메뉴 건너뛰기




Volumn 362, Issue 3, 2007, Pages 651-657

9-O-Acetylated GD3 triggers programmed cell death in mature erythrocytes

Author keywords

9 O Acetylated GD3; Apoptosis; Caspase; Erythropoiesis; Glycophorin A; Maturation; Mature erythrocytes; Membrane alteration; Phosphatidyl serine

Indexed keywords

CASPASE 3; CYSTEINE PROTEINASE; ESTER; GANGLIOSIDE GD3; PHOSPHATIDYLSERINE;

EID: 34548499107     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.08.048     Document Type: Article
Times cited : (23)

References (29)
  • 2
    • 34548473244 scopus 로고
    • Developmental changes in ganglioside composition and synthesis in embryonic rat brain
    • Yu R.K., Macala L.J., Taki T., Weinfield H.M., and Yu F.S. Developmental changes in ganglioside composition and synthesis in embryonic rat brain. J. Neurochem. 501 (1988) 825-829
    • (1988) J. Neurochem. , vol.501 , pp. 825-829
    • Yu, R.K.1    Macala, L.J.2    Taki, T.3    Weinfield, H.M.4    Yu, F.S.5
  • 3
    • 0021262517 scopus 로고
    • The D1.1 antigen: a cell surface marker for germinal cells of the central nervous system
    • Levine J.M., Beasley L., and Stallcup W. The D1.1 antigen: a cell surface marker for germinal cells of the central nervous system. J. Neurosci. 4 (1984) 820-831
    • (1984) J. Neurosci. , vol.4 , pp. 820-831
    • Levine, J.M.1    Beasley, L.2    Stallcup, W.3
  • 4
    • 0021254732 scopus 로고
    • A monoclonal antibody recognizes an O-acylated sialic acid in a human melanoma-associated ganglioside
    • Cheresh D.A., Varki A.P., Varki N.M., Stallcup W.B., Levine J., and Reisfeld R.A. A monoclonal antibody recognizes an O-acylated sialic acid in a human melanoma-associated ganglioside. J. Biol. Chem. 259 (1984) 7453-7459
    • (1984) J. Biol. Chem. , vol.259 , pp. 7453-7459
    • Cheresh, D.A.1    Varki, A.P.2    Varki, N.M.3    Stallcup, W.B.4    Levine, J.5    Reisfeld, R.A.6
  • 5
    • 0025763640 scopus 로고
    • Studies of the developing chick retina using monoclonal antibody 8A2 that recognizes a novel set of gangliosides
    • Drazba J., Pierce M., and Lemmon V. Studies of the developing chick retina using monoclonal antibody 8A2 that recognizes a novel set of gangliosides. Dev. Biol. 145 (1991) 154-163
    • (1991) Dev. Biol. , vol.145 , pp. 154-163
    • Drazba, J.1    Pierce, M.2    Lemmon, V.3
  • 7
    • 0032536876 scopus 로고    scopus 로고
    • Acidic sphingomyelinase (ASM) is necessary for fas-induced GD3 ganglioside accumulation and efficient apoptosis of lymphoid cells
    • De Maria R., Rippo M.R., Schuchman E.H., and Testi R. Acidic sphingomyelinase (ASM) is necessary for fas-induced GD3 ganglioside accumulation and efficient apoptosis of lymphoid cells. J. Exp. Med. 187 (1998) 897-902
    • (1998) J. Exp. Med. , vol.187 , pp. 897-902
    • De Maria, R.1    Rippo, M.R.2    Schuchman, E.H.3    Testi, R.4
  • 10
    • 0033565557 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore and its role in cell death
    • Crompton M. The mitochondrial permeability transition pore and its role in cell death. Biochem. J. 341 (1999) 233-249
    • (1999) Biochem. J. , vol.341 , pp. 233-249
    • Crompton, M.1
  • 11
    • 0033580926 scopus 로고    scopus 로고
    • Cytochrome c and dATP-mediated oligomerization of Apaf-1 is a prerequisite for procaspase-9 activation
    • Saleh A., Srinivasula S.M., Acharya S., Fishel R., and Alnemri E.S. Cytochrome c and dATP-mediated oligomerization of Apaf-1 is a prerequisite for procaspase-9 activation. J. Biol. Chem. 274 (1999) 17941-17945
    • (1999) J. Biol. Chem. , vol.274 , pp. 17941-17945
    • Saleh, A.1    Srinivasula, S.M.2    Acharya, S.3    Fishel, R.4    Alnemri, E.S.5
  • 12
    • 0037122008 scopus 로고    scopus 로고
    • Acetylation suppresses the proapoptotic activity of GD3 ganglioside
    • Malisan F., Franchi L., Tomassini B., et al. Acetylation suppresses the proapoptotic activity of GD3 ganglioside. J. Exp. Med. 196 (2002) 1535-1541
    • (2002) J. Exp. Med. , vol.196 , pp. 1535-1541
    • Malisan, F.1    Franchi, L.2    Tomassini, B.3
  • 13
    • 33646528465 scopus 로고    scopus 로고
    • 9-O-Acetyl GD3 protects tumor cells from apoptosis
    • Kniep B., Kniep E., Ozkucur N., et al. 9-O-Acetyl GD3 protects tumor cells from apoptosis. Int. J. Cancer 119 (2006) 67-70
    • (2006) Int. J. Cancer , vol.119 , pp. 67-70
    • Kniep, B.1    Kniep, E.2    Ozkucur, N.3
  • 14
    • 0023943252 scopus 로고
    • Senescence of red blood cells: progress and problems
    • Clark M.R. Senescence of red blood cells: progress and problems. Physiol. Rev. 68 (1988) 503-554
    • (1988) Physiol. Rev. , vol.68 , pp. 503-554
    • Clark, M.R.1
  • 15
    • 0032539931 scopus 로고    scopus 로고
