hepatoma cell: roles of Bcl-2 family proteins, caspases, Ca(2+)-dependent proteases and protein kinase C. J. Cell. Biochem. 81:2001;583-593.
    • (2001) J. Cell. Biochem. , vol.81 , pp. 583-593
    • Hu, R.1    Zhai, Q.2    Liu, W.3    Liu, X.4
  • 15
    • 0029918819 scopus 로고    scopus 로고
    • Quantitation of DNA fragmentation in apoptosis
    • Ioannou Y.A., Chen F.W. Quantitation of DNA fragmentation in apoptosis. Nucleic Acids Res. 24:1996;992-993.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 992-993
    • Ioannou, Y.A.1    Chen, F.W.2
  • 16
    • 0032394928 scopus 로고    scopus 로고
    • Role of caspases in immunotoxin-induced apoptosis of cancer cells
    • Keppler-Hafkemeyer A., Brinkmann U., Pastan I. Role of caspases in immunotoxin-induced apoptosis of cancer cells. Biochemistry. 37:1998;16934-16942.
    • (1998) Biochemistry , vol.37 , pp. 16934-16942
    • Keppler-Hafkemeyer, A.1    Brinkmann, U.2    Pastan, I.3
  • 17
    • 0033000042 scopus 로고    scopus 로고
    • Diphtheria toxin fused to granulocyte-macrophage colony-stimulating factor and Ara-C exert synergistic toxicity against human AML HL-60 cells
    • Kim C.N., Bhalla K., Kreitman R.J., Willingham M.C., Hall P., Tagge E.P., Jia T., Frankel A.E. Diphtheria toxin fused to granulocyte-macrophage colony-stimulating factor and Ara-C exert synergistic toxicity against human AML HL-60 cells. Leuk. Res. 23:1999;527-538.
    • (1999) Leuk. Res. , vol.23 , pp. 527-538
    • Kim, C.N.1    Bhalla, K.2    Kreitman, R.J.3    Willingham, M.C.4    Hall, P.5    Tagge, E.P.6    Jia, T.7    Frankel, A.E.8
  • 18
    • 0031727477 scopus 로고    scopus 로고
    • Involvement of both caspase-like proteases and serine proteases in apoptotic cell death induced by ricin, modeccin, diphtheria toxin, and Pseudomonas toxin
    • Komatsu N., Oda T., Muramatsu T. Involvement of both caspase-like proteases and serine proteases in apoptotic cell death induced by ricin, modeccin, diphtheria toxin, and Pseudomonas toxin. J. Biochem. 124:1998;1038-1044.
    • (1998) J. Biochem. , vol.124 , pp. 1038-1044
    • Komatsu, N.1    Oda, T.2    Muramatsu, T.3
  • 19
    • 0035194166 scopus 로고    scopus 로고
    • Matrix protein and another viral component contribute to induction of apoptosis in cells infected with vesicular stomatitis virus
    • Kopecky S.A., Willingham M.C., Lyles D.S. Matrix protein and another viral component contribute to induction of apoptosis in cells infected with vesicular stomatitis virus. J. Virol. 75:2001;12169-12181.
    • (2001) J. Virol. , vol.75 , pp. 12169-12181
    • Kopecky, S.A.1    Willingham, M.C.2    Lyles, D.S.3
  • 20
    • 0019460964 scopus 로고
    • Isolation of four isotoxic proteins and one agglutinin from jequiriti bean (Abrus precatorius)
    • Lin J.Y., Lee T.C., Hu S.T., Tung T.C. Isolation of four isotoxic proteins and one agglutinin from jequiriti bean (Abrus precatorius). Toxicon. 19:1980;41-51.
