메뉴 건너뛰기




Volumn 1487, Issue 2-3, 2000, Pages 296-308

Preferential externalization of newly synthesized phosphatidylserine in apoptotic U937 cells is dependent on caspase-mediated pathways

Author keywords

Apoptosis; Camptothecin; Caspase; Phosphatidylserine; Phospholipid; U937 cell

Indexed keywords

CAMPTOTHECIN; CASPASE; CASPASE INHIBITOR; DNA TOPOISOMERASE INHIBITOR; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLETHANOLAMINE; PHOSPHATIDYLSERINE; SPHINGOMYELIN; TUMOR NECROSIS FACTOR ALPHA;

EID: 0034721547     PISSN: 13881981     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1388-1981(00)00100-1     Document Type: Article
Times cited : (30)

References (51)
  • 1
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr J.F., Wyllie A.H., Currie A.R. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer. 26:1972;239-257.
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 2
    • 0030947095 scopus 로고    scopus 로고
    • Programmed cell death in animal development
    • Jacobson M.D., Weil M., Raff M.C. Programmed cell death in animal development. Cell. 88:1997;347-354.
    • (1997) Cell , vol.88 , pp. 347-354
    • Jacobson, M.D.1    Weil, M.2    Raff, M.C.3
  • 3
    • 0030790430 scopus 로고    scopus 로고
    • Cell death in the regulation of immune responses
    • Winoto A. Cell death in the regulation of immune responses. Curr. Opin. Immunol. 9:1997;365-370.
    • (1997) Curr. Opin. Immunol. , vol.9 , pp. 365-370
    • Winoto, A.1
  • 7
    • 0029845577 scopus 로고    scopus 로고
    • Signal transduction pathways in apoptosis
    • McConkey D.J., Orrenius S. Signal transduction pathways in apoptosis. Stem Cells. 14:1996;619-631.
    • (1996) Stem Cells , vol.14 , pp. 619-631
    • McConkey, D.J.1    Orrenius, S.2
  • 9
    • 0030931876 scopus 로고    scopus 로고
    • Caspases: The executioners of apoptosis
    • Cohen G.M. Caspases: the executioners of apoptosis. Biochem. J. 326:1997;1-16.
    • (1997) Biochem. J. , vol.326 , pp. 1-16
    • Cohen, G.M.1
  • 10
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry N.A., Lazebnik Y. Caspases: enemies within. Science. 281:1998;1312-1316.
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 11
    • 0033613143 scopus 로고    scopus 로고
    • Caspase activation: The induced-proximity model
    • Salvesen G.S., Dixit V.M. Caspase activation: the induced-proximity model. Proc. Natl. Acad. Sci. USA. 96:1999;10964-10967.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10964-10967
    • Salvesen, G.S.1    Dixit, V.M.2
  • 12
    • 0028800947 scopus 로고
    • Early redistribution of plasma membrane phosphatidylserine is a general feature of apoptosis regardless of the initiating stimulus: Inhibition by overexpression of Bcl-2 and Abl
    • Martin S.J., Reutelingsperger C.P., McGahon A.J., Rader J.A., vanSchie R.C., LaFace D.M., Green D.R. Early redistribution of plasma membrane phosphatidylserine is a general feature of apoptosis regardless of the initiating stimulus: inhibition by overexpression of Bcl-2 and Abl. J. Exp. Med. 182:1995;1545-1556.
    • (1995) J. Exp. Med. , vol.182 , pp. 1545-1556
    • Martin, S.J.1    Reutelingsperger, C.P.2    McGahon, A.J.3    Rader, J.A.4    Vanschie, R.C.5    Laface, D.M.6    Green, D.R.7
  • 13
    • 0033002858 scopus 로고    scopus 로고
    • Exposure of phosphatidylserine is a general feature in the phagocytosis of apoptotic lymphocytes by macrophages
    • Krahling S., Callahan M.K., Williamson P., Schlegel R.A. Exposure of phosphatidylserine is a general feature in the phagocytosis of apoptotic lymphocytes by macrophages. Cell Death Differ. 6:1999;183-189.
