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Volumn 66, Issue 6, 2004, Pages 619-625

The detection of bovine lactoferrin binding protein on Trypanosoma brucei

Author keywords

Glyceraldehyde 3 phosphate dehydrogenase; Lactoferrin; Ovotransferrin; Transferrin; Trypanosoma brucei

Indexed keywords

BACTERIA (MICROORGANISMS); BOVINAE; MAMMALIA; TRYPANOSOMA BRUCEI;

EID: 4844224546     PISSN: 09167250     EISSN: None     Source Type: Journal    
DOI: 10.1292/jvms.66.619     Document Type: Article
Times cited : (29)

References (29)
  • 1
    • 0015528159 scopus 로고
    • Lactoferrin and transferrin: A comparative study
    • Aisen, P. and Leibman, A. 1972. Lactoferrin and transferrin: a comparative study. Biochim. Biophys. Acta 257: 314-323.
    • (1972) Biochim. Biophys. Acta , vol.257 , pp. 314-323
    • Aisen, P.1    Leibman, A.2
  • 3
    • 0023443661 scopus 로고
    • Receptor-mediated endocytosis in the bloodstream form of Trypanosoma brucei
    • Coppens, I., Opperdoes, F. R., Courtoy, P. J. and Baudhuin, P. 1987. Receptor-mediated endocytosis in the bloodstream form of Trypanosoma brucei. J. Protozool. 34: 465-473.
    • (1987) J. Protozool. , vol.34 , pp. 465-473
    • Coppens, I.1    Opperdoes, F.R.2    Courtoy, P.J.3    Baudhuin, P.4
  • 5
    • 0000505513 scopus 로고
    • Identification of the parasite transf errin-receptor of Plasmodium falciparum-infected erythrocytes and its acylation via 1,2-diacyl-sn-glycerol
    • Haldar, K., Henderson, C. L. and Cross, G. A. 1986. Identification of the parasite transf errin-receptor of Plasmodium falciparum-infected erythrocytes and its acylation via 1,2-diacyl-sn-glycerol. Proc. Natl. Acad. Sci. U.S.A. 83: 8565-8569.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 8565-8569
    • Haldar, K.1    Henderson, C.L.2    Cross, G.A.3
  • 6
    • 0004262299 scopus 로고
    • (Boyer, P. D. ed.), Academic Press, New York
    • Harris, J. I. and Waters, M. 1976. The Enzymes (Boyer, P. D. ed.), Academic Press, New York.
    • (1976) The Enzymes
    • Harris, J.I.1    Waters, M.2
  • 7
    • 0021323245 scopus 로고
    • Monocyte and NK cell cytotoxic activity in human adherent cell preparations: Discriminating effects of interferon and lactoferrin
    • Horwitz, D. A., Bakke, A. C., Abo, W. and Nishiya, K. 1984. Monocyte and NK cell cytotoxic activity in human adherent cell preparations: discriminating effects of interferon and lactoferrin. J. Immunol. 132: 2370-2374.
    • (1984) J. Immunol. , vol.132 , pp. 2370-2374
    • Horwitz, D.A.1    Bakke, A.C.2    Abo, W.3    Nishiya, K.4
  • 8
  • 9
    • 0019308713 scopus 로고
    • Association of glyceraldehyde-3-phosphate-dehydrogenase with the human red blood cell membrane. A kinetic analysis
    • Kliman, H. J. and Steck, T. L. 1980. Association of glyceraldehyde-3- phosphate-dehydrogenase with the human red blood cell membrane. A kinetic analysis. J. Biol. Chem. 255: 6314-6321.
    • (1980) J. Biol. Chem. , vol.255 , pp. 6314-6321
    • Kliman, H.J.1    Steck, T.L.2
  • 10
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.) 227: 680-685.
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 11
    • 0017542540 scopus 로고
    • The isolation and bacteriostatic properties of lactoferrin from bovine milk whey
    • Law, B. A. and Reiter, B. 1977. The isolation and bacteriostatic properties of lactoferrin from bovine milk whey. J. Dairy Res. 44: 595-599.
    • (1977) J. Dairy Res. , vol.44 , pp. 595-599
    • Law, B.A.1    Reiter, B.2
  • 12
    • 0026502193 scopus 로고
    • Iron regulates growth of Trichomonas vaginalis and the expression of immunogenic trichomonad proteins
    • Lehker, M. W. and Alderete, J. F. 1992. Iron regulates growth of Trichomonas vaginalis and the expression of immunogenic trichomonad proteins. Mol. Microbiol. 6: 123-132.