    • (1980) Toxicon , vol.19 , pp. 41-51
    • Lin, J.Y.1    Lee, T.C.2    Hu, S.T.3    Tung, T.C.4
  • 21
    • 0034695623 scopus 로고    scopus 로고
    • Primary structure and function analysis of the Abrus precatorius agglutinin a chain by site-directed mutagenesis. Pro(199) of amphiphilic alpha-helix H impairs protein synthesis inhibitory activity
    • Liu C.L., Tsai C.C., Lin S.C., Wang L.I., Hsu C.I., Hwang M.J., Lin J.Y. Primary structure and function analysis of the Abrus precatorius agglutinin A chain by site-directed mutagenesis. Pro(199) of amphiphilic alpha-helix H impairs protein synthesis inhibitory activity. J. Biol. Chem. 275:2000;1897-1901.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1897-1901
    • Liu, C.L.1    Tsai, C.C.2    Lin, S.C.3    Wang, L.I.4    Hsu, C.I.5    Hwang, M.J.6    Lin, J.Y.7
  • 22
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • Luo X., Budihardjo I., Zou H., Slaughter C., Wang X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell. 94:1998;481-490.
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 23
    • 0028891783 scopus 로고
    • Apoptosis, oncosis, and necrosis. An overview of cell death
    • Majno G., Joris I. Apoptosis, oncosis, and necrosis. An overview of cell death. Am. J. Pathol. 146:1995;3-15.
    • (1995) Am. J. Pathol. , vol.146 , pp. 3-15
    • Majno, G.1    Joris, I.2
  • 25
    • 0031126382 scopus 로고    scopus 로고
    • Spectroscopic analysis of the cytoagglutination activity of abrin-b isolated from Abrus precatorius seeds against leukemic cells
    • Ohba H., Toyokawa T., Yasuda S., Hoshino T., Itoh K., Yamasaki N. Spectroscopic analysis of the cytoagglutination activity of abrin-b isolated from Abrus precatorius seeds against leukemic cells. Biosci., Biotechnol., Biochem. 61:1997;737-739.
    • (1997) Biosci., Biotechnol., Biochem. , vol.61 , pp. 737-739
    • Ohba, H.1    Toyokawa, T.2    Yasuda, S.3    Hoshino, T.4    Itoh, K.5    Yamasaki, N.6
  • 26
    • 0015972554 scopus 로고
    • Isolation and comparison of galactose-binding lectins from Abrus precatorius and Ricinus communis
    • Olsnes S., Saltvedt E., Pihl A. Isolation and comparison of galactose-binding lectins from Abrus precatorius and Ricinus communis. J. Biol. Chem. 249:1974;803-810.
    • (1974) J. Biol. Chem. , vol.249 , pp. 803-810
    • Olsnes, S.1    Saltvedt, E.2    Pihl, A.3
  • 27
    • 0032502855 scopus 로고    scopus 로고
    • Activation of caspases triggered by cytochrome c in vitro
    • Pan G., Humke E.W., Dixit V.M. Activation of caspases triggered by cytochrome c in vitro. FEBS Lett. 426:1998;151-154.
    • (1998) FEBS Lett. , vol.426 , pp. 151-154
    • Pan, G.1    Humke, E.W.2    Dixit, V.M.3
  • 28
    • 0033977060 scopus 로고    scopus 로고
    • Regulation of phosphatidylserine exposure at the cell surface by the serine-base exchange enzyme system during CD95-induced apoptosis
    • Pelassy C., Breittmayer J.P., Aussel C. Regulation of phosphatidylserine exposure at the cell surface by the serine-base exchange enzyme system during CD95-induced apoptosis. Biochem. Pharmacol. 59:2000;855-863.
    • (2000) Biochem. Pharmacol. , vol.59 , pp. 855-863
    • Pelassy, C.1    Breittmayer, J.P.2    Aussel, C.3
  • 29
    • 0035877840 scopus 로고    scopus 로고
    • Abrin triggers cell death by inactivating a thiol-specific antioxidant protein
    • Shin S.-F., Wu Y.-H., Hung C.-H., Yang H.-Y., Lin J.-Y. Abrin triggers cell death by inactivating a thiol-specific antioxidant protein. J. Biol. Chem. 276:2001;21870-21877.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21870-21877
    • Shin, S.-F.1    Wu, Y.-H.2    Hung, C.-H.3    Yang, H.-Y.4    Lin, J.-Y.5
  • 30
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U.S.A. 76:1979;4350-4354.
