메뉴 건너뛰기




Volumn 179, Issue 6, 2007, Pages 4003-4014

A glycosylphosphatidylinositol-based treatment alleviates trypanosomiasis-associated immunopathology

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOSYLPHOSPHATIDYLINOSITOL; INTERLEUKIN 10; INTERLEUKIN 12; INTERLEUKIN 6; LIPOPOLYSACCHARIDE; TUMOR NECROSIS FACTOR; AUTACOID; CD1 ANTIGEN; CD1D ANTIGEN; VARIANT SURFACE GLYCOPROTEIN;

EID: 35748961998     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.179.6.4003     Document Type: Article
Times cited : (67)

References (66)
  • 3
    • 0035916983 scopus 로고    scopus 로고
    • Drug resistance in pathogenic African trypanosomes: What hopes for the future?
    • Anene, B. M., D. N. Onah, and Y. Nawa. 2001. Drug resistance in pathogenic African trypanosomes: what hopes for the future? Vet. Parasitol. 96: 83-100.
    • (2001) Vet. Parasitol , vol.96 , pp. 83-100
    • Anene, B.M.1    Onah, D.N.2    Nawa, Y.3
  • 4
    • 0034904388 scopus 로고    scopus 로고
    • Drug resistance in Trypanosoma brucei spp., the causative agents of sleeping sickness in man and nagana in cattle
    • Matovu, E., T. Seebeck, J. C. Enyaru, and R. Kaminsky. 2001. Drug resistance in Trypanosoma brucei spp., the causative agents of sleeping sickness in man and nagana in cattle. Microbes Infect. 3: 763-770.
    • (2001) Microbes Infect , vol.3 , pp. 763-770
    • Matovu, E.1    Seebeck, T.2    Enyaru, J.C.3    Kaminsky, R.4
  • 5
    • 0024163058 scopus 로고
    • How do African game animals control trypanosome infections?
    • Mulla, A. F., and L. R. Rickman. 1988. How do African game animals control trypanosome infections? Parasitol. Today 4: 352-354.
    • (1988) Parasitol. Today , vol.4 , pp. 352-354
    • Mulla, A.F.1    Rickman, L.R.2
  • 6
    • 0034977978 scopus 로고    scopus 로고
    • An update on antigenic variation in African trypanosomes
    • Vanhamme, L., E. Pays, R. McCulloch, and J. D. Barry. 2001. An update on antigenic variation in African trypanosomes. Trends Parasitol. 17: 338-343.
    • (2001) Trends Parasitol , vol.17 , pp. 338-343
    • Vanhamme, L.1    Pays, E.2    McCulloch, R.3    Barry, J.D.4
  • 7
    • 1342328134 scopus 로고    scopus 로고
    • Antigenic variation in African trypanosomes: Monitoring progress
    • McCulloch, R. 2004. Antigenic variation in African trypanosomes: monitoring progress. Trends Parasitol. 20: 117-121.
    • (2004) Trends Parasitol , vol.20 , pp. 117-121
    • McCulloch, R.1
  • 8
    • 0035007622 scopus 로고    scopus 로고
    • Analysis of macrophage activation in African trypanosomiasis
    • Paulnock, D. M., and S. P. Coller. 2001. Analysis of macrophage activation in African trypanosomiasis. J. Leukocyte Biol. 69: 685-690.
    • (2001) J. Leukocyte Biol , vol.69 , pp. 685-690
    • Paulnock, D.M.1    Coller, S.P.2
  • 9
    • 0031963652 scopus 로고    scopus 로고
    • Immunobiology of African trypanosomiasis
    • Sternberg, J. M. 1998. Immunobiology of African trypanosomiasis. Chem. Immunol. 70: 186-199.
    • (1998) Chem. Immunol , vol.70 , pp. 186-199
    • Sternberg, J.M.1
  • 10
    • 0035081401 scopus 로고    scopus 로고
    • An accessory role for the diacylglycerol moiety of variable surface glycoprotein of African trypanosomes in the stimulation of bovine monocytes
    • Sileghem, M., R. Saya, D. J. Grab, and J. Naessens. 2001. An accessory role for the diacylglycerol moiety of variable surface glycoprotein of African trypanosomes in the stimulation of bovine monocytes. Vet. Immunol. Immunopathol. 78: 325-339.
