메뉴 건너뛰기




Volumn 69, Issue 3, 1996, Pages 288-296

Internalization of human lactoferrin by the Jurkat human lymphoblastic T-cell line

Author keywords

Endocytosis; Lactoferrin; Lymphocytes; Lysosome

Indexed keywords

CHLOROQUINE; FLUORESCEIN; IRON; IRON BINDING PROTEIN; LACTOFERRIN; TRANSFERRIN;

EID: 0029918626     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (40)

References (42)
  • 1
    • 0024389662 scopus 로고
    • Structure of human lactoferrin: Crystallographic structure analysis and refinement at 2.8Å resolution
    • Anderson, B. F., H. M. Baker, G. E. Norris, D. W. Rice, E. N. Baker: Structure of human lactoferrin: crystallographic structure analysis and refinement at 2.8Å resolution. J. Mol. Biol. 209, 711-734 (1989).
    • (1989) J. Mol. Biol. , vol.209 , pp. 711-734
    • Anderson, B.F.1    Baker, H.M.2    Norris, G.E.3    Rice, D.W.4    Baker, E.N.5
  • 2
    • 0028967655 scopus 로고
    • Enter a polypeptide messenger
    • Baeurle, P.: Enter a polypeptide messenger. Nature 373, 661-662 (1995).
    • (1995) Nature , vol.373 , pp. 661-662
    • Baeurle, P.1
  • 3
    • 0018608406 scopus 로고
    • Lactoferrin turnover in man
    • Bennett, R. M., T. Kokocinski: Lactoferrin turnover in man. Clin. Sci. 57, 453-460 (1979).
    • (1979) Clin. Sci. , vol.57 , pp. 453-460
    • Bennett, R.M.1    Kokocinski, T.2
  • 4
    • 0028231589 scopus 로고
    • Human lactoferrin inhibits growth and solid tumors and development of experimental metastases in mice
    • Bezault, J., R. Bhimani, J. Wiprovnick, P. Furmanski: Human lactoferrin inhibits growth and solid tumors and development of experimental metastases in mice. Cancer Res. 54, 2310-2312 (1994).
    • (1994) Cancer Res. , vol.54 , pp. 2310-2312
    • Bezault, J.1    Bhimani, R.2    Wiprovnick, J.3    Furmanski, P.4
  • 6
    • 0018132103 scopus 로고
    • Identification of lactoferrin as the granulocyte derived inhibitor of colony stimulating activity (CSA-production)
    • Broxmeyer, H. E., A. Smithyman, R. R. Eger, P. A. Meyers, M. de Sousa: Identification of lactoferrin as the granulocyte derived inhibitor of colony stimulating activity (CSA-production). J. Exp. Med. 148, 1052-1067 (1978).
    • (1978) J. Exp. Med. , vol.148 , pp. 1052-1067
    • Broxmeyer, H.E.1    Smithyman, A.2    Eger, R.R.3    Meyers, P.A.4    De Sousa, M.5
  • 9
    • 0028910517 scopus 로고
    • Sequence specificity and transcriptional activation in the binding of lactoferrin to DNA
    • He, J., P. Furmanski: Sequence specificity and transcriptional activation in the binding of lactoferrin to DNA. Nature 373, 721-724 (1995).
    • (1995) Nature , vol.373 , pp. 721-724
    • He, J.1    Furmanski, P.2
  • 10
    • 0025139279 scopus 로고
    • Isolation and partial characterization of a lactoferrin receptor from mouse intestinal brush border
    • Hu, W. L., J. Mazurier, J. Montreuil, G. Spik: Isolation and partial characterization of a lactoferrin receptor from mouse intestinal brush border. Biochemistry 29, 535-541 (1990).
    • (1990) Biochemistry , vol.29 , pp. 535-541
    • Hu, W.L.1    Mazurier, J.2    Montreuil, J.3    Spik, G.4
  • 11
    • 0027378892 scopus 로고
    • Binding of lactoferrin and transferrin to the human promonocytic cell line U937