    • (1999) Cell Death Differ. , vol.6 , pp. 183-189
    • Krahling, S.1    Callahan, M.K.2    Williamson, P.3    Schlegel, R.A.4
  • 15
    • 0030697996 scopus 로고    scopus 로고
    • Appearance of phosphatidylserine on apoptotic cells requires calcium-mediated nonspecific flip-flop and is enhanced by loss of the aminophospholipid translocase
    • Bratton D.L., Fadok V.A., Richter D.A., Kailey J.M., Guthrie L.A., Henson P.M. Appearance of phosphatidylserine on apoptotic cells requires calcium-mediated nonspecific flip-flop and is enhanced by loss of the aminophospholipid translocase. J. Biol. Chem. 272:1997;26159-26165.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26159-26165
    • Bratton, D.L.1    Fadok, V.A.2    Richter, D.A.3    Kailey, J.M.4    Guthrie, L.A.5    Henson, P.M.6
  • 16
    • 0030590899 scopus 로고    scopus 로고
    • Involvement of extracellular calcium in phosphatidylserine exposure during apoptosis
    • Hampton M.B., Vanags D.M., Porn-Ares M.I., Orrenius S. Involvement of extracellular calcium in phosphatidylserine exposure during apoptosis. FEBS Lett. 399:1996;277-282.
    • (1996) FEBS Lett. , vol.399 , pp. 277-282
    • Hampton, M.B.1    Vanags, D.M.2    Porn-Ares, M.I.3    Orrenius, S.4
  • 18
    • 0032549693 scopus 로고    scopus 로고
    • Level of expression of phospholipid scramblase regulates induced movement of phosphatidylserine to the cell surface
    • Zhao J., Zhou Q., Wiedmer T., Sims P.J. Level of expression of phospholipid scramblase regulates induced movement of phosphatidylserine to the cell surface. J. Biol. Chem. 273:1998;6603-6606.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6603-6606
    • Zhao, J.1    Zhou, Q.2    Wiedmer, T.3    Sims, P.J.4
  • 19
    • 10544238107 scopus 로고    scopus 로고
    • Protease involvement in fodrin cleavage and phosphatidylserine exposure in apoptosis
    • Vanags D.M., Porn-Ares M.I., Coppola S., Burgess D.H., Orrenius S. Protease involvement in fodrin cleavage and phosphatidylserine exposure in apoptosis. J. Biol. Chem. 271:1996;31075-31085.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31075-31085
    • Vanags, D.M.1    Porn-Ares, M.I.2    Coppola, S.3    Burgess, D.H.4    Orrenius, S.5
  • 21
    • 0031711701 scopus 로고    scopus 로고
    • Transmembrane phospholipid distribution in blood cells: Control mechanisms and pathophysiological significance
    • Bevers E.M., Comfurius P., Dekkers D.W., Harmsma M., Zwaal R.F. Transmembrane phospholipid distribution in blood cells: control mechanisms and pathophysiological significance. Biol. Chem. 379:1998;973-986.
    • (1998) Biol. Chem. , vol.379 , pp. 973-986
    • Bevers, E.M.1    Comfurius, P.2    Dekkers, D.W.3    Harmsma, M.4    Zwaal, R.F.5
  • 22
    • 0029802815 scopus 로고    scopus 로고
    • Phosphatidylserine externalization during CD95-induced apoptosis of cells and cytoplasts requires ICE/CED-3 protease activity
    • Martin S.J., Finucane D.M., Amarante-Mendes G.P., O'Brien G.A., Green D.R. Phosphatidylserine externalization during CD95-induced apoptosis of cells and cytoplasts requires ICE/CED-3 protease activity. J. Biol. Chem. 271:1996;28753-28756.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28753-28756
    • Martin, S.J.1    Finucane, D.M.2    Amarante-Mendes, G.P.3    O'Brien, G.A.4    Green, D.R.5
  • 23
    • 0030942175 scopus 로고    scopus 로고
    • Phosphatidylserine externalization is a downstream event of interleukin-1β-converting enzyme family protease activation during apoptosis
    • Naito M., Nagashima K., Mashima T., Tsuruo T. Phosphatidylserine externalization is a downstream event of interleukin-1β-converting enzyme family protease activation during apoptosis. Blood. 89:1997;2060-2066.
    • (1997) Blood , vol.89 , pp. 2060-2066
    • Naito, M.1    Nagashima, K.2    Mashima, T.3    Tsuruo, T.4
  • 24
    • 0344631682 scopus 로고    scopus 로고
    • A caspase-independent pathway of MHC class II antigen-mediated apoptosis of human B lymphocytes
    • Drenou B., Blancheteau V., Burgess D.H., Fauchet R., Charron D.J., Mooney N.A. A caspase-independent pathway of MHC class II antigen-mediated apoptosis of human B lymphocytes. J. Immunol. 163:1999;4115-4124.