    • (2001) Vet. Immunol. Immunopathol , vol.78 , pp. 325-339
    • Sileghem, M.1    Saya, R.2    Grab, D.J.3    Naessens, J.4
  • 11
    • 0028630691 scopus 로고
    • Glycosylphosphatidylinositol toxin of Trypanosoma brucei regulates IL-1 α and TNF-α expression in macrophages by protein tyrosine kinase mediated signal transduction
    • Tachado, S. D., and L. Schofield. 1994. Glycosylphosphatidylinositol toxin of Trypanosoma brucei regulates IL-1 α and TNF-α expression in macrophages by protein tyrosine kinase mediated signal transduction. Biochem. Biophys. Res. Commun. 205: 984-991.
    • (1994) Biochem. Biophys. Res. Commun , vol.205 , pp. 984-991
    • Tachado, S.D.1    Schofield, L.2
  • 12
    • 0032519414 scopus 로고    scopus 로고
    • The glycosyl-inositol-phosphate and dimyristoylglycerol moieties of the glycosylphosphatidylinositol anchor of the trypanosome variant-specific surface glycoprotein are distinct macrophage-activating factors
    • Magez, S., B. Stijlemans, M. Radwanska, E. Pays, M. A. Ferguson, and P. De Baetselier. 1998. The glycosyl-inositol-phosphate and dimyristoylglycerol moieties of the glycosylphosphatidylinositol anchor of the trypanosome variant-specific surface glycoprotein are distinct macrophage-activating factors. J. Immunol. 160: 1949-1956.
    • (1998) J. Immunol , vol.160 , pp. 1949-1956
    • Magez, S.1    Stijlemans, B.2    Radwanska, M.3    Pays, E.4    Ferguson, M.A.5    De Baetselier, P.6
  • 15
    • 0036069888 scopus 로고    scopus 로고
    • VSG-GPI anchors of African trypanosomes: Their role in macrophage activation and induction of infection-associated immunopathology
    • Magez, S., B. Stijlemans, T. Baral, and P. De Baetselier. 2002. VSG-GPI anchors of African trypanosomes: their role in macrophage activation and induction of infection-associated immunopathology. Microbes Infect. 4: 999-1006.
    • (2002) Microbes Infect , vol.4 , pp. 999-1006
    • Magez, S.1    Stijlemans, B.2    Baral, T.3    De Baetselier, P.4
  • 16
    • 0030042523 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol toxin of Plasmodium induces nitric oxide synthase expression in macrophages and vascular endothelial cells by a protein tyrosine kinase-dependent and protein kinase C-dependent signaling pathway
    • Tachado, S. D., P. Gerold, M. J. McConville, T. Baldwin, D. Quilici, R. T. Schwarz, and L. Schofield. 1996. Glycosylphosphatidylinositol toxin of Plasmodium induces nitric oxide synthase expression in macrophages and vascular endothelial cells by a protein tyrosine kinase-dependent and protein kinase C-dependent signaling pathway. J. Immunol. 156: 1897-1907.
    • (1996) J. Immunol , vol.156 , pp. 1897-1907
    • Tachado, S.D.1    Gerold, P.2    McConville, M.J.3    Baldwin, T.4    Quilici, D.5    Schwarz, R.T.6    Schofield, L.7
  • 17
    • 0034606283 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol anchors of Plasmodium falciparum: Molecular characterization and naturally elicited antibody response that may provide immunity to malaria pathogenesis
    • Naik, R. S., O. H. Branch, A. S. Woods, M. Vijaykumar, D. J. Perkins, B. L. Nahlen, A. A. Lal, R. J. Cotter, C. E. Costello, C. F. Ockenhouse, et al. 2000. Glycosylphosphatidylinositol anchors of Plasmodium falciparum: molecular characterization and naturally elicited antibody response that may provide immunity to malaria pathogenesis. J. Exp. Med. 192: 1563-1576.