    • Ismail, M., J. H. Brock: Binding of lactoferrin and transferrin to the human promonocytic cell line U937. J. Biol. Chem. 268, 21618-21625 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 21618-21625
    • Ismail, M.1    Brock, J.H.2
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K.: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 0025793408 scopus 로고
    • Inhibition of the specific binding of human lactoferrin to human peripheral blood phytohemagglutinin-stimulated lymphocytes by fluorescein labelling and location of the binding site
    • Legrand, D., J. Mazurier, P. Maes, E. Rochard, J. Montreuil, G. Spik: Inhibition of the specific binding of human lactoferrin to human peripheral blood phytohemagglutinin-stimulated lymphocytes by fluorescein labelling and location of the binding site. Biochem. J. 276. 733-738 (1991).
    • (1991) Biochem. J. , vol.276 , pp. 733-738
    • Legrand, D.1    Mazurier, J.2    Maes, P.3    Rochard, E.4    Montreuil, J.5    Spik, G.6
  • 14
    • 0026803187 scopus 로고
    • Molecular interactions between human lactoferrin and the phytohemagglutinin-activated human lymphocyte lactoferrin receptor lie in two loop-containing regions of the N-terminal domain I of human lactoferrin
    • Legrand, D., J. Mazurier, A. Elass, E. Rochard, G. Vergoten, P. Maes, J. Montreuil, G. Spik: Molecular interactions between human lactoferrin and the phytohemagglutinin-activated human lymphocyte lactoferrin receptor lie in two loop-containing regions of the N-terminal domain I of human lactoferrin. Biochemistry 31, 9243-9251 (1992).
    • (1992) Biochemistry , vol.31 , pp. 9243-9251
    • Legrand, D.1    Mazurier, J.2    Elass, A.3    Rochard, E.4    Vergoten, G.5    Maes, P.6    Montreuil, J.7    Spik, G.8
  • 16
    • 0141667257 scopus 로고
    • Development and evaluation of luminescence based sandwich assay for plasma lactoferrin as a marker for septis and bacterial infections in pediatric medicine
    • Maacks, S., H. Z-Yuan, W. G. Wood: Development and evaluation of luminescence based sandwich assay for plasma lactoferrin as a marker for septis and bacterial infections in pediatric medicine. J. Biolumin. Chemilumin. 3, 221-226 (1989).
    • (1989) J. Biolumin. Chemilumin. , vol.3 , pp. 221-226
    • Maacks, S.1    Yuan, H.Z.2    Wood, W.G.3
  • 17
    • 0026340745 scopus 로고
    • Binding and endocytosis of apoand holo-lactoferrin by isolated rat hepatocytes
    • McAbee, D. D., K. Esbensen: Binding and endocytosis of apoand holo-lactoferrin by isolated rat hepatocytes. J. Biol. Chem. 226, 23624-23631 (1991).
    • (1991) J. Biol. Chem. , vol.226 , pp. 23624-23631
    • McAbee, D.D.1    Esbensen, K.2
  • 18
    • 0027515007 scopus 로고
    • Lactoferrin regulates the release of tumor necrosis factor alpha and interleukin 6 in vivo
    • Machnicki, M., M. Zimecki, T. Zagulski: Lactoferrin regulates the release of tumor necrosis factor alpha and interleukin 6 in vivo. Int. J. Exp. Pathol. 74, 433-439 (1993).
    • (1993) Int. J. Exp. Pathol. , vol.74 , pp. 433-439
    • Machnicki, M.1    Zimecki, M.2    Zagulski, T.3
  • 19
    • 0014574791 scopus 로고
    • Lactoferrin an iron binding protein in neutrophilic leukocytes
    • Masson, P. L., J. F. Heremans, E. Schönne: Lactoferrin an iron binding protein in neutrophilic leukocytes. J. Exp. Med. 130, 643-658 (1969).
    • (1969) J. Exp. Med. , vol.130 , pp. 643-658
