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Volumn 269, Issue 18, 2002, Pages 4435-4445

The soluble form of the membrane-bound transferrin homologue, melanotransferrin, inefficiently donates iron to cells via nonspecific internalization and degradation of the protein

Author keywords

Iron; Iron uptake; Melanotransferrin; Transferrin; Transferrin receptor

Indexed keywords

IODINE 125; IRON 59; IRON BINDING PROTEIN; MELANOTRANSFERRIN; TRANSFERRIN; TRANSFERRIN RECEPTOR; UNCLASSIFIED DRUG;

EID: 0036381706     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2002.03140.x     Document Type: Article
Times cited : (37)

References (51)
  • 2
    • 0019428822 scopus 로고
    • Analysis of normal and neoplastic human tissues for the tumor-associated protein p97
    • Woodbury, R.G., Brown, J.P., Loop, S.M., Hellström, K.E. & Hellström, I. (1981) Analysis of normal and neoplastic human tissues for the tumor-associated protein p97. Int. J. Cancer 27, 145-149.
    • (1981) Int. J. Cancer , vol.27 , pp. 145-149
    • Woodbury, R.G.1    Brown, J.P.2    Loop, S.M.3    Hellström, K.E.4    Hellström, I.5
  • 4
    • 0023108569 scopus 로고
    • Immunohistochemical detection of antigen in human primary and metastatic melanomas by the monoclonal antibody 140.240 and its possible prognostic significance
    • Natali, P.G., Roberts, J.T., Difilippo, F., Bigotti, A., Dent, P.B., Ferrone, S. & Liao, S.K. (1987) Immunohistochemical detection of antigen in human primary and metastatic melanomas by the monoclonal antibody 140.240 and its possible prognostic significance. Cancer 59, 55-63.
    • (1987) Cancer , vol.59 , pp. 55-63
    • Natali, P.G.1    Roberts, J.T.2    Difilippo, F.3    Bigotti, A.4    Dent, P.B.5    Ferrone, S.6    Liao, S.K.7
  • 5
    • 0027312095 scopus 로고
    • Glycosyl phosphatidylinositol membrane anchoring of melanotransferrin (p97): Apical compartmentalization in intestinal epithelial cells
    • Alemany, R., Rosa Vilá, M., Franci, C., Egea, G., Real, F.X. & Thompson, J.M. (1993) Glycosyl phosphatidylinositol membrane anchoring of melanotransferrin (p97): apical compartmentalization in intestinal epithelial cells. J. Cell Sci. 104, 1155-1162.
    • (1993) J. Cell Sci. , vol.104 , pp. 1155-1162
    • Alemany, R.1    Rosa Vilá, M.2    Franci, C.3    Egea, G.4    Real, F.X.5    Thompson, J.M.6
  • 6
    • 0024539607 scopus 로고
    • In situ localization of melanotransferrin (melanoma-associated antigen P97) in human liver. A light- and electron-microscopic immunohistochemical study
    • Sciot, R., De Vos, R., van Eyken, P., van der Steen, K., Moerman, P. & Desmet, V.J. (1989) In situ localization of melanotransferrin (melanoma-associated antigen P97) in human liver. A light- and electron-microscopic immunohistochemical study. Liver 9, 110-119.
    • (1989) Liver , vol.9 , pp. 110-119
    • Sciot, R.1    De Vos, R.2    Van Eyken, P.3    Van der Steen, K.4    Moerman, P.5    Desmet, V.J.6
  • 7
    • 0029935613 scopus 로고    scopus 로고
    • Reactive microglia specifically associated with amyloid plaques in Alzheimer's disease brain tissue express melanotransferrin
    • Jefferies, W.A., Food, M.R., Gabathuler, R., Rothenberger, S., Yamada, T., Yasuhara, O. & McGeer, P.L. (1996) Reactive microglia specifically associated with amyloid plaques in Alzheimer's disease brain tissue express melanotransferrin. Brain Res. 712, 122-126.
