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Volumn 208, Issue 5, 2011, Pages 909-921

Trypanosoma cruzi subverts the sphingomyelinase-mediated plasma membrane repair pathway for cell invasion

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; CERAMIDE; SPHINGOMYELIN PHOSPHODIESTERASE; TOXIN;

EID: 79956075012     PISSN: 00221007     EISSN: 15409538     Source Type: Journal    
DOI: 10.1084/jem.20102518     Document Type: Article
Times cited : (112)

References (53)
  • 1
    • 8644238313 scopus 로고    scopus 로고
    • Lysosomal fusion is essential for the retention of Trypanosoma cruzi inside host cells
    • Andrade, L.O., and N.W. Andrews. 2004. Lysosomal fusion is essential for the retention of Trypanosoma cruzi inside host cells. J. Exp. Med. 200:1135-1143.
    • (2004) J. Exp. Med. , vol.200 , pp. 1135-1143
    • Andrade, L.O.1    Andrews, N.W.2
  • 2
    • 0024583847 scopus 로고
    • Secretion by Trypanosoma cruzi of a hemolysin active at low pH
    • Andrews, N.W., and M.B. Whitlow. 1989. Secretion by Trypanosoma cruzi of a hemolysin active at low pH. Mol. Biochem. Parasitol. 33:249-256.
    • (1989) Mol. Biochem. Parasitol. , vol.33 , pp. 249-256
    • Andrews, N.W.1    Whitlow, M.B.2
  • 3
    • 0023502334 scopus 로고
    • Stagespecific surface antigens expressed during the morphogenesis of vertebrate forms of Trypanosoma cruzi
    • Andrews, N.W., K.S. Hong, E.S. Robbins, and V. Nussenzweig. 1987. Stagespecific surface antigens expressed during the morphogenesis of vertebrate forms of Trypanosoma cruzi. Exp. Parasitol. 64:474-484.
    • (1987) Exp. Parasitol. , vol.64 , pp. 474-484
    • Andrews, N.W.1    Hong, K.S.2    Robbins, E.S.3    Nussenzweig, V.4
  • 4
    • 0025277577 scopus 로고
    • cruzisecreted protein immunologically related to the complement component C9: evidence for membrane pore-forming activity at low pH
    • Andrews, N.W., C.K. Abrams, S.L. Slatin, and G. Griffiths. 1990. A T. cruzisecreted protein immunologically related to the complement component C9: evidence for membrane pore-forming activity at low pH. Cell. 61:1277-1287.
    • (1990) Cell , vol.61 , pp. 1277-1287
    • Andrews, N.W.1    Abrams, C.K.2    Slatin, S.L.3    Griffiths, G.4
  • 6
    • 0029609143 scopus 로고
    • Calcium-regulated exocytosis is required for cell membrane resealing
    • Bi, G.Q., J.M. Alderton, and R.A. Steinhardt. 1995. Calcium-regulated exocytosis is required for cell membrane resealing. J. Cell Biol. 131:1747-1758.
    • (1995) J. Cell Biol. , vol.131 , pp. 1747-1758
    • Bi, G.Q.1    Alderton, J.M.2    Steinhardt, R.A.3
  • 7
    • 0028900481 scopus 로고
    • A 120-kDa alkaline peptidase from Trypanosoma cruzi is involved in the generation of a novel Ca(2+)-signaling factor for mammalian cells
    • Burleigh, B.A., and N.W. Andrews. 1995. A 120-kDa alkaline peptidase from Trypanosoma cruzi is involved in the generation of a novel Ca(2+)-signaling factor for mammalian cells. J. Biol. Chem. 270:5172-5180.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5172-5180
    • Burleigh, B.A.1    Andrews, N.W.2
  • 8
    • 0032130568 scopus 로고    scopus 로고
    • Signaling and host cell invasion by Trypanosoma cruzi
    • Burleigh, B.A., and N.W. Andrews. 1998. Signaling and host cell invasion by Trypanosoma cruzi. Curr. Opin. Microbiol. 1:461-465.