    • (1999) J. Immunol. , vol.163 , pp. 4115-4124
    • Drenou, B.1    Blancheteau, V.2    Burgess, D.H.3    Fauchet, R.4    Charron, D.J.5    Mooney, N.A.6
  • 26
    • 0034104294 scopus 로고    scopus 로고
    • Constitutive death of platelets leading to scavenger receptor-mediated phagocytosis. A caspase-independent cell clearance program
    • Brown S.B., Clarke M.C., Magowan L., Sanderson H., Savill J. Constitutive death of platelets leading to scavenger receptor-mediated phagocytosis. A caspase-independent cell clearance program. J. Biol. Chem. 275:2000;5987-5996.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5987-5996
    • Brown, S.B.1    Clarke, M.C.2    Magowan, L.3    Sanderson, H.4    Savill, J.5
  • 27
    • 0026337977 scopus 로고
    • A Chinese hamster cDNA encoding a protein essential for phosphatidylserine synthase I activity
    • Kuge O., Nishijima M., Akamatsu Y. A Chinese hamster cDNA encoding a protein essential for phosphatidylserine synthase I activity. J. Biol. Chem. 266:1991;24184-24189.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24184-24189
    • Kuge, O.1    Nishijima, M.2    Akamatsu, Y.3
  • 28
    • 0030814763 scopus 로고    scopus 로고
    • Cloning of a Chinese hamster ovary (CHO) cDNA encoding phosphatidylserine synthase (PSS) II, overexpression of which suppresses the phosphatidylserine biosynthetic defect of a PSS I-lacking mutant of CHO-K1 cells
    • Kuge O., Saito K., Nishijima M. Cloning of a Chinese hamster ovary (CHO) cDNA encoding phosphatidylserine synthase (PSS) II, overexpression of which suppresses the phosphatidylserine biosynthetic defect of a PSS I-lacking mutant of CHO-K1 cells. J. Biol. Chem. 272:1997;19133-19139.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19133-19139
    • Kuge, O.1    Saito, K.2    Nishijima, M.3
  • 29
    • 0032479436 scopus 로고    scopus 로고
    • Genetic evidence that phosphatidylserine synthase II catalyzes the conversion of phosphatidylethanolamine to phosphatidylserine in Chinese hamster ovary cells
    • Saito K., Nishijima M., Kuge O. Genetic evidence that phosphatidylserine synthase II catalyzes the conversion of phosphatidylethanolamine to phosphatidylserine in Chinese hamster ovary cells. J. Biol. Chem. 273:1998;17199-17205.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17199-17205
    • Saito, K.1    Nishijima, M.2    Kuge, O.3
  • 30
    • 0031553017 scopus 로고    scopus 로고
    • Phosphatidylserine synthase I and II of mammalian cells
    • Kuge O., Nishijima M. Phosphatidylserine synthase I and II of mammalian cells. Biochim. Biophys. Acta. 1348:1997;151-156.
    • (1997) Biochim. Biophys. Acta , vol.1348 , pp. 151-156
    • Kuge, O.1    Nishijima, M.2
  • 31
    • 0029055754 scopus 로고
    • Evidence that phosphatidylserine is imported into mitochondria via a mitochondria-associated membrane and that the majority of mitochondrial phosphatidylethanolamine is derived from decarboxylation of phosphatidylserine
    • Shiao Y.J., Lupo G., Vance J.E. Evidence that phosphatidylserine is imported into mitochondria via a mitochondria-associated membrane and that the majority of mitochondrial phosphatidylethanolamine is derived from decarboxylation of phosphatidylserine. J. Biol. Chem. 270:1995;11190-11198.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11190-11198
    • Shiao, Y.J.1    Lupo, G.2    Vance, J.E.3
  • 32
    • 0030059122 scopus 로고    scopus 로고
    • Intracellular trafficking of phospholipids: Import of phosphatidylserine into mitochondria
    • Vance J.E., Shiao Y.J. Intracellular trafficking of phospholipids: import of phosphatidylserine into mitochondria. Anticancer Res. 16:1996;1333-1339.