    • (1996) Brain Res. , vol.712 , pp. 122-126
    • Jefferies, W.A.1    Food, M.R.2    Gabathuler, R.3    Rothenberger, S.4    Yamada, T.5    Yasuhara, O.6    McGeer, P.L.7
  • 8
  • 9
    • 0034054183 scopus 로고    scopus 로고
    • The role of melanotransferrin (tumor antigen p97) in iron uptake by the human malignant melanoma cell
    • Richardson, D.R. (2000) The role of melanotransferrin (tumor antigen p97) in iron uptake by the human malignant melanoma cell. Eur. J. Biochem. 267, 1290-1298.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1290-1298
    • Richardson, D.R.1
  • 10
    • 0019493358 scopus 로고
    • Structural characterization of human melanoma-associated antigen p97 with monoclonal antibodies
    • Brown, J.P., Nishiyama, K., Hellström, I. & Hellström, K.E. (1981) Structural characterization of human melanoma-associated antigen p97 with monoclonal antibodies. J. Immunol. 127, 539-546.
    • (1981) J. Immunol. , vol.127 , pp. 539-546
    • Brown, J.P.1    Nishiyama, K.2    Hellström, I.3    Hellström, K.E.4
  • 12
    • 0008144817 scopus 로고
    • Primary structure of human melanoma-associated antigen p97 (melanotransferrin) deduced from the mRNA sequence
    • Rose, T.M., Plowman, G.D., Teplow, D.B., Dreyer, W.J., Hellström, K.E. & Brown, J.P. (1986) Primary structure of human melanoma-associated antigen p97 (melanotransferrin) deduced from the mRNA sequence. Proc. Natl. Acad. Sci. USA 83, 1261-1265.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 1261-1265
    • Rose, T.M.1    Plowman, G.D.2    Teplow, D.B.3    Dreyer, W.J.4    Hellström, K.E.5    Brown, J.P.6
  • 15
    • 0034644835 scopus 로고    scopus 로고
    • The membrane-bound transferrin homologue melanotransferrin: Roles other than iron transport?
    • Sekyere, E. & Richardson, D.R. (2000) The membrane-bound transferrin homologue melanotransferrin: Roles other than iron transport? FEBS Lett. 483, 11-16.
    • (2000) FEBS Lett. , vol.483 , pp. 11-16
    • Sekyere, E.1    Richardson, D.R.2
  • 16
    • 0028111120 scopus 로고
    • Transport and expression in human melanomas of a transferrin-like glycosylphosphatidylinositol-anchored protein
    • Food, M.R., Rothenberger, S., Gabathuler, R., Haidl, I.D., Reid, G. & Jefferies, W.A. (1994) Transport and expression in human melanomas of a transferrin-like glycosylphosphatidylinositol-anchored protein. J. Biol. Chem. 269, 3034-3040.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3034-3040
    • Food, M.R.1    Rothenberger, S.2    Gabathuler, R.3    Haidl, I.D.4    Reid, G.5    Jefferies, W.A.6
  • 19
    • 0029955035 scopus 로고    scopus 로고
    • Serum levels of the iron binding protein p97 are elevated in Alzheimer's disease
    • Kennard, M.L., Feldman, H., Yamada, T. & Jefferies, W.A. (1996) Serum levels of the iron binding protein p97 are elevated in Alzheimer's disease. Nature Med. 2, 1230-1235.
    • (1996) Nature Med. , vol.2 , pp. 1230-1235
    • Kennard, M.L.1    Feldman, H.2    Yamada, T.3    Jefferies, W.A.4
  • 21
    • 0037070209 scopus 로고    scopus 로고
    • A second melanotransferrin gene (MTf2) and a novel protein isoform: Explanation for the membrane-bound and soluble forms of melanotransferrin?
    • Sekyere, E., Food, M.R. & Richardson, D.R. (2002) A second melanotransferrin gene (MTf2) and a novel protein isoform: Explanation for the membrane-bound and soluble forms of melanotransferrin? FEBS Lett. 512, 350-352.