    • (1998) Curr. Opin. Microbiol. , vol.1 , pp. 461-465
    • Burleigh, B.A.1    Andrews, N.W.2
  • 9
    • 0036855862 scopus 로고    scopus 로고
    • Cell signalling and Trypanosoma cruzi invasion
    • Burleigh, B.A., and A.M. Woolsey. 2002. Cell signalling and Trypanosoma cruzi invasion. Cell. Microbiol. 4:701-711.
    • (2002) Cell. Microbiol. , vol.4 , pp. 701-711
    • Burleigh, B.A.1    Woolsey, A.M.2
  • 13
    • 33845742173 scopus 로고    scopus 로고
    • Bromoenol lactone, an inhibitor of Group V1A calcium-independent phospholipase A2 inhibits antigen-stimulated mast cell exocytosis without blocking Ca2+ influx
    • Fensome-Green, A., N. Stannard, M. Li, S. Bolsover, and S. Cockcroft. 2007. Bromoenol lactone, an inhibitor of Group V1A calcium-independent phospholipase A2 inhibits antigen-stimulated mast cell exocytosis without blocking Ca2+ influx. Cell Calcium. 41:145-153.
    • (2007) Cell Calcium , vol.41 , pp. 145-153
    • Fensome-Green, A.1    Stannard, N.2    Li, M.3    Bolsover, S.4    Cockcroft, S.5
  • 16
    • 0027104231 scopus 로고
    • High resolution scanning electron microscopy of the nuclear envelope: demonstration of a new, regular, fibrous lattice attached to the baskets of the nucleoplasmic face of the nuclear pores
    • Goldberg, M.W., and T.D. Allen. 1992. High resolution scanning electron microscopy of the nuclear envelope: demonstration of a new, regular, fibrous lattice attached to the baskets of the nucleoplasmic face of the nuclear pores. J. Cell Biol. 119:1429-1440.
    • (1992) J. Cell Biol. , vol.119 , pp. 1429-1440
    • Goldberg, M.W.1    Allen, T.D.2
  • 17
    • 34250742501 scopus 로고    scopus 로고
    • Biological aspects of ceramide-enriched membrane domains
    • Grassmé, H., J. Riethmüller, and E. Gulbins. 2007. Biological aspects of ceramide-enriched membrane domains. Prog. Lipid Res. 46:161-170.
    • (2007) Prog. Lipid Res. , vol.46 , pp. 161-170
    • Grassmé, H.1    Riethmüller, J.2    Gulbins, E.3
  • 18
    • 0242574357 scopus 로고    scopus 로고
    • Raft ceramide in molecular medicine
    • Gulbins, E., and R. Kolesnick. 2003. Raft ceramide in molecular medicine. Oncogene. 22:7070-7077.
    • (2003) Oncogene , vol.22 , pp. 7070-7077
    • Gulbins, E.1    Kolesnick, R.2
  • 20
    • 0038058958 scopus 로고    scopus 로고
    • Hill, K.L. 2003. Biology and mechanism of trypanosome cell motility. Eukaryot. Cell. 2:200-208.
    • (2003) Eukaryot. Cell. , vol.2 , pp. 200-208
    • Hill, K.L.1
  • 21
    • 0034087155 scopus 로고    scopus 로고
    • Vectorial budding of vesicles by asymmetrical enzymatic formation of ceramide in giant liposomes
    • Holopainen, J.M., M.I. Angelova, and P.K. Kinnunen. 2000. Vectorial budding of vesicles by asymmetrical enzymatic formation of ceramide in giant liposomes. Biophys. J. 78:830-838.
