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Volumn 168, Issue 1, 1996, Pages 71-80

Hemopexin in the human retina: Protection of the retina against heme-mediated toxicity

Author keywords

[No Author keywords available]

Indexed keywords

ANTIOXIDANT; FERRIC ION; FERRITIN; FREE RADICAL; HEME; HEME OXYGENASE; HEMOPEXIN; METALLOTHIONEIN; REACTIVE OXYGEN METABOLITE; TRANSFERRIN;

EID: 0030017273     PISSN: 00219541     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-4652(199607)168:1<71::AID-JCP9>3.0.CO;2-5     Document Type: Article
Times cited : (63)

References (64)
  • 1
    • 0024427488 scopus 로고
    • Receptor-mediated transport of heme by hemopexin regulates gene expression in mammalian cells
    • Alam, J., and Smith, A. (1989) Receptor-mediated transport of heme by hemopexin regulates gene expression in mammalian cells. J. Biol. Chem., 264:17637-17640.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17637-17640
    • Alam, J.1    Smith, A.2
  • 2
    • 0026665256 scopus 로고
    • Heme-hemopexin-mediated induction of metallothionein gene expression
    • Alam, J., and Smith, A. (1992) Heme-hemopexin-mediated induction of metallothionein gene expression. J. Biol. Chem., 267:16379-16384.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16379-16384
    • Alam, J.1    Smith, A.2
  • 3
    • 0024516371 scopus 로고
    • Transcriptional activation of the heme oxygenase gene by heme and cadmium in mouse hepatoma cells
    • Alam, J., Shibahara, S., and Smith, A. (1989) Transcriptional activation of the heme oxygenase gene by heme and cadmium in mouse hepatoma cells. J. Biol. Chem., 264:6371-6375.
    • (1989) J. Biol. Chem. , vol.264 , pp. 6371-6375
    • Alam, J.1    Shibahara, S.2    Smith, A.3
  • 4
    • 0019170218 scopus 로고
    • Serum-free cell culture: A unifying approach
    • Barnes, D., and Sato, G. (1980) Serum-free cell culture: A unifying approach. Cell, 22:649-655.
    • (1980) Cell , vol.22 , pp. 649-655
    • Barnes, D.1    Sato, G.2
  • 5
    • 0016272915 scopus 로고
    • Heme complexes of rabbit hemopexin, human hemopexin and human serum-albumin: Electron spin resonance and Mossbauer spectroscopic studies
    • Bearden, A.J., Morgan, W.T., and Muller-Eberhard, U. (1974) Heme complexes of rabbit hemopexin, human hemopexin and human serum-albumin: Electron spin resonance and Mossbauer spectroscopic studies. Biochem. Biophys. Res. Commun., 61:265-272.
    • (1974) Biochem. Biophys. Res. Commun. , vol.61 , pp. 265-272
    • Bearden, A.J.1    Morgan, W.T.2    Muller-Eberhard, U.3
  • 7
    • 0027741818 scopus 로고
    • The retinal pigment epithelium: A versatile partner in vision
    • Bok, D. (1993) The retinal pigment epithelium: a versatile partner in vision. J. Cell Sci., 17(Suppl):189-195.
    • (1993) J. Cell Sci. , vol.17 , Issue.SUPPL. , pp. 189-195
    • Bok, D.1
  • 8
    • 0017112585 scopus 로고
    • Transport of retinol from the blood to the retina: An autoradiographic study of the pigment epithelial cell surface receptor for plasma retinol-binding protein
    • Bok, D., and Heller, J. (1976) Transport of retinol from the blood to the retina: An autoradiographic study of the pigment epithelial cell surface receptor for plasma retinol-binding protein. Exp. Eye Res., 22:395-402.
    • (1976) Exp. Eye Res. , vol.22 , pp. 395-402