    • Phosphatidylserine exposure and red cell viability in red cell aging and in hemolytic anemia
    • Boas F.E., Forman L., and Beutler E. Phosphatidylserine exposure and red cell viability in red cell aging and in hemolytic anemia. Proc. Natl. Acad. Sci. USA 95 (1998) 3077-3081
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3077-3081
    • Boas, F.E.1    Forman, L.2    Beutler, E.3
  • 17
    • 0032006450 scopus 로고    scopus 로고
    • Cellular and molecular mechanisms of senescent erythrocyte phagocytosis by macrophages
    • Bratosin D., Mazurier J., Tissier J., et al. Cellular and molecular mechanisms of senescent erythrocyte phagocytosis by macrophages. Biochimie 80 (1998) 173-195
    • (1998) Biochimie , vol.80 , pp. 173-195
    • Bratosin, D.1    Mazurier, J.2    Tissier, J.3
  • 18
    • 28244434797 scopus 로고    scopus 로고
    • Fas-, caspase 8-, and caspase 3-dependent signaling regulates the activity of the aminophospholipid translocase and phosphatidylserine externalization in human erythrocytes
    • Mandal D., Mazumder A., Das P., Kundu M., and Basu J. Fas-, caspase 8-, and caspase 3-dependent signaling regulates the activity of the aminophospholipid translocase and phosphatidylserine externalization in human erythrocytes. J. Biol. Chem. 280 (2005) 39460-39467
    • (2005) J. Biol. Chem. , vol.280 , pp. 39460-39467
    • Mandal, D.1    Mazumder, A.2    Das, P.3    Kundu, M.4    Basu, J.5
  • 19
    • 0023158748 scopus 로고
    • Flow cytometric analysis of human bone marrow: I. Normal erythroid development
    • Loken M.R., Shah V.O., Dattilio K.L., and Civin C.I. Flow cytometric analysis of human bone marrow: I. Normal erythroid development. Blood 69 (1978) 255-263
    • (1978) Blood , vol.69 , pp. 255-263
    • Loken, M.R.1    Shah, V.O.2    Dattilio, K.L.3    Civin, C.I.4
  • 20
    • 0028785347 scopus 로고
    • Kinetics of folding and membrane insertion of a b-barrel membrane protein
    • Surrey T., and Jähnig F. Kinetics of folding and membrane insertion of a b-barrel membrane protein. J. Biol. Chem. 270 (1995) 28199-28203
    • (1995) J. Biol. Chem. , vol.270 , pp. 28199-28203
    • Surrey, T.1    Jähnig, F.2
  • 21
    • 0032746015 scopus 로고    scopus 로고
    • Effect of cell ageing on Ca2+ influx into human red cells
    • Romero P.J., and Romero E.A. Effect of cell ageing on Ca2+ influx into human red cells. Cell Calcium 26 (1999) 131-137
    • (1999) Cell Calcium , vol.26 , pp. 131-137
    • Romero, P.J.1    Romero, E.A.2
  • 22
    • 0033081526 scopus 로고    scopus 로고
    • The role of calcium metabolism in human red blood cell ageing: a proposal
    • Romero P.J., and Romero E.A. The role of calcium metabolism in human red blood cell ageing: a proposal. Blood Cells Mol. Dis. 25 (1999) 9-19
    • (1999) Blood Cells Mol. Dis. , vol.25 , pp. 9-19
    • Romero, P.J.1    Romero, E.A.2
  • 23
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • Hengartner M. The biochemistry of apoptosis. Nature 407 (2000) 770-776
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.1
  • 24
    • 0034616946 scopus 로고    scopus 로고
    • Apoptotic pathways: paper wraps stone blunt scissors
    • Green D.R. Apoptotic pathways: paper wraps stone blunt scissors. Cell 102 (2000) 1-4
    • (2000) Cell , vol.102 , pp. 1-4
    • Green, D.R.1
  • 25
    • 0032885388 scopus 로고    scopus 로고
    • Mammalian caspases: structure, activation, substrates, and functions during apoptosis
    • Earnshaw W.C., Martins L.M., and Kaufmann S.H. Mammalian caspases: structure, activation, substrates, and functions during apoptosis. Annu. Rev. Biochem. 68 (1999) 383-424
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 383-424
    • Earnshaw, W.C.1    Martins, L.M.2    Kaufmann, S.H.3
  • 26
    • 0034641980 scopus 로고    scopus 로고
    • Apoptosis in development
    • Meier P., Finch A., and Evan G. Apoptosis in development. Nature 407 (2000) 796-801
    • (2000) Nature , vol.407 , pp. 796-801
    • Meier, P.1    Finch, A.2    Evan, G.3
  • 27
    • 0034284637 scopus 로고    scopus 로고
    • Mitochondria as the central control point of apoptosis
    • Desagher S., and Martinou J.C. Mitochondria as the central control point of apoptosis. Trends Cell Biol. 10 (2000) 369-377
    • (2000) Trends Cell Biol. , vol.10 , pp. 369-377
    • Desagher, S.1    Martinou, J.C.2
  • 29
    • 0035229427 scopus 로고    scopus 로고
    • The mitochondrion in apoptosis: how Pandora′s box opens
    • Zamzami N., and Kroemer G. The mitochondrion in apoptosis: how Pandora′s box opens. Nature Rev. Mol. Cell Biol. 2 (2001) 67-71
    • (2001) Nature Rev. Mol. Cell Biol. , vol.2 , pp. 67-71
    • Zamzami, N.1    Kroemer, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.