    • (2000) Biophys. J. , vol.78 , pp. 830-838
    • Holopainen, J.M.1    Angelova, M.I.2    Kinnunen, P.K.3
  • 22
    • 0028468309 scopus 로고
    • The tricyclic antidepressant desipramine causes proteolytic degradation of lysosomal sphingomyelinase in human fibroblasts
    • Hurwitz, R., K. Ferlinz, and K. Sandhoff. 1994. The tricyclic antidepressant desipramine causes proteolytic degradation of lysosomal sphingomyelinase in human fibroblasts. Biol. Chem. Hoppe Seyler. 375:447-450.
    • (1994) Biol. Chem. Hoppe Seyler. , vol.375 , pp. 447-450
    • Hurwitz, R.1    Ferlinz, K.2    Sandhoff, K.3
  • 23
    • 0015895273 scopus 로고
    • Trypanosoma cruzi: interaction with vertebrate cells in vitro. 2. Quantitative analysis of the penetration phase
    • Hyde, T.P., and J.A. Dvorak. 1973. Trypanosoma cruzi: interaction with vertebrate cells in vitro. 2. Quantitative analysis of the penetration phase. Exp. Parasitol. 34:284-294.
    • (1973) Exp. Parasitol. , vol.34 , pp. 284-294
    • Hyde, T.P.1    Dvorak, J.A.2
  • 25
    • 0037175388 scopus 로고    scopus 로고
    • Membrane proximal lysosomes are the major vesicles responsible for calcium-dependent exocytosis in nonsecretory cells
    • Jaiswal, J.K., N.W. Andrews, and S.M. Simon. 2002. Membrane proximal lysosomes are the major vesicles responsible for calcium-dependent exocytosis in nonsecretory cells. J. Cell Biol. 159:625-635.
    • (2002) J. Cell Biol. , vol.159 , pp. 625-635
    • Jaiswal, J.K.1    Andrews, N.W.2    Simon, S.M.3
  • 26
    • 12144281320 scopus 로고    scopus 로고
    • Functional characterization of the postulated intramolecular sphingolipid activator protein domain of human acid sphingomyelinase
    • Kölzer, M., K. Ferlinz, O. Bartelsen, S.L. Hoops, F. Lang, and K. Sandhoff. 2004. Functional characterization of the postulated intramolecular sphingolipid activator protein domain of human acid sphingomyelinase. Biol. Chem. 385:1193-1195.
    • (2004) Biol. Chem. , vol.385 , pp. 1193-1195
    • Kölzer, M.1    Ferlinz, K.2    Bartelsen, O.3    Hoops, S.L.4    Lang, F.5    Sandhoff, K.6
  • 27
    • 0026016879 scopus 로고
    • Intracellular transport and metabolism of sphingomyelin
    • Koval, M., and R.E. Pagano. 1991. Intracellular transport and metabolism of sphingomyelin. Biochim. Biophys. Acta. 1082:113-125.
    • (1991) Biochim. Biophys. Acta. , vol.1082 , pp. 113-125
    • Koval, M.1    Pagano, R.E.2
  • 28
    • 0025098535 scopus 로고
    • The exit of Trypanosoma cruzi from the phagosome is inhibited by raising the pH of acidic compartments
    • Ley, V., E.S. Robbins, V. Nussenzweig, and N.W. Andrews. 1990. The exit of Trypanosoma cruzi from the phagosome is inhibited by raising the pH of acidic compartments. J. Exp. Med. 171:401-413.
    • (1990) J. Exp. Med. , vol.171 , pp. 401-413
    • Ley, V.1    Robbins, E.S.2    Nussenzweig, V.3    Andrews, N.W.4
  • 29
    • 0344824647 scopus 로고    scopus 로고
    • Plasma membrane disruption: repair, prevention, adaptation
    • McNeil, P.L., and R.A. Steinhardt. 2003. Plasma membrane disruption: repair, prevention, adaptation. Annu. Rev. Cell Dev. Biol. 19:697-731.