    • (2002) FEBS Lett. , vol.512 , pp. 350-352
    • Sekyere, E.1    Food, M.R.2    Richardson, D.R.3
  • 22
    • 0025341256 scopus 로고
    • The uptake of iron and transferrin by the human melanoma cell
    • Richardson, D.R. & Baker, E. (1990) The uptake of iron and transferrin by the human melanoma cell. Biochim. Biophys. Acta 1053, 1-12.
    • (1990) Biochim. Biophys. Acta , vol.1053 , pp. 1-12
    • Richardson, D.R.1    Baker, E.2
  • 23
    • 0027944830 scopus 로고
    • Two saturable mechanisms of iron uptake from transferrin in human melanoma cells: The effect of transferrin concentration, chelators, and metabolic probes on transferrin and iron uptake
    • Richardson, D.R. & Baker, E. (1994) Two saturable mechanisms of iron uptake from transferrin in human melanoma cells: The effect of transferrin concentration, chelators, and metabolic probes on transferrin and iron uptake. J. Cell. Physiol. 161, 160-168.
    • (1994) J. Cell. Physiol. , vol.161 , pp. 160-168
    • Richardson, D.R.1    Baker, E.2
  • 24
    • 0025793961 scopus 로고
    • The uptake of inorganic iron complexes by human melanoma cells
    • Richardson, D. & Baker, E. (1991) The uptake of inorganic iron complexes by human melanoma cells. Biochim. Biophys. Acta 1093, 20-28.
    • (1991) Biochim. Biophys. Acta , vol.1093 , pp. 20-28
    • Richardson, D.1    Baker, E.2
  • 25
    • 0026081935 scopus 로고
    • The release of iron and transferrin by the human melanoma cell
    • Richardson, D.R. & Baker, E. (1991) The release of iron and transferrin by the human melanoma cell. Biochim. Biophys. Acta 1091, 294-304.
    • (1991) Biochim. Biophys. Acta , vol.1091 , pp. 294-304
    • Richardson, D.R.1    Baker, E.2
  • 27
    • 0022515085 scopus 로고
    • The mechanisms of iron uptake by rat fetal hepatocytes
    • Trinder, D., Morgan, E.H. & Baker, E. (1986) The mechanisms of iron uptake by rat fetal hepatocytes. Hepatology 6, 852-858.
    • (1986) Hepatology , vol.6 , pp. 852-858
    • Trinder, D.1    Morgan, E.H.2    Baker, E.3
  • 28
    • 0029953577 scopus 로고    scopus 로고
    • Transferrin receptor-independent uptake of diferric transferrin by human hepatoma cells with antisense inhibition of receptor expression
    • Trinder, D., Zak, O. & Aisen, P. (1996) Transferrin receptor-independent uptake of diferric transferrin by human hepatoma cells with antisense inhibition of receptor expression. Hepatology 23, 1512-1520.
    • (1996) Hepatology , vol.23 , pp. 1512-1520
    • Trinder, D.1    Zak, O.2    Aisen, P.3
  • 29
    • 0019860059 scopus 로고
    • Transferrin biochemistry, physiology and clinical significance
    • Morgan, E.H. (1981) Transferrin biochemistry, physiology and clinical significance. Mol. Aspects Med. 4, 1-123.
    • (1981) Mol. Aspects Med. , vol.4 , pp. 1-123
    • Morgan, E.H.1
  • 30
    • 0019794184 scopus 로고
    • Receptor-mediated endocytosis of transferrin in totipotent mouse teratocarcinoma cells
    • Karin, M. & Mintz, B. (1981) Receptor-mediated endocytosis of transferrin in totipotent mouse teratocarcinoma cells. J. Biol. Chem. 256, 3245-3252.