    • (1996) Anticancer Res. , vol.16 , pp. 1333-1339
    • Vance, J.E.1    Shiao, Y.J.2
  • 33
    • 0032516053 scopus 로고    scopus 로고
    • Control of phosphatidylserine biosynthesis through phosphatidylserine-mediated inhibition of phosphatidylserine synthase I in Chinese hamster ovary cells
    • Kuge O., Hasegawa K., Saito K., Nishijima M. Control of phosphatidylserine biosynthesis through phosphatidylserine-mediated inhibition of phosphatidylserine synthase I in Chinese hamster ovary cells. Proc. Natl. Acad. Sci. USA. 95:1998;4199-4203.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4199-4203
    • Kuge, O.1    Hasegawa, K.2    Saito, K.3    Nishijima, M.4
  • 34
    • 0033588336 scopus 로고    scopus 로고
    • Control of phosphatidylserine synthase II activity in Chinese hamster ovary cells
    • Kuge O., Saito K., Nishijima M. Control of phosphatidylserine synthase II activity in Chinese hamster ovary cells. J. Biol. Chem. 274:1999;23844-23849.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23844-23849
    • Kuge, O.1    Saito, K.2    Nishijima, M.3
  • 35
    • 0032541025 scopus 로고    scopus 로고
    • CD95 (Fas/APO-1) induces an increased phosphatidylserine synthesis that precedes its externalization during programmed cell death
    • Aussel C., Pelassy C., Breittmayer J.P. CD95 (Fas/APO-1) induces an increased phosphatidylserine synthesis that precedes its externalization during programmed cell death. FEBS Lett. 431:1998;195-199.
    • (1998) FEBS Lett. , vol.431 , pp. 195-199
    • Aussel, C.1    Pelassy, C.2    Breittmayer, J.P.3
  • 36
    • 0033538462 scopus 로고    scopus 로고
    • Inhibition of phosphatidylcholine biosynthesis following induction of apoptosis in HL-60 cells
    • Anthony M.L., Zhao M., Brindle K.M. Inhibition of phosphatidylcholine biosynthesis following induction of apoptosis in HL-60 cells. J. Biol. Chem. 274:1999;19686-19692.
    • (1999) J. Biol. Chem. , vol.274 , pp. 19686-19692
    • Anthony, M.L.1    Zhao, M.2    Brindle, K.M.3
  • 37
    • 0013881712 scopus 로고
    • Synchronization of mammalian cells in vitro by inhibition of the DNA synthesis. I. Optimal conditions
    • Galavazi G., Schenk H., Bootsma D. Synchronization of mammalian cells in vitro by inhibition of the DNA synthesis. I. Optimal conditions. Exp. Cell Res. 41:1966;428-437.
    • (1966) Exp. Cell Res. , vol.41 , pp. 428-437
    • Galavazi, G.1    Schenk, H.2    Bootsma, D.3
  • 38
    • 70449158340 scopus 로고
    • A simple method for the isolation and purification of total lipids from animal tissues
    • Folch J., Lees M., Sloane-Stanley G.H. A simple method for the isolation and purification of total lipids from animal tissues. J. Biol. Chem. 226:1957;497-509.
    • (1957) J. Biol. Chem. , vol.226 , pp. 497-509
    • Folch, J.1    Lees, M.2    Sloane-Stanley, G.H.3
  • 39
    • 0025337627 scopus 로고
    • Incorporation of polyunsaturated fatty acids into plasmalogens, compared to other phospholipids of cultured glioma cells, is more dependent on chain length than on selectivity between (n-3) and (n-6) families
    • Thomas S.E., Byers D.M., Palmer F.B.S.C., Spence M.W., Cook H.W. Incorporation of polyunsaturated fatty acids into plasmalogens, compared to other phospholipids of cultured glioma cells, is more dependent on chain length than on selectivity between (n-3) and (n-6) families. Biochim. Biophys. Acta Lipids Lipid Metab. 1044:1990;349-356.
    • (1990) Biochim. Biophys. Acta Lipids Lipid Metab. , vol.1044 , pp. 349-356
    • Thomas, S.E.1    Byers, D.M.2    Palmer, F.B.S.C.3    Spence, M.W.4    Cook, H.W.5
  • 41
    • 0030826929 scopus 로고    scopus 로고
    • Topoisomerase I inhibitors: Review and update
    • Rothenberg M.L. Topoisomerase I inhibitors: review and update. Ann. Oncol. 8:1997;837-855.