    • (2000) J. Exp. Med , vol.192 , pp. 1563-1576
    • Naik, R.S.1    Branch, O.H.2    Woods, A.S.3    Vijaykumar, M.4    Perkins, D.J.5    Nahlen, B.L.6    Lal, A.A.7    Cotter, R.J.8    Costello, C.E.9    Ockenhouse, C.F.10
  • 18
    • 19344365599 scopus 로고    scopus 로고
    • Differential antibody responses to Plasmodium falciparum glycosylphosphatidylinositol anchors in patients with cerebral and mild malaria
    • Perraut, R., B. Diatta, L. Marrama, O. Garraud, R. Jambou, S. Longacre, G. Krishnegowda, A. Dieye, and D. C. Gowda. 2005. Differential antibody responses to Plasmodium falciparum glycosylphosphatidylinositol anchors in patients with cerebral and mild malaria. Microbes Infect. 7: 682-687.
    • (2005) Microbes Infect , vol.7 , pp. 682-687
    • Perraut, R.1    Diatta, B.2    Marrama, L.3    Garraud, O.4    Jambou, R.5    Longacre, S.6    Krishnegowda, G.7    Dieye, A.8    Gowda, D.C.9
  • 19
    • 0037102205 scopus 로고    scopus 로고
    • Synthetic GPI as a candidate anti-toxic vaccine in a model of malaria
    • Schofield, L., M. C. Hewitt, K. Evans, M. A. Siomos, and P. H. Seeberger. 2002. Synthetic GPI as a candidate anti-toxic vaccine in a model of malaria. Nature 418: 785-789.
    • (2002) Nature , vol.418 , pp. 785-789
    • Schofield, L.1    Hewitt, M.C.2    Evans, K.3    Siomos, M.A.4    Seeberger, P.H.5
  • 20
    • 0030963611 scopus 로고    scopus 로고
    • Signal transduction in macrophages by glycosylphosphatidylinositols of Plasmodium, Trypanosoma, and Leishmania: Activation of protein tyrosine kinases and protein kinase C by inositolglycan and diacylglycerol moieties
    • Tachado, S. D., P. Gerold, R. Schwarz, S. Novakovic, M. McConville, and L. Schofield. 1997. Signal transduction in macrophages by glycosylphosphatidylinositols of Plasmodium, Trypanosoma, and Leishmania: activation of protein tyrosine kinases and protein kinase C by inositolglycan and diacylglycerol moieties. Proc. Natl. Acad. Sci. USA 94: 4022-4027.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4022-4027
    • Tachado, S.D.1    Gerold, P.2    Schwarz, R.3    Novakovic, S.4    McConville, M.5    Schofield, L.6
  • 22
    • 0025131829 scopus 로고
    • Purification of the membrane-form variant surface glycoprotein of Trypanosoma brucei
    • Schell, D., and P. Overath. 1990. Purification of the membrane-form variant surface glycoprotein of Trypanosoma brucei. J. Chromatogr. 521: 239-243.
    • (1990) J. Chromatogr , vol.521 , pp. 239-243
    • Schell, D.1    Overath, P.2
  • 23
    • 0021314973 scopus 로고
    • Release and purification of Trypanosoma brucei variant surface glycoprotein
    • Cross, G. A. 1984. Release and purification of Trypanosoma brucei variant surface glycoprotein. J. Cell. Biochem. 24: 79-90.
    • (1984) J. Cell. Biochem , vol.24 , pp. 79-90
    • Cross, G.A.1
  • 24
    • 0023746673 scopus 로고
    • Characterization of the cross-reacting determinant (CRD) of the glycosylphosphatidylinositol membrane anchor of Trypanosoma brucei variant surface glycoprotein
    • Zamze, S. E., M. A. Ferguson, R. Collins, R. A. Dwek, and T. W. Rademacher. 1988. Characterization of the cross-reacting determinant (CRD) of the glycosylphosphatidylinositol membrane anchor of Trypanosoma brucei variant surface glycoprotein. Eur J. Biochem. 176: 527-534.
    • (1988) Eur J. Biochem , vol.176 , pp. 527-534
    • Zamze, S.E.1    Ferguson, M.A.2    Collins, R.3    Dwek, R.A.4    Rademacher, T.W.5
  • 25
    • 0021824362 scopus 로고
    • Trypanosoma brucei variant surface glycoprotein has a sn-1,2-dimyristyl glycerol membrane anchor at its COOH terminus
    • Ferguson, M. A., K. Haldar, and G. A. Cross. 1985. Trypanosoma brucei variant surface glycoprotein has a sn-1,2-dimyristyl glycerol membrane anchor at its COOH terminus. J. Biol. Chem. 260: 4963-4968.