    • (1981) J. Biol. Chem. , vol.256 , pp. 3245-3252
    • Karin, M.1    Mintz, B.2
  • 31
    • 0033597780 scopus 로고    scopus 로고
    • Molecular cloning of transferrin receptor 2: A new member of the transferrin receptor-like family
    • Kawabata, H., Yang, R., Hirama, T., Vuong, P.T., Kawano, S., Gombart, A.F. & Koeffler, H.P. (1999) Molecular cloning of transferrin receptor 2: a new member of the transferrin receptor-like family. J. Biol. Chem. 274, 20826-20832.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20826-20832
    • Kawabata, H.1    Yang, R.2    Hirama, T.3    Vuong, P.T.4    Kawano, S.5    Gombart, A.F.6    Koeffler, H.P.7
  • 32
    • 0021220580 scopus 로고
    • Transferrin and iron uptake by rat hepatocytes in culture
    • Page, M.A., Baker, E. & Morgan, E.H. (1984) Transferrin and iron uptake by rat hepatocytes in culture. Am. J. Physiol. 246, G26-G33.
    • (1984) Am. J. Physiol. , vol.246
    • Page, M.A.1    Baker, E.2    Morgan, E.H.3
  • 33
    • 0029152149 scopus 로고
    • Uptake of iron from N-terminal half-transferrin by isolated rat hepatocytes. Evidence of transferrin-receptor-independent iron uptake
    • Thorstensen, K., Trinder, D., Zak, O. & Aisen, P. (1995) Uptake of iron from N-terminal half-transferrin by isolated rat hepatocytes. Evidence of transferrin-receptor-independent iron uptake. Eur. J. Biochem. 232, 129-133.
    • (1995) Eur. J. Biochem. , vol.232 , pp. 129-133
    • Thorstensen, K.1    Trinder, D.2    Zak, O.3    Aisen, P.4
  • 34
    • 0027943480 scopus 로고
    • Purification of a cell growth factor from a human lung cancer cell line: Its relationship with ferritin
    • Kikyo, N., Hagiwara, K., Fujisawa, M., Kikyo, N., Yazaki, Y. & Okabe, T. (1994) Purification of a cell growth factor from a human lung cancer cell line: Its relationship with ferritin. J. Cell. Physiol. 161, 106-110.
    • (1994) J. Cell. Physiol. , vol.161 , pp. 106-110
    • Kikyo, N.1    Hagiwara, K.2    Fujisawa, M.3    Kikyo, N.4    Yazaki, Y.5    Okabe, T.6
  • 36
    • 0023243675 scopus 로고
    • Functional expression of the human transferrin receptor cDNA in Chinese hamster ovary cells deficient in endogenous transferrin receptor
    • McGraw, T.E., Greenfield, L. & Maxfield, F.R. (1987) Functional expression of the human transferrin receptor cDNA in Chinese hamster ovary cells deficient in endogenous transferrin receptor. J. Cell. Biol. 105, 207-214.
    • (1987) J. Cell. Biol. , vol.105 , pp. 207-214
    • McGraw, T.E.1    Greenfield, L.2    Maxfield, F.R.3
  • 37
    • 0026770143 scopus 로고
    • Transferrin-receptor-independent but iron-dependent proliferation of variant Chinese hamster ovary cells
    • Chan, R.Y., Ponka, P. & Schulman, H.M. (1992) Transferrin-receptor-independent but iron-dependent proliferation of variant Chinese hamster ovary cells. Exp. Cell. Res. 202, 326-336.
    • (1992) Exp. Cell. Res. , vol.202 , pp. 326-336
    • Chan, R.Y.1    Ponka, P.2    Schulman, H.M.3
  • 39
    • 0029865751 scopus 로고    scopus 로고
    • Distribution of iron in reticulocytes after inhibition of heme synthesis with succinylacetone. Examination of the intermediates involved in iron metabolism
    • Richardson, D.R., Ponka, P. & Vyoral, D. (1996) Distribution of iron in reticulocytes after inhibition of heme synthesis with succinylacetone. Examination of the intermediates involved in iron metabolism. Blood 87, 3477-3488.
    • (1996) Blood , vol.87 , pp. 3477-3488
    • Richardson, D.R.1    Ponka, P.2    Vyoral, D.3
  • 40
    • 34548003946 scopus 로고
    • Efficient trace labelling of protein with iodine
    • McFarlane, A.S. (1958) Efficient trace labelling of protein with iodine. Nature 182, 53.
    • (1958) Nature , vol.182 , pp. 53
    • McFarlane, A.S.1
  • 43
    • 0020333335 scopus 로고
    • 125I-protein uptake from the adult mouse gut
    • 125I-protein uptake from the adult mouse gut. Gut 23, 1077-1080.