    • (1992) Mol. Microbiol. , vol.6 , pp. 123-132
    • Lehker, M.W.1    Alderete, J.F.2
  • 13
    • 0022721627 scopus 로고
    • Two tandemly linked identical genes code for the glycosomal glyceraldehyde-phosphate dehydrogenase in Trypanosoma brucei
    • Michels, P. A., Poliszczak, A., Osinga, K. A., Misset, O., Van Beeumen, J., Wierenga, R. K., Borst, P. and Opperdoes, F. R. 1986. Two tandemly linked identical genes code for the glycosomal glyceraldehyde-phosphate dehydrogenase in Trypanosoma brucei. EMBO J. 5: 1049-1056.
    • (1986) EMBO J. , vol.5 , pp. 1049-1056
    • Michels, P.A.1    Poliszczak, A.2    Osinga, K.A.3    Misset, O.4    Van Beeumen, J.5    Wierenga, R.K.6    Borst, P.7    Opperdoes, F.R.8
  • 14
    • 0032975361 scopus 로고    scopus 로고
    • The staphylococcal transferrin-binding protein is a cell wall glyceraldehyde-3-phosphate dehydrogenase
    • Modun, B. and Williams, P. 1999. The staphylococcal transferrin-binding protein is a cell wall glyceraldehyde-3-phosphate dehydrogenase. Infect. Immun. 67: 1086-1092.
    • (1999) Infect. Immun. , vol.67 , pp. 1086-1092
    • Modun, B.1    Williams, P.2
  • 15
    • 0026146982 scopus 로고
    • Bovine lactoferrin receptors in Staphylococcus aureus isolated from bovine mastitis
    • Naidu, A. S., Andersson, M., Miedzobrodzki, J., Forsgren, A. and Watts, J. L. 1991. Bovine lactoferrin receptors in Staphylococcus aureus isolated from bovine mastitis. J. Dairy Sci. 74: 1218-1226.
    • (1991) J. Dairy Sci. , vol.74 , pp. 1218-1226
    • Naidu, A.S.1    Andersson, M.2    Miedzobrodzki, J.3    Forsgren, A.4    Watts, J.L.5
  • 16
    • 0020459189 scopus 로고
    • Contrasting effects of lactoferrin on human lymphocyte and monocyte natural killer activity and antibody-dependent cell-mediated cytotoxicity
    • Nishiya, K. and Horwitz, D. A. 1982. Contrasting effects of lactoferrin on human lymphocyte and monocyte natural killer activity and antibody-dependent cell-mediated cytotoxicity. J. Immunol. 129: 2519-2523.
    • (1982) J. Immunol. , vol.129 , pp. 2519-2523
    • Nishiya, K.1    Horwitz, D.A.2
  • 17
    • 0021211306 scopus 로고
    • Iron uptake and increased intracellular enzyme activity follow host lactoferrin binding by Trichomonas vaginalis receptors
    • Peterson, K. M. and Alderete, J. F. 1984. Iron uptake and increased intracellular enzyme activity follow host lactoferrin binding by Trichomonas vaginalis receptors. J. Exp. Med. 160: 398-410.
    • (1984) J. Exp. Med. , vol.160 , pp. 398-410
    • Peterson, K.M.1    Alderete, J.F.2
  • 18
    • 0028246436 scopus 로고
    • A novel heterodimeric transferrin receptor encoded by a pair of VSG expression site-associated genes in T. brucei
    • Salmon, D., Geuskens, M., Hanocq, F., Hanocq-Quertier, J., Nolan, D., Ruben, L. and Pays, E. 1994. A novel heterodimeric transferrin receptor encoded by a pair of VSG expression site-associated genes in T. brucei. Cell 78: 75-86.
    • (1994) Cell , vol.78 , pp. 75-86
    • Salmon, D.1    Geuskens, M.2    Hanocq, F.3    Hanocq-Quertier, J.4    Nolan, D.5    Ruben, L.6    Pays, E.7
  • 19
    • 0025744496 scopus 로고
    • Transferrin is a growth factor for the bloodstream form of Trypanosoma brucei
    • Schell, D., Borowy, N. K. and Overath, P. 1991. Transferrin is a growth factor for the bloodstream form of Trypanosoma brucei. Parasitol. Res. 77: 558-560.
    • (1991) Parasitol. Res. , vol.77 , pp. 558-560
    • Schell, D.1    Borowy, N.K.2    Overath, P.3
  • 20
    • 0024475213 scopus 로고
    • Identification of the transferrin- and lactoferrin- binding proteins in Haemophilus influenzae
    • Schryvers, A. B. 1989. Identification of the transferrin- and lactoferrin- binding proteins in Haemophilus influenzae. J. Med. Microbiol. 29: 121-130.