    • (2003) Annu. Rev. Cell Dev. Biol. , vol.19 , pp. 697-731
    • McNeil, P.L.1    Steinhardt, R.A.2
  • 30
    • 0034130361 scopus 로고    scopus 로고
    • Patching plasma membrane disruptions with cytoplasmic membrane
    • McNeil, P.L., S.S. Vogel, K. Miyake, and M. Terasaki. 2000. Patching plasma membrane disruptions with cytoplasmic membrane. J. Cell Sci. 113:1891-1902.
    • (2000) J. Cell Sci. , vol.113 , pp. 1891-1902
    • McNeil, P.L.1    Vogel, S.S.2    Miyake, K.3    Terasaki, M.4
  • 31
    • 0029585288 scopus 로고
    • Vesicle accumulation and exocytosis at sites of plasma membrane disruption
    • Miyake, K., and P.L. McNeil. 1995. Vesicle accumulation and exocytosis at sites of plasma membrane disruption. J. Cell Biol. 131:1737-1745.
    • (1995) J. Cell Biol. , vol.131 , pp. 1737-1745
    • Miyake, K.1    McNeil, P.L.2
  • 32
    • 0027941410 scopus 로고
    • Cytosolic-free calcium elevation in Trypanosoma cruzi is required for cell invasion
    • Moreno, S.N., J. Silva, A.E. Vercesi, and R. Docampo. 1994. Cytosolic-free calcium elevation in Trypanosoma cruzi is required for cell invasion. J. Exp. Med. 180:1535-1540.
    • (1994) J. Exp. Med. , vol.180 , pp. 1535-1540
    • Moreno, S.N.1    Silva, J.2    Vercesi, A.E.3    Docampo, R.4
  • 33
    • 0021809190 scopus 로고
    • Comparative biology of intracellular parasitism
    • Moulder, J.W. 1985. Comparative biology of intracellular parasitism. Microbiol. Rev. 49:298-337.
    • (1985) Microbiol. Rev. , vol.49 , pp. 298-337
    • Moulder, J.W.1
  • 34
    • 0017075718 scopus 로고
    • Trypanosoma cruzi: mechanism of entry and intracellular fate in mammalian cells
    • Nogueira, N., and Z. Cohn. 1976. Trypanosoma cruzi: mechanism of entry and intracellular fate in mammalian cells. J. Exp. Med. 143:1402-1420.
    • (1976) J. Exp. Med. , vol.143 , pp. 1402-1420
    • Nogueira, N.1    Cohn, Z.2
  • 35
    • 0035958557 scopus 로고    scopus 로고
    • Plasma membrane repair is mediated by Ca(2+)-regulated exocytosis of lysosomes
    • Reddy, A., E.V. Caler, and N.W. Andrews. 2001. Plasma membrane repair is mediated by Ca(2+)-regulated exocytosis of lysosomes. Cell. 106:157-169.
    • (2001) Cell , vol.106 , pp. 157-169
    • Reddy, A.1    Caler, E.V.2    Andrews, N.W.3
  • 38
    • 0026577038 scopus 로고
    • HeLa cells extend and internalize pseudopodia during active invasion by Trypanosoma cruzi trypomastigotes
    • Schenkman, S., and R.A. Mortara. 1992. HeLa cells extend and internalize pseudopodia during active invasion by Trypanosoma cruzi trypomastigotes. J. Cell Sci. 101:895-905.
    • (1992) J. Cell Sci. , vol.101 , pp. 895-905
    • Schenkman, S.1    Mortara, R.A.2
  • 39
    • 0025968123 scopus 로고
    • Attachment of Trypanosoma cruzi to mammalian cells requires parasite energy, and invasion can be independent of the target cell cytoskeleton
    • Schenkman, S., E.S. Robbins, and V. Nussenzweig. 1991. Attachment of Trypanosoma cruzi to mammalian cells requires parasite energy, and invasion can be independent of the target cell cytoskeleton. Infect. Immun. 59:645-654.