    • (1982) Gut , vol.23 , pp. 1077-1080
    • Skogh, T.1
  • 44
    • 0028891974 scopus 로고
    • The potential of iron chelators of the pyridoxal isonicotinoyl hydrazone class as effective anti-proliferative agents
    • Richardson, D.R., Tran, E.H. & Ponka, P. (1995) The potential of iron chelators of the pyridoxal isonicotinoyl hydrazone class as effective anti-proliferative agents. Blood 86, 4295-4306.
    • (1995) Blood , vol.86 , pp. 4295-4306
    • Richardson, D.R.1    Tran, E.H.2    Ponka, P.3
  • 45
    • 0026575576 scopus 로고
    • Evaluation of the iron chelation potential of hydrazones of pyridoxal, salicylaldehyde and 2-hydroxy-1-naphthylaldehyde using the hepatocyte in culture
    • Baker, E., Richardson, D.R., Gross, A. & Ponka, P. (1992) Evaluation of the iron chelation potential of hydrazones of pyridoxal, salicylaldehyde and 2-hydroxy-1-naphthylaldehyde using the hepatocyte in culture. Hepatology 15, 492-501.
    • (1992) Hepatology , vol.15 , pp. 492-501
    • Baker, E.1    Richardson, D.R.2    Gross, A.3    Ponka, P.4
  • 46
    • 0036373911 scopus 로고    scopus 로고
    • The mechanism of nitrogen monoxide (NO) -mediated iron mobilization from cells: NO intercepts iron before incorporation into ferritin and indirectly mobilizes iron from ferritin in a glutathione-dependent manner
    • Watts, R.N. & Richardson, D.R. (2002) The mechanism of nitrogen monoxide (NO) -mediated iron mobilization from cells: NO intercepts iron before incorporation into ferritin and indirectly mobilizes iron from ferritin in a glutathione-dependent manner. Eur. J. Biochem. 269, 3382-3392.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3382-3392
    • Watts, R.N.1    Richardson, D.R.2
  • 47
    • 0035863245 scopus 로고    scopus 로고
    • Endogenous glycosylphosphatidylinositol-specific phospholipase releases renal dipeptidase from kidney proximal tubules in vitro
    • Park, S.W., Choi, K., Kim, I.C., Lee, H.H., Hooper, N.M. & Park, H.S. (2001) Endogenous glycosylphosphatidylinositol-specific phospholipase releases renal dipeptidase from kidney proximal tubules in vitro. Biochem. J. 353, 339-344.
    • (2001) Biochem. J. , vol.353 , pp. 339-344
    • Park, S.W.1    Choi, K.2    Kim, I.C.3    Lee, H.H.4    Hooper, N.M.5    Park, H.S.6
  • 48
    • 0035930894 scopus 로고    scopus 로고
    • Analysis of the C-terminal structure of urinary tamm-horsfall protein reveals that the release of the glycosyl phosphatidylinositol-anchored counterpart from the kidney occurs by phenylalanine-specific proteolysis
    • Fukuoka, S. & Kobayashi, K. (2001) Analysis of the C-terminal structure of urinary tamm-horsfall protein reveals that the release of the glycosyl phosphatidylinositol-anchored counterpart from the kidney occurs by phenylalanine-specific proteolysis. Biochem. Biophys. Res. Commun. 289, 1044-1048.
    • (2001) Biochem. Biophys. Res. Commun. , vol.289 , pp. 1044-1048
    • Fukuoka, S.1    Kobayashi, K.2
  • 51
    • 0037022176 scopus 로고    scopus 로고
    • A new method for obtaining human transferrin C-lobe in the native conformation: Preparation and properties
    • Zak, O. & Aisen, P. (2002) A new method for obtaining human transferrin C-lobe in the native conformation: preparation and properties. Biochemistry 41, 1647-1653.
    • (2002) Biochemistry , vol.41 , pp. 1647-1653
    • Zak, O.1    Aisen, P.2


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