    • (1989) J. Med. Microbiol. , vol.29 , pp. 121-130
    • Schryvers, A.B.1
  • 21
    • 0023880568 scopus 로고
    • Identification and characterization of the human lactoferrin-binding protein from Neisseria meningitidis
    • Schryvers, A. B. and Morris, L. J. 1988. Identification and characterization of the human lactoferrin-binding protein from Neisseria meningitidis. Infect. Immun. 56: 1144-1149.
    • (1988) Infect. Immun. , vol.56 , pp. 1144-1149
    • Schryvers, A.B.1    Morris, L.J.2
  • 22
    • 0000505345 scopus 로고    scopus 로고
    • Lactoferrin: A marvelous protein in milk?
    • Shimazaki, K. 2000. Lactoferrin: A marvelous protein in milk? Anim. Sci. J. 71: 329-347.
    • (2000) Anim. Sci. J. , vol.71 , pp. 329-347
    • Shimazaki, K.1
  • 23
    • 0026691797 scopus 로고
    • Identification of a large pre-lysosomal compartment in the pathogenic protozoan Trypanosoma cruzi
    • Soares, M. J., Souto-Padron, T. and De Souza, W. 1992. Identification of a large pre-lysosomal compartment in the pathogenic protozoan Trypanosoma cruzi. J. Cell Sci. 102: 157-167.
    • (1992) J. Cell Sci. , vol.102 , pp. 157-167
    • Soares, M.J.1    Souto-Padron, T.2    De Souza, W.3
  • 24
    • 0031907806 scopus 로고    scopus 로고
    • Bloodstream forms of Trypanosoma brucei require only small amounts of iron for growth
    • Steverding, D. 1998. Bloodstream forms of Trypanosoma brucei require only small amounts of iron for growth. Parasitol. Res. 84: 59-62.
    • (1998) Parasitol. Res. , vol.84 , pp. 59-62
    • Steverding, D.1
  • 25
    • 0028861990 scopus 로고
    • Transferrin-binding protein complex is the receptor for transferrin uptake in Trypanosoma brucei
    • Steverding, D., Stierhof, Y. D., Fuchs, H., Tauber, R. and Overath, P. 1995. Transferrin-binding protein complex is the receptor for transferrin uptake in Trypanosoma brucei. J. Cell Biol. 131: 1173-1182.
    • (1995) J. Cell Biol. , vol.131 , pp. 1173-1182
    • Steverding, D.1    Stierhof, Y.D.2    Fuchs, H.3    Tauber, R.4    Overath, P.5
  • 26
    • 0031662736 scopus 로고    scopus 로고
    • The host-protein-independent iron uptake by Tritrichomonas foetus
    • Tachezy, J., Suchan, P., Schrevel, J. and Kulda, J. 1998. The host-protein-independent iron uptake by Tritrichomonas foetus. Exp. Parasitol. 90: 155-163.
    • (1998) Exp. Parasitol. , vol.90 , pp. 155-163
    • Tachezy, J.1    Suchan, P.2    Schrevel, J.3    Kulda, J.4
  • 27
    • 0028931748 scopus 로고
    • Mode of action of iron (III) chelators as antimalarials. III. Overadditive effects in the combined action of hydroxamate-based agents on in vitro growth of Plasmodium falciparum
    • Tsafack, A., Golenser, J., Libman, J., Shanzer, A. and Cabantchik, Z. I. 1995. Mode of action of iron (III) chelators as antimalarials. III. Overadditive effects in the combined action of hydroxamate-based agents on in vitro growth of Plasmodium falciparum. Mol. Pharmacol. 47: 403-409.
    • (1995) Mol. Pharmacol. , vol.47 , pp. 403-409
    • Tsafack, A.1    Golenser, J.2    Libman, J.3    Shanzer, A.4    Cabantchik, Z.I.5
  • 28
    • 0026787119 scopus 로고
    • Identification and isolation of the Leishmania transferrin receptor
    • Voyiatzaki, C. S. and Soteriadou, K. P. 1992. Identification and isolation of the Leishmania transferrin receptor. J. Biol. Chem. 267: 9112-9117.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9112-9117
    • Voyiatzaki, C.S.1    Soteriadou, K.P.2
  • 29
    • 0032171693 scopus 로고    scopus 로고
    • Iron acquisition by parasitic protozoa
    • Wilson, M. E. and Britigan, B. E. 1998. Iron acquisition by parasitic protozoa. Parasitol. Today 14: 348-353.
    • (1998) Parasitol. Today , vol.14 , pp. 348-353
    • Wilson, M.E.1    Britigan, B.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.