    • (1985) J. Biol. Chem , vol.260 , pp. 4963-4968
    • Ferguson, M.A.1    Haldar, K.2    Cross, G.A.3
  • 26
    • 0015474668 scopus 로고
    • Lipid bilayers and biomembranes
    • Bangham, A. D. 1972. Lipid bilayers and biomembranes. Annu. Rev. Biochem. 41: 753-776.
    • (1972) Annu. Rev. Biochem , vol.41 , pp. 753-776
    • Bangham, A.D.1
  • 28
    • 0020581557 scopus 로고
    • T cell-replacing activity of C8-derivatized guanine ribonucleosides
    • Goodman, M. G., and W. O. Weigle. 1983. T cell-replacing activity of C8-derivatized guanine ribonucleosides. J. Immunol. 130: 2042-2045.
    • (1983) J. Immunol , vol.130 , pp. 2042-2045
    • Goodman, M.G.1    Weigle, W.O.2
  • 29
    • 0024804105 scopus 로고
    • 8-Mercaptoguanosine-mediated enhancement of in vivo IgG1, IgG2 and IgG3 antibody responses to polysaccharide antigens in normal and xid mice
    • Mond, J. J., K. Hunter, J. J. Kenny, F. Finkelman, and K. Witherspoon. 1989. 8-Mercaptoguanosine-mediated enhancement of in vivo IgG1, IgG2 and IgG3 antibody responses to polysaccharide antigens in normal and xid mice. Immunopharmacology 18: 205-212.
    • (1989) Immunopharmacology , vol.18 , pp. 205-212
    • Mond, J.J.1    Hunter, K.2    Kenny, J.J.3    Finkelman, F.4    Witherspoon, K.5
  • 30
    • 0032986496 scopus 로고    scopus 로고
    • Tumor necrosis factor α is a key mediator in the regulation of experimental Trypanosoma brucei infections
    • Magez, S., M. Radwanska, A. Beschin, K. Sekikawa, and P. De Baetselier. 1999. Tumor necrosis factor α is a key mediator in the regulation of experimental Trypanosoma brucei infections. Infect. Immun. 67: 3128-3132.
    • (1999) Infect. Immun , vol.67 , pp. 3128-3132
    • Magez, S.1    Radwanska, M.2    Beschin, A.3    Sekikawa, K.4    De Baetselier, P.5
  • 31
    • 20044387192 scopus 로고    scopus 로고
    • Macrophage galactose-type C-type lectins as novel markers for alternatively activated macrophages elicited by parasitic infections and allergic airway inflammation
    • Raes, G., L. Brys, B. K. Dahal, J. Brandt, J. Grooten, F. Brombacher, G. Vanham, W. Noel, P. Bogaert, T. Boonefaes, et al. 2005. Macrophage galactose-type C-type lectins as novel markers for alternatively activated macrophages elicited by parasitic infections and allergic airway inflammation. J. Leukocyte Biol. 77: 321-327.
    • (2005) J. Leukocyte Biol , vol.77 , pp. 321-327
    • Raes, G.1    Brys, L.2    Dahal, B.K.3    Brandt, J.4    Grooten, J.5    Brombacher, F.6    Vanham, G.7    Noel, W.8    Bogaert, P.9    Boonefaes, T.10
  • 32
    • 33646342744 scopus 로고    scopus 로고
    • Bovine trypanotolerance: A natural ability to prevent severe anaemia and haemophagocytic syndrome?
    • Naessens, J. 2006. Bovine trypanotolerance: a natural ability to prevent severe anaemia and haemophagocytic syndrome? Int. J. Parasitol. 36: 521-528.
    • (2006) Int. J. Parasitol , vol.36 , pp. 521-528
    • Naessens, J.1
  • 33
    • 0035820184 scopus 로고    scopus 로고
    • The role of tumour necrosis factor-α in the pathogenesis of complicated falciparum malaria
    • Odeh, M. 2001. The role of tumour necrosis factor-α in the pathogenesis of complicated falciparum malaria. Cytokine 14: 11-18.