    • Masson, P.L.1    Heremans, J.F.2    Schönne, E.3
  • 21
    • 0019153180 scopus 로고
    • Comparative study of the iron-binding properties of human transferrins
    • Mazurier, J., G. Spik: Comparative study of the iron-binding properties of human transferrins. Biochim. Biophys. Acta 629, 399-408 (1980).
    • (1980) Biochim. Biophys. Acta , vol.629 , pp. 399-408
    • Mazurier, J.1    Spik, G.2
  • 22
    • 0022367691 scopus 로고
    • Visualization of lactotransferrin brush-border receptors by ligand-blotting
    • Mazurier, J., J. Montreuil, G. Spik: Visualization of lactotransferrin brush-border receptors by ligand-blotting. Biochim. Biophys. Acta 82L 453-460 (1985).
    • (1985) Biochim. Biophys. Acta , vol.82 L , pp. 453-460
    • Mazurier, J.1    Montreuil, J.2    Spik, G.3
  • 23
    • 0024586305 scopus 로고
    • Expression of human lactoferrin receptors in phytohemagglutininstimulated human peripheral blood lymphocytes
    • Mazurier, J., D. Legrand, W. L. Hu, J. Montreuil, G. Spik: Expression of human lactoferrin receptors in phytohemagglutininstimulated human peripheral blood lymphocytes. Eur. J. Biochem. 179, 481-487 (1989).
    • (1989) Eur. J. Biochem. , vol.179 , pp. 481-487
    • Mazurier, J.1    Legrand, D.2    Hu, W.L.3    Montreuil, J.4    Spik, G.5
  • 25
    • 0028025037 scopus 로고
    • Apical-tobasolateral transepithelial transport of human lactoferrin in the intestinal cell line HT29 cl. 19A
    • Mikogami, T., M. Heyman, G. Spik, J. E Desjeux: Apical-tobasolateral transepithelial transport of human lactoferrin in the intestinal cell line HT29 cl. 19A. Am. J. Physiol. 267, G308-G315 (1994).
    • (1994) Am. J. Physiol. , vol.267
    • Mikogami, T.1    Heyman, M.2    Spik, G.3    Desjeux, J.E.4
  • 26
    • 72849165990 scopus 로고
    • Isolement d'une lactosidérophiline du lait de Femme
    • Montreuil, J., S. Mullet: Isolement d'une lactosidérophiline du lait de Femme. C. R. Acad. Sci. Paris 250D, 1736-1737 (1960).
    • (1960) C. R. Acad. Sci. Paris , vol.250 D , pp. 1736-1737
    • Montreuil, J.1    Mullet, S.2
  • 27
    • 0001213833 scopus 로고
    • Préparation et propriétés de la lactosidérophiline (lactoferrine) du lait de Femme
    • Montreuil, J., J. Tonnelat, S. Mullet: Préparation et propriétés de la lactosidérophiline (lactoferrine) du lait de Femme. Biochim. Biophys. Acta 45, 413-421 (1960).
    • (1960) Biochim. Biophys. Acta , vol.45 , pp. 413-421
    • Montreuil, J.1    Tonnelat, J.2    Mullet, S.3
  • 29
    • 0025081991 scopus 로고
    • Evidence for a different mechanisms of lactoferrin and transferrin translocation on HT29-D4 cells
    • Roiron-Lagroux, D., C. Figarella: Evidence for a different mechanisms of lactoferrin and transferrin translocation on HT29-D4 cells. Biochem. Biophys. Res. Commun. 170, 837-842 (1990).
    • (1990) Biochem. Biophys. Res. Commun. , vol.170 , pp. 837-842
    • Roiron-Lagroux, D.1    Figarella, C.2
  • 30
    • 0027075914 scopus 로고
    • Characterization of lactoferrin receptor in epithelial cell lines from non-malignant human breast, benign mastopathies and breast carcinomas
    • Rochard, E., D. Legrand, M. Lecocq, R. Hamelin, M. Crépin, J. Montreuil, G. Spik: Characterization of lactoferrin receptor in epithelial cell lines from non-malignant human breast, benign mastopathies and breast carcinomas. Anticancer Res. 12, 2047-2052 (1992).