    • (1991) Infect. Immun. , vol.59 , pp. 645-654
    • Schenkman, S.1    Robbins, E.S.2    Nussenzweig, V.3
  • 40
    • 0032579258 scopus 로고    scopus 로고
    • Secretory sphingomyelinase, a product of the acid sphingomyelinase gene, can hydrolyze atherogenic lipoproteins at neutral Ph. Implications for atherosclerotic lesion development
    • Schissel, S.L., X. Jiang, J. Tweedie-Hardman, T. Jeong, E.H. Camejo, J. Najib, J.H. Rapp, K.J. Williams, and I. Tabas. 1998. Secretory sphingomyelinase, a product of the acid sphingomyelinase gene, can hydrolyze atherogenic lipoproteins at neutral pH. Implications for atherosclerotic lesion development. J. Biol. Chem. 273:2738-2746.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2738-2746
    • Schissel, S.L.1    Jiang, X.2    Tweedie-Hardman, J.3    Jeong, T.4    Camejo, E.H.5    Najib, J.6    Rapp, J.H.7    Williams, K.J.8    Tabas, I.9
  • 41
    • 0028014529 scopus 로고
    • Cell membrane resealing by a vesicular mechanism similar to neurotransmitter release
    • Steinhardt, R.A., G. Bi, and J.M. Alderton. 1994. Cell membrane resealing by a vesicular mechanism similar to neurotransmitter release. Science. 263:390-393.
    • (1994) Science , vol.263 , pp. 390-393
    • Steinhardt, R.A.1    Bi, G.2    Alderton, J.M.3
  • 43
    • 0027049531 scopus 로고
    • Lysosome recruitment and fusion are early events required for trypanosome invasion of mammalian cells
    • Tardieux, I., P. Webster, J. Ravesloot, W. Boron, J.A. Lunn, J.E. Heuser, and N.W. Andrews. 1992. Lysosome recruitment and fusion are early events required for trypanosome invasion of mammalian cells. Cell. 71:1117-1130.
    • (1992) Cell , vol.71 , pp. 1117-1130
    • Tardieux, I.1    Webster, P.2    Ravesloot, J.3    Boron, W.4    Lunn, J.A.5    Heuser, J.E.6    Andrews, N.W.7
  • 45
    • 0033067513 scopus 로고    scopus 로고
    • The mechanism of facilitated cell membrane resealing
    • Togo, T., J.M. Alderton, G.Q. Bi, and R.A. Steinhardt. 1999. The mechanism of facilitated cell membrane resealing. J. Cell Sci. 112:719-731.
    • (1999) J. Cell Sci. , vol.112 , pp. 719-731
    • Togo, T.1    Alderton, J.M.2    Bi, G.Q.3    Steinhardt, R.A.4
  • 47
    • 25444452398 scopus 로고    scopus 로고
    • Cholesterol-dependent cytolysins, a family of versatile pore-forming toxins
    • Tweten, R.K. 2005. Cholesterol-dependent cytolysins, a family of versatile pore-forming toxins. Infect. Immun. 73:6199-6209.
    • (2005) Infect. Immun. , vol.73 , pp. 6199-6209
    • Tweten, R.K.1
  • 51
    • 46249124859 scopus 로고    scopus 로고
    • Trypanosoma cruzi: parasite and host cell signaling during the invasion process
    • Yoshida, N., and M. Cortez. 2008. Trypanosoma cruzi: parasite and host cell signaling during the invasion process. Subcell. Biochem. 47:82-91.
    • (2008) Subcell. Biochem. , vol.47 , pp. 82-91
    • Yoshida, N.1    Cortez, M.2
  • 52
    • 34249657837 scopus 로고    scopus 로고
    • Activation of acid sphingomyelinase by protein kinase Cdelta-mediated phosphorylation
    • Zeidan, Y.H., and Y.A. Hannun. 2007. Activation of acid sphingomyelinase by protein kinase Cdelta-mediated phosphorylation. J. Biol. Chem. 282:11549-11561.
    • (2007) J. Biol. Chem. , vol.282 , pp. 11549-11561
    • Zeidan, Y.H.1    Hannun, Y.A.2


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