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 32
    • 0031985647 scopus 로고    scopus 로고
    • Annexin V-affinity assay: A review on an apoptosis detection system based on phosphatidylserine exposure
    • Van Engeland M., Nieland L.J., Ramaekers F.C., Schutte B., Reutelingsperger C.P. Annexin V-affinity assay: a review on an apoptosis detection system based on phosphatidylserine exposure. Cytometry. 31:1998;1-9.
    • (1998) Cytometry , vol.31 , pp. 1-9
    • Van Engeland, M.1    Nieland, L.J.2    Ramaekers, F.C.3    Schutte, B.4    Reutelingsperger, C.P.5
  • 33
    • 0029043888 scopus 로고
    • A novel assay for apoptosis. Flow cytometric detection of phosphatidylserine expression on early apoptotic cells using fluorescein labelled Annexin V
    • Vermes I., Haanen C., Steffens-Nakken H., Reutelingsperger C. A novel assay for apoptosis. Flow cytometric detection of phosphatidylserine expression on early apoptotic cells using fluorescein labelled Annexin V. J. Immunol. Methods. 184:1995;39-51.
    • (1995) J. Immunol. Methods , vol.184 , pp. 39-51
    • Vermes, I.1    Haanen, C.2    Steffens-Nakken, H.3    Reutelingsperger, C.4
  • 34
    • 0033979708 scopus 로고    scopus 로고
    • Induction of apoptosis by mistletoe lectin I and its subunits. No evidence for cytotoxic effects caused by isolated A- and B-chains
    • Vervecken W., Kleff S., Pfuller U., Bussing A. Induction of apoptosis by mistletoe lectin I and its subunits. No evidence for cytotoxic effects caused by isolated A- and B-chains. Int. J. Biochem. Cell Biol. 32:2000;317-326.
    • (2000) Int. J. Biochem. Cell Biol. , vol.32 , pp. 317-326
    • Vervecken, W.1    Kleff, S.2    Pfuller, U.3    Bussing, A.4
  • 35
    • 0016233130 scopus 로고
    • Purification and characterization of two major toxic proteins from seeds of Abrus precatorius
    • Wei C.H., Hartman F.C., Pfuderer P., Yang W.K. Purification and characterization of two major toxic proteins from seeds of Abrus precatorius. J. Biol. Chem. 249:1974;3061-3067.
    • (1974) J. Biol. Chem. , vol.249 , pp. 3061-3067
    • Wei, C.H.1    Hartman, F.C.2    Pfuderer, P.3    Yang, W.K.4
  • 36
    • 0034279897 scopus 로고    scopus 로고
    • DNA fragmentation in apoptosis
    • Zhang J.H., Xu M. DNA fragmentation in apoptosis. Cell Res. 10:2000;205-211.
    • (2000) Cell Res. , vol.10 , pp. 205-211
    • Zhang, J.H.1    Xu, M.2
  • 37
    • 0035800806 scopus 로고    scopus 로고
    • Ionizing radiation-induced apoptosis in ataxia-telangiectasia fibroblasts. Roles of caspase-9 and cellular inhibitor of apoptosis protein-1
    • Zhang Y., Dimtchev A., Dritschilo A., Jung M. Ionizing radiation-induced apoptosis in ataxia-telangiectasia fibroblasts. Roles of caspase-9 and cellular inhibitor of apoptosis protein-1. J. Biol. Chem. 276:2001;28842-28848.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28842-28848
    • Zhang, Y.1    Dimtchev, A.2    Dritschilo, A.3    Jung, M.4


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