    • Bok, D.1    Heller, J.2
  • 9
    • 0026603267 scopus 로고
    • Prevention of pre-PCR mis-priming and primer dimerization improves low-copy-number amplification
    • Chou, Q., Russell, M., Birch, D.E., Raymond, J., and Bloch, W. (1992) Prevention of pre-PCR mis-priming and primer dimerization improves low-copy-number amplification. Nucleic Acids Res., 7:1717-1723.
    • (1992) Nucleic Acids Res. , vol.7 , pp. 1717-1723
    • Chou, Q.1    Russell, M.2    Birch, D.E.3    Raymond, J.4    Bloch, W.5
  • 10
    • 0018424866 scopus 로고
    • The blood-ocular barriers
    • Cuhna-Vaz, J. (1979) The blood-ocular barriers. Surv. Ophthal., 23:279-296.
    • (1979) Surv. Ophthal. , vol.23 , pp. 279-296
    • Cuhna-Vaz, J.1
  • 11
    • 0018582274 scopus 로고
    • Hepatic subcellular metabolism of heme from heme-hemopexin: Incorporation of iron into ferritin
    • Davies, D.M., Smith, A., Muller-Eberhard, U., and Morgan, W.T. (1979) Hepatic subcellular metabolism of heme from heme-hemopexin: Incorporation of iron into ferritin. Biochem. Biophys. Res. Commun., 91:1504-1511.
    • (1979) Biochem. Biophys. Res. Commun. , vol.91 , pp. 1504-1511
    • Davies, D.M.1    Smith, A.2    Muller-Eberhard, U.3    Morgan, W.T.4
  • 12
    • 0027259012 scopus 로고
    • Transferrin is made and bound by photoreceptor cells
    • Davis, A.A., and Hunt, R.C. (1993) Transferrin is made and bound by photoreceptor cells. J. Cell. Physiol., 156:280-285.
    • (1993) J. Cell. Physiol. , vol.156 , pp. 280-285
    • Davis, A.A.1    Hunt, R.C.2
  • 13
    • 0028903353 scopus 로고
    • A human retinal pigment epithelial cell line that retains epithelial characteristics after prolonged culture
    • Davis, A.A., Bernstein, P., Bok, D., Turner, J., Nachtigal, M., and Hunt, R.C. (1995) A human retinal pigment epithelial cell line that retains epithelial characteristics after prolonged culture. Invest. Ophthalmol. Vis. Sci., 36.955-964.
    • (1995) Invest. Ophthalmol. Vis. Sci. , vol.36 , pp. 955-964
    • Davis, A.A.1    Bernstein, P.2    Bok, D.3    Turner, J.4    Nachtigal, M.5    Hunt, R.C.6
  • 14
    • 0028033537 scopus 로고
    • Brain-specific expression of the human transferrin gene. Similar elements govern transcription in oligodendrocytes and in a neuronal cell line
    • Espinosa de los Monteros, A., Sawaya, B.E., Guillou, F., Zakin, M.M., De Vellis, J., and Schaeffer, E. (1994) Brain-specific expression of the human transferrin gene. Similar elements govern transcription in oligodendrocytes and in a neuronal cell line. J. Biol. Chem., 269:24504-24510.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24504-24510
    • Espinosa De Los Monteros, A.1    Sawaya, B.E.2    Guillou, F.3    Zakin, M.M.4    De Vellis, J.5    Schaeffer, E.6
  • 15
    • 0026635456 scopus 로고
    • Iron and oxygen radicals in brain
    • Gutteridge, J.M.C. (1992) Iron and oxygen radicals in brain. Ann. Neurol., 32:S16-S21.
    • (1992) Ann. Neurol. , vol.32
    • Gutteridge, J.M.C.1
  • 16
    • 0024241523 scopus 로고
    • Antioxidant protection by haemopexin of haem-stimulated lipid peroxidation
    • Gutteridge, J.M C., and Smith, A. (1988) Antioxidant protection by haemopexin of haem-stimulated lipid peroxidation. Biochem. J., 256:861-865.
    • (1988) Biochem. J. , vol.256 , pp. 861-865
    • Gutteridge, J.M.C.1    Smith, A.2