    • (2001) Cytokine , vol.14 , pp. 11-18
    • Odeh, M.1
  • 34
    • 0036180521 scopus 로고    scopus 로고
    • Control of experimental Trypanosoma brucei infections occurs independently of lymphotoxin-α induction
    • Magez, S., B. Stijlemans, G. Caljon, H. P. Eugster, and P. De Baetselier. 2002. Control of experimental Trypanosoma brucei infections occurs independently of lymphotoxin-α induction. Infect. Immun. 70: 1342-1351.
    • (2002) Infect. Immun , vol.70 , pp. 1342-1351
    • Magez, S.1    Stijlemans, B.2    Caljon, G.3    Eugster, H.P.4    De Baetselier, P.5
  • 35
    • 0028342537 scopus 로고
    • Tumour necrosis factor production by monocytes from cattle infected with Trypanosoma (Duttonella) vivax and Trypanosoma (Nannomonas) congolense: Possible association with severity of anaemia associated with the disease
    • Sileghem, M., J. N. Flynn, L. Logan-Henfrey, and J. Ellis. 1994. Tumour necrosis factor production by monocytes from cattle infected with Trypanosoma (Duttonella) vivax and Trypanosoma (Nannomonas) congolense: possible association with severity of anaemia associated with the disease. Parasite Immunol. 16: 51-54.
    • (1994) Parasite Immunol , vol.16 , pp. 51-54
    • Sileghem, M.1    Flynn, J.N.2    Logan-Henfrey, L.3    Ellis, J.4
  • 36
    • 0023193720 scopus 로고
    • Large, activated B cells are the primary B-cell target of 8-bromoguanosine and 8-mercaptoguanosine
    • Wicker, L. S., R. C. Boltz, Jr., E. A. Nichols, B. J. Miller, N. H. Sigal, and L. B. Peterson. 1987. Large, activated B cells are the primary B-cell target of 8-bromoguanosine and 8-mercaptoguanosine. Cell. Immunol. 106: 318-329.
    • (1987) Cell. Immunol , vol.106 , pp. 318-329
    • Wicker, L.S.1    Boltz Jr., R.C.2    Nichols, E.A.3    Miller, B.J.4    Sigal, N.H.5    Peterson, L.B.6
  • 37
    • 0021849830 scopus 로고
    • Demonstration of T-cell-dependent and T-cell-independent components of 8-mercaptoguanosine-mediated adjuvanticity
    • Goodman, M. G. 1985. Demonstration of T-cell-dependent and T-cell-independent components of 8-mercaptoguanosine-mediated adjuvanticity. Proc. Soc. Exp. Biol. Med. 179: 479-486.
    • (1985) Proc. Soc. Exp. Biol. Med , vol.179 , pp. 479-486
    • Goodman, M.G.1
  • 39
    • 0020384570 scopus 로고
    • Activation of the alternative pathway of bovine complement by Trypanosoma congolense
    • Tabel, H. 1982. Activation of the alternative pathway of bovine complement by Trypanosoma congolense. Parasite Immunol. 4: 329-335.
    • (1982) Parasite Immunol , vol.4 , pp. 329-335
    • Tabel, H.1
  • 40
    • 0035916971 scopus 로고    scopus 로고
    • Demonstration of erythrophagocytosis in Trypanosoma congolense-infected goats
    • Witola, W. H., and C. E. Lovelace. 2001. Demonstration of erythrophagocytosis in Trypanosoma congolense-infected goats. Vet. Parasitol. 96: 115-126.
    • (2001) Vet. Parasitol , vol.96 , pp. 115-126
    • Witola, W.H.1    Lovelace, C.E.2
  • 41
    • 0035340424 scopus 로고    scopus 로고
    • Alternative versus classical macrophage activation during experimental African trypanosomosis
    • Baetselier, P. D., B. Namangala, W. Noel, L. Brys, E. Pays, and A. Beschin. 2001. Alternative versus classical macrophage activation during experimental African trypanosomosis. Int. J. Parasitol. 31: 575-587.
    • (2001) Int. J. Parasitol , vol.31 , pp. 575-587
    • Baetselier, P.D.1    Namangala, B.2    Noel, W.3    Brys, L.4    Pays, E.5    Beschin, A.6
  • 42
    • 28444455575 scopus 로고    scopus 로고
    • Impaired Kupffer cells in highly susceptible mice infected with Trypanosoma congolense
    • Shi, M., G. Wei, W. Pan, and H. Tabel. 2005. Impaired Kupffer cells in highly susceptible mice infected with Trypanosoma congolense. Infect. Immun. 73: 8393-8396.