    • (1992) Anticancer Res. , vol.12 , pp. 2047-2052
    • Rochard, E.1    Legrand, D.2    Lecocq, M.3    Hamelin, R.4    Crépin, M.5    Montreuil, J.6    Spik, G.7
  • 32
    • 0023801797 scopus 로고
    • Plasma lactoferrin and plasma lactoferrin/neutrophil ratio
    • Rosenmund, A., J. Friedli, H. Bebie, P. Werner: Plasma lactoferrin and plasma lactoferrin/neutrophil ratio. Acta Haematol. 80, 40-48 (1988).
    • (1988) Acta Haematol. , vol.80 , pp. 40-48
    • Rosenmund, A.1    Friedli, J.2    Bebie, H.3    Werner, P.4
  • 33
    • 0024473916 scopus 로고
    • Lactoferrin stimulates colony stimulatjing factor production in vitro and in vivo
    • Sawatzki, G., I. N. Rich: Lactoferrin stimulates colony stimulatjing factor production in vitro and in vivo. Blood Cells 15, 371-385 (1989).
    • (1989) Blood Cells , vol.15 , pp. 371-385
    • Sawatzki, G.1    Rich, I.N.2
  • 34
    • 0026691005 scopus 로고
    • Modulation of natural killer and lymphokine-activated killer cell cytotoxicity by lactoferrin
    • Shau, H., A. Kim, H. Golub: Modulation of natural killer and lymphokine-activated killer cell cytotoxicity by lactoferrin. J. Leukocyte Biol. 51, 343-349 (1992).
    • (1992) J. Leukocyte Biol. , vol.51 , pp. 343-349
    • Shau, H.1    Kim, A.2    Golub, H.3
  • 37
    • 0026786340 scopus 로고
    • Endocytosis: What goes in and how?
    • Watts, C., M. Marsh: Endocytosis: what goes in and how? J. Cell Sci. 103, 1-8 (1992).
    • (1992) J. Cell Sci. , vol.103 , pp. 1-8
    • Watts, C.1    Marsh, M.2
  • 38
    • 0027079937 scopus 로고
    • Low density lipoprotein receptor-related protein and gp330 bind similar ligands, including plasminogen activator-inhibitor complexes and lactoferrin, an inhibitor of chylomicron remnant clearance
    • Willnow, T. E., J. L. Goldstein, K. Orth, M. S. Brown, J. Herz: Low density lipoprotein receptor-related protein and gp330 bind similar ligands, including plasminogen activator-inhibitor complexes and lactoferrin, an inhibitor of chylomicron remnant clearance. J. Biol. Chem. 267, 26172-26180 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 26172-26180
    • Willnow, T.E.1    Goldstein, J.L.2    Orth, K.3    Brown, M.S.4    Herz, J.5
  • 39
    • 0024842051 scopus 로고
    • Lactoferrin can protect mice against a lethal dose of E. coli in experimental infection in vivo
    • Zagulski, T., P. Lipinski, A. Zagulska, S. Bronieck, Z. Jarbazek: Lactoferrin can protect mice against a lethal dose of E. coli in experimental infection in vivo. Br. J. Exp. Pathol. 70, 697-704 (1989).
    • (1989) Br. J. Exp. Pathol. , vol.70 , pp. 697-704
    • Zagulski, T.1    Lipinski, P.2    Zagulska, A.3    Bronieck, S.4    Jarbazek, Z.5
  • 41
  • 42
    • 0024468617 scopus 로고
    • Lactoferrin decreases monocyte induced fibroblast production of myeloid colony stimulating-activity by suppressing monocyte release of interleukin 1
    • Zucali, J. R., H. E. Broxmeyer, D. Levy, C. Morse: Lactoferrin decreases monocyte induced fibroblast production of myeloid colony stimulating-activity by suppressing monocyte release of interleukin 1. Blood 74, 1531-1536 (1989).
    • (1989) Blood , vol.74 , pp. 1531-1536
    • Zucali, J.R.1    Broxmeyer, H.E.2    Levy, D.3    Morse, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.