  • 17
    • 0026773281 scopus 로고
    • Oxygen radicals as key mediators in neurological disease: Fact or fiction?
    • Halliwell, B. (1992) Oxygen radicals as key mediators in neurological disease: Fact or fiction?. Ann. Neurol., 32:S10-S15.
    • (1992) Ann. Neurol. , vol.32
    • Halliwell, B.1
  • 19
    • 0025126555 scopus 로고
    • Role of free radicals and catalytic metal ions in human disease: An overview
    • L. Packer, and A.N. Glazer, eds. Academic Press, New York
    • Halliwell, B., and Gutteridge, J.M.C. (1990) Role of free radicals and catalytic metal ions in human disease: An overview. In: Methods in Enzymology. L. Packer, and A.N. Glazer, eds. Academic Press, New York, pp. 1-85.
    • (1990) Methods in Enzymology , pp. 1-85
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 20
    • 8944224496 scopus 로고
    • Transferrin: Receptor-mediated endocytosis and iron delivery
    • I. Pastan and M.C. Willingham, eds. Plenum Press, New York
    • Hanover, J.A., and Dickson, R.B. (1985) Transferrin: Receptor-mediated endocytosis and iron delivery. In: Endocytosis. I. Pastan and M.C. Willingham, eds. Plenum Press, New York, pp. 131-161.
    • (1985) Endocytosis , pp. 131-161
    • Hanover, J.A.1    Dickson, R.B.2
  • 21
    • 0022981514 scopus 로고
    • Contributions of plasma proteins to the vitreous of the rat
    • Hawkins, K.N. (1986) Contributions of plasma proteins to the vitreous of the rat. Curr. Eye Res., 5:655-663.
    • (1986) Curr. Eye Res. , vol.5 , pp. 655-663
    • Hawkins, K.N.1
  • 22
    • 0016784512 scopus 로고
    • Interactions of plasma retinol-binding protein with its receptor. Specific binding of bovine and human retinol-binding protein to pigment epithelium cells from bovine eyes
    • Heller, J. (1975) Interactions of plasma retinol-binding protein with its receptor. Specific binding of bovine and human retinol-binding protein to pigment epithelium cells from bovine eyes. J. Biol. Chem., 250:3613-3619.
    • (1975) J. Biol. Chem. , vol.250 , pp. 3613-3619
    • Heller, J.1
  • 23
    • 0019836314 scopus 로고
    • Catabolism of globin-haptoglobin in liver cells after intravenous administration of hemoglobin-haptoglobin to rats
    • Higa, Y., Oshiro, S., Kino, K., Tsunoo, H., and Nakajima, H. (1981) Catabolism of globin-haptoglobin in liver cells after intravenous administration of hemoglobin-haptoglobin to rats. J. Biol. Chem., 256:12322-12328.
    • (1981) J. Biol. Chem. , vol.256 , pp. 12322-12328
    • Higa, Y.1    Oshiro, S.2    Kino, K.3    Tsunoo, H.4    Nakajima, H.5
  • 24
    • 0015980699 scopus 로고
    • Transfer of heme from ferrihemoglobin and ferrihemoglobin isolated chains to hemopexin
    • Hrkal, Z , Vodrazka, Z., and Kalousek, I. (1974) Transfer of heme from ferrihemoglobin and ferrihemoglobin isolated chains to hemopexin. Eur. J. Biochem., 43:73-78.
    • (1974) Eur. J. Biochem. , vol.43 , pp. 73-78
    • Hrkal, Z.1    Vodrazka, Z.2    Kalousek, I.3
  • 25
    • 0026666880 scopus 로고
    • Release of iron by human retinal pigment epithelial cells
    • Hunt, R.C., and Davis, A.A. (1992) Release of iron by human retinal pigment epithelial cells. J. Cell Physiol., 152:102-110.
    • (1992) J. Cell Physiol. , vol.152 , pp. 102-110
    • Hunt, R.C.1    Davis, A.A.2
  • 26
    • 0021166916 scopus 로고