    • (2005) Infect. Immun , vol.73 , pp. 8393-8396
    • Shi, M.1    Wei, G.2    Pan, W.3    Tabel, H.4
  • 43
    • 33745938947 scopus 로고    scopus 로고
    • Identification of a common gene signature for type II cytokine-associated myeloid cells elicited in vivo in different pathologic conditions
    • Ghassabeh, G. H., P. De Baetselier, L. Brys, W. Noel, J. A. Van Ginderachter, S. Meerschaut, A. Beschin, F. Brombacher, and G. Raes. 2006. Identification of a common gene signature for type II cytokine-associated myeloid cells elicited in vivo in different pathologic conditions. Blood 108: 575-583.
    • (2006) Blood , vol.108 , pp. 575-583
    • Ghassabeh, G.H.1    De Baetselier, P.2    Brys, L.3    Noel, W.4    Van Ginderachter, J.A.5    Meerschaut, S.6    Beschin, A.7    Brombacher, F.8    Raes, G.9
  • 44
    • 0034488154 scopus 로고    scopus 로고
    • Selenoprotein P
    • Moschos, M. P. 2000. Selenoprotein P. Cell. Mol. Life Sci. 57: 1836-1845.
    • (2000) Cell. Mol. Life Sci , vol.57 , pp. 1836-1845
    • Moschos, M.P.1
  • 45
    • 0033152222 scopus 로고    scopus 로고
    • Blood coagulation factor XIII: Structure and function
    • Muszbek, L., V. C. Yee, and Z. Hevessy. 1999. Blood coagulation factor XIII: structure and function. Thromb. Res. 94: 271-305.
    • (1999) Thromb. Res , vol.94 , pp. 271-305
    • Muszbek, L.1    Yee, V.C.2    Hevessy, Z.3
  • 47
    • 6944224067 scopus 로고    scopus 로고
    • From pattern recognition receptor to regulator of homeostasis: The double-faced macrophage mannose receptor
    • Allavena, P., M. Chieppa, P. Monti, and L. Piemonti. 2004. From pattern recognition receptor to regulator of homeostasis: the double-faced macrophage mannose receptor. Crit. Rev. Immunol. 24: 179-192.
    • (2004) Crit. Rev. Immunol , vol.24 , pp. 179-192
    • Allavena, P.1    Chieppa, M.2    Monti, P.3    Piemonti, L.4
  • 48
    • 0030826423 scopus 로고    scopus 로고
    • Crystal structure of mouse CD1: An MHC-like fold with a large hydrophobic binding groove
    • Zeng, Z., A. R. Castano, B. W. Segelke, E. A. Stura, P. A. Peterson, and I. A. Wilson. 1997. Crystal structure of mouse CD1: an MHC-like fold with a large hydrophobic binding groove. Science 277: 339-345.
    • (1997) Science , vol.277 , pp. 339-345
    • Zeng, Z.1    Castano, A.R.2    Segelke, B.W.3    Stura, E.A.4    Peterson, P.A.5    Wilson, I.A.6
  • 49
    • 33745838249 scopus 로고    scopus 로고
    • CD1d ligands: The good, the bad, and the ugly
    • Brutkiewicz, R. R. 2006. CD1d ligands: the good, the bad, and the ugly. J. Immunol. 177: 769-775.
    • (2006) J. Immunol , vol.177 , pp. 769-775
    • Brutkiewicz, R.R.1
  • 51
    • 0027424857 scopus 로고
    • A role for TNF during African trypanosomiasis: Involvement in parasite control, immunosuppression and pathology
    • Lucas, R., S. Magez, B. Songa, A. Darji, R. Hamers, and P. de Baetselier. 1993. A role for TNF during African trypanosomiasis: involvement in parasite control, immunosuppression and pathology. Res. Immunol. 144: 370-376.