    • (1997) Ann. Oncol. , vol.8 , pp. 837-855
    • Rothenberg, M.L.1
  • 42
    • 0030772293 scopus 로고    scopus 로고
    • Camptothecin causes cell cycle perturbations within T-lymphoblastoid cells followed by dose dependent induction of apoptosis
    • Johnson N., Ng T.T., Parkin J.M. Camptothecin causes cell cycle perturbations within T-lymphoblastoid cells followed by dose dependent induction of apoptosis. Leuk. Res. 21:1997;961-972.
    • (1997) Leuk. Res. , vol.21 , pp. 961-972
    • Johnson, N.1    Ng, T.T.2    Parkin, J.M.3
  • 43
    • 0027261147 scopus 로고
    • The cell cycle related differences in susceptibility of HL-60 cells to apoptosis induced by various antitumor agents
    • Gorczyca W., Gong J., Ardelt B., Traganos F., Darzynkiewicz Z. The cell cycle related differences in susceptibility of HL-60 cells to apoptosis induced by various antitumor agents. Cancer Res. 53:1993;3186-3192.
    • (1993) Cancer Res. , vol.53 , pp. 3186-3192
    • Gorczyca, W.1    Gong, J.2    Ardelt, B.3    Traganos, F.4    Darzynkiewicz, Z.5
  • 44
    • 0028990125 scopus 로고
    • Yama/CPP32β, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase
    • Tewari M., Quan L.T., O'Rourke K., Desnoyers S., Zeng Z., Beidler D.R., Poirier G.G., Salvesen G.S., Dixit V.M. Yama/CPP32β, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell. 81:1995;801-809.
    • (1995) Cell , vol.81 , pp. 801-809
    • Tewari, M.1    Quan, L.T.2    O'Rourke, K.3    Desnoyers, S.4    Zeng, Z.5    Beidler, D.R.6    Poirier, G.G.7    Salvesen, G.S.8    Dixit, V.M.9
  • 47
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors: Signaling and modulation
    • Ashkenazi A., Dixit V.M. Death receptors: signaling and modulation. Science. 281:1998;1305-1308.
    • (1998) Science , vol.281 , pp. 1305-1308
    • Ashkenazi, A.1    Dixit, V.M.2
  • 48
    • 0025098063 scopus 로고
    • Drug-induced alterations of tumor necrosis factor-mediated cytotoxicity: Discrimination of early versus late stage action
    • Kull F.C. Jr., Besterman J.M. Drug-induced alterations of tumor necrosis factor-mediated cytotoxicity: discrimination of early versus late stage action. J. Cell Biochem. 42:1990;1-12.
    • (1990) J. Cell Biochem. , vol.42 , pp. 1-12
    • Kull, F.C.1    Besterman, J.M.2
  • 49
    • 0029965928 scopus 로고    scopus 로고
    • Tumor cell resistance to apoptosis due to a defect in the activation of sphingomyelinase and the 24 kDa apoptotic protease (AP24)
    • Wright S.C., Zheng H., Zhong J. Tumor cell resistance to apoptosis due to a defect in the activation of sphingomyelinase and the 24 kDa apoptotic protease (AP24). FASEB J. 10:1996;325-332.
    • (1996) FASEB J. , vol.10 , pp. 325-332
    • Wright, S.C.1    Zheng, H.2    Zhong, J.3
  • 50
    • 0015209679 scopus 로고
    • Enzymic characterization and lipid composition of rat liver subcellular membranes
    • Colbeau A., Nachbaur J., Vignais P.M. Enzymic characterization and lipid composition of rat liver subcellular membranes. Biochim. Biophys. Acta. 249:1971;462-492.
    • (1971) Biochim. Biophys. Acta , vol.249 , pp. 462-492
    • Colbeau, A.1    Nachbaur, J.2    Vignais, P.M.3
  • 51
    • 0033579422 scopus 로고    scopus 로고
    • Resistance to the cytotoxic effects of tumor necrosis factor α can be overcome by inhibition of a FADD/caspase-dependent signaling pathway
    • Khwaja A., Tatton L. Resistance to the cytotoxic effects of tumor necrosis factor α can be overcome by inhibition of a FADD/caspase-dependent signaling pathway. J. Biol. Chem. 274:1999;36817-36823.
    • (1999) J. Biol. Chem. , vol.274 , pp. 36817-36823
    • Khwaja, A.1    Tatton, L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.