    • (1993) Res. Immunol , vol.144 , pp. 370-376
    • Lucas, R.1    Magez, S.2    Songa, B.3    Darji, A.4    Hamers, R.5    de Baetselier, P.6
  • 52
    • 0031441342 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositols of Plasmodium chabaudi chabaudi: A basis for the study of malarial glycolipid toxins in a rodent model
    • Gerold, P., L. Vivas, S. A. Ogun, N. Azzouz, K. N. Brown, A. A. Holder, and R. T. Schwarz. 1997. Glycosylphosphatidylinositols of Plasmodium chabaudi chabaudi: a basis for the study of malarial glycolipid toxins in a rodent model. Biochem. J. 328: 905-911.
    • (1997) Biochem. J , vol.328 , pp. 905-911
    • Gerold, P.1    Vivas, L.2    Ogun, S.A.3    Azzouz, N.4    Brown, K.N.5    Holder, A.A.6    Schwarz, R.T.7
  • 53
    • 0036063389 scopus 로고    scopus 로고
    • Structure and activity of glycosylphosphatidylinositol anchors of Plasmodium falciparum
    • Channe Gowda, D. 2002. Structure and activity of glycosylphosphatidylinositol anchors of Plasmodium falciparum. Microbes Infect. 4: 983-990.
    • (2002) Microbes Infect , vol.4 , pp. 983-990
    • Channe Gowda, D.1
  • 54
    • 0026558521 scopus 로고
    • Tumour necrosis factor induction by malaria exoantigens depends upon phospholipid
    • Bate, C. A., J. Taverne, E. Roman, C. Moreno, and J. H. Playfair. 1992. Tumour necrosis factor induction by malaria exoantigens depends upon phospholipid. Immunology 75: 129-135.
    • (1992) Immunology , vol.75 , pp. 129-135
    • Bate, C.A.1    Taverne, J.2    Roman, E.3    Moreno, C.4    Playfair, J.H.5
  • 55
    • 14844304290 scopus 로고    scopus 로고
    • Induction of proinflammatory responses in macrophages by the glycosylphosphatidylinositols of Plasmodium falciparum: The requirement of extracellular signal-regulated kinase, p38, c-Jun N-terminal kinase and NF-κB pathways for the expression of proinflammatory cytokines and nitric oxide
    • Zhu, J., G. Krishnegowda, and D. C. Gowda. 2005. Induction of proinflammatory responses in macrophages by the glycosylphosphatidylinositols of Plasmodium falciparum: the requirement of extracellular signal-regulated kinase, p38, c-Jun N-terminal kinase and NF-κB pathways for the expression of proinflammatory cytokines and nitric oxide. J. Biol. Chem. 280: 8617-8627.
    • (2005) J. Biol. Chem , vol.280 , pp. 8617-8627
    • Zhu, J.1    Krishnegowda, G.2    Gowda, D.C.3
  • 56
    • 0027471132 scopus 로고
    • Signal transduction in host cells by a glycosylphosphatidylinositol toxin of malaria parasites
    • Schofield, L., and F. Hackett. 1993. Signal transduction in host cells by a glycosylphosphatidylinositol toxin of malaria parasites. J. Exp. Med. 177: 145-153.
    • (1993) J. Exp. Med , vol.177 , pp. 145-153
    • Schofield, L.1    Hackett, F.2
  • 57
    • 0035831443 scopus 로고    scopus 로고
    • Plasmodium falciparum glycosylphosphatidylinositol-induced TNF-α secretion by macrophages is mediated without membrane insertion or endocytosis
    • Vijaykumar, M., R. S. Naik, and D. C. Gowda. 2001. Plasmodium falciparum glycosylphosphatidylinositol-induced TNF-α secretion by macrophages is mediated without membrane insertion or endocytosis. J. Biol. Chem. 276: 6909-6912.
    • (2001) J. Biol. Chem , vol.276 , pp. 6909-6912
    • Vijaykumar, M.1    Naik, R.S.2    Gowda, D.C.3
  • 59
    • 0042346122 scopus 로고    scopus 로고
    • Glycosylinositolphosphate soluble variant surface glycoprotein inhibits IFN-γ-induced nitric oxide production via reduction in STAT1 phosphorylation in African trypanosomiasis
    • Coller, S. P., J. M. Mansfield, and D. M. Paulnock. 2003. Glycosylinositolphosphate soluble variant surface glycoprotein inhibits IFN-γ-induced nitric oxide production via reduction in STAT1 phosphorylation in African trypanosomiasis. J. Immunol. 171: 1466-1472.
    • (2003) J. Immunol , vol.171 , pp. 1466-1472
    • Coller, S.P.1    Mansfield, J.M.2    Paulnock, D.M.3
  • 60
    • 0036301934 scopus 로고    scopus 로고
    • The relationships between intestinal damage and circulating endotoxins in experimental Trypanosoma brucei brucei infections
    • Nyakundi, J. N., B. Crawley, R. A. Smith, and V. W. Pentreath. 2002. The relationships between intestinal damage and circulating endotoxins in experimental Trypanosoma brucei brucei infections. Parasitology 124: 589-595.
    • (2002) Parasitology , vol.124 , pp. 589-595
    • Nyakundi, J.N.1    Crawley, B.2    Smith, R.A.3    Pentreath, V.W.4
  • 61
    • 0035107942 scopus 로고    scopus 로고
    • Alternative versus classical macrophage activation during experimental African trypanosomosis
    • Namangala, B., P. De Baetselier, W. Noel, L. Brys, and A. Beschin. 2001. Alternative versus classical macrophage activation during experimental African trypanosomosis. J. Leukocyte Biol. 69: 387-396.
    • (2001) J. Leukocyte Biol , vol.69 , pp. 387-396
    • Namangala, B.1    De Baetselier, P.2    Noel, W.3    Brys, L.4    Beschin, A.5
  • 62
    • 7644231561 scopus 로고    scopus 로고
    • The chemokine system in diverse forms of macrophage activation and polarization
    • Mantovani, A., A. Sica, S. Sozzani, P. Allavena, A. Vecchi, and M. Locati. 2004. The chemokine system in diverse forms of macrophage activation and polarization. Trends Immunol. 25: 677-686.
    • (2004) Trends Immunol , vol.25 , pp. 677-686
    • Mantovani, A.1    Sica, A.2    Sozzani, S.3    Allavena, P.4    Vecchi, A.5    Locati, M.6
  • 64
    • 33750584214 scopus 로고    scopus 로고
    • TLR4 links innate immunity and fatty acid-induced insulin resistance
    • Shi, H., M. V. Kokoeva, K. Inouye, I. Tzameli, H. Yin, and J. S. Flier. 2006. TLR4 links innate immunity and fatty acid-induced insulin resistance. J. Clin. Invest. 116: 3015-3025.
    • (2006) J. Clin. Invest , vol.116 , pp. 3015-3025
    • Shi, H.1    Kokoeva, M.V.2    Inouye, K.3    Tzameli, I.4    Yin, H.5    Flier, J.S.6
  • 65
    • 0029769511 scopus 로고    scopus 로고
    • Regulation of the expression of nitric oxide synthase and leishmanicidal activity by glycoconjugates of Leishmania lipophosphoglycan in murine macrophages
    • Proudfoot, L., A. V. Nikolaev, G. J. Feng, W. Q. Wei, M. A. Ferguson, J. S. Brimacombe, and F. Y. Liew. 1996. Regulation of the expression of nitric oxide synthase and leishmanicidal activity by glycoconjugates of Leishmania lipophosphoglycan in murine macrophages. Proc. Natl. Acad. Sci. USA 93: 10984-10989.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10984-10989
    • Proudfoot, L.1    Nikolaev, A.V.2    Feng, G.J.3    Wei, W.Q.4    Ferguson, M.A.5    Brimacombe, J.S.6    Liew, F.Y.7
  • 66
    • 0034577470 scopus 로고    scopus 로고
    • In vitro erythrophagocytosis by cultured macrophages stimulated with extraneous substances and those isolated from the blood, spleen and bone marrow of Boran and N'Dama cattle infected with Trypanosoma congolense and Trypanosoma vivax
    • Taiwo, V. O., and V. O. Anosa. 2000. In vitro erythrophagocytosis by cultured macrophages stimulated with extraneous substances and those isolated from the blood, spleen and bone marrow of Boran and N'Dama cattle infected with Trypanosoma congolense and Trypanosoma vivax. Onderstepoort. J. Vet. Res. 67: 273-287.
    • (2000) Onderstepoort. J. Vet. Res , vol.67 , pp. 273-287
    • Taiwo, V.O.1    Anosa, V.O.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.