    • Alterations in the transferrin receptor of human erythroleukemic cells after induction of hemoglobin synthesis
    • Hunt, R.C., Ruffin, R., and Yang, Y-S. (1984) Alterations in the transferrin receptor of human erythroleukemic cells after induction of hemoglobin synthesis. J. Biol. Chem., 259:9944-9952.
    • (1984) J. Biol. Chem. , vol.259 , pp. 9944-9952
    • Hunt, R.C.1    Ruffin, R.2    Yang, Y.-S.3
  • 27
    • 0024643741 scopus 로고
    • Transferrin receptors of the retinal pigment epithelium are associated with the cytoskeleton
    • Hunt, R.C., Dewey, A., and Davis, A.A. (1989) Transferrin receptors of the retinal pigment epithelium are associated with the cytoskeleton. J. Cell Sci., 92:655-666.
    • (1989) J. Cell Sci. , vol.92 , pp. 655-666
    • Hunt, R.C.1    Dewey, A.2    Davis, A.A.3
  • 28
    • 0024155024 scopus 로고
    • Autoxidative damage to the retina: Potential role in retinopathy of prematurity
    • Katz, M.L., and Robison, W.G. Jr. (1988) Autoxidative damage to the retina: Potential role in retinopathy of prematurity. Birth Defects: Orig. Artic. Ser., 24:237-248.
    • (1988) Birth Defects: Orig. Artic. Ser. , vol.24 , pp. 237-248
    • Katz, M.L.1    Robison Jr., W.G.2
  • 29
    • 0024497521 scopus 로고
    • Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite
    • Keyse, S.M., and Tyrrell, R.M. (1989) Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite. Proc. Natl. Acad. Sci. U.S.A., 86:99-103.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 99-103
    • Keyse, S.M.1    Tyrrell, R.M.2
  • 30
    • 0026520625 scopus 로고
    • Heme oxygenase: Expression in human retina and modulation by stress agents in a human retinoblastoma cell model system
    • Kutty, G., Hayden, B., Osawa, Y., Wiggert, B., Chader, G.J., and Kutty, R.K. (1992) Heme oxygenase: Expression in human retina and modulation by stress agents in a human retinoblastoma cell model system. Curr. Eye Res., 11:153-160.
    • (1992) Curr. Eye Res. , vol.11 , pp. 153-160
    • Kutty, G.1    Hayden, B.2    Osawa, Y.3    Wiggert, B.4    Chader, G.J.5    Kutty, R.K.6
  • 31
    • 0028256192 scopus 로고
    • Increased expression of heme-oxygenase-1 in human retinal pigment epithelial cells by transforming growth factor beta
    • Kutty, R.K , Nagineni, C.N., Kutty, G., Hooks, J.J., Chader, G.J., and Wiggert, B. (1994) Increased expression of heme-oxygenase-1 in human retinal pigment epithelial cells by transforming growth factor beta. J. Cell. Physiol., 159:371-378.
    • (1994) J. Cell. Physiol. , vol.159 , pp. 371-378
    • Kutty, R.K.1    Nagineni, C.N.2    Kutty, G.3    Hooks, J.J.4    Chader, G.J.5    Wiggert, B.6
  • 32
    • 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, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 0028033748 scopus 로고
    • Transferrin, one of the major vitreous proteins, is produced within the eye
    • Laicine, E.M., and Haddad, A. (1994) Transferrin, one of the major vitreous proteins, is produced within the eye. Exp. Eye Res., 59:441-446.
    • (1994) Exp. Eye Res. , vol.59 , pp. 441-446
    • Laicine, E.M.1    Haddad, A.2
  • 35
    • 0017198426 scopus 로고
    • The binding and transport of heme by hemopexin
    • Morgan, W.T. (1976) The binding and transport of heme by hemopexin. Ann. Clin. Res., 8(Suppl. 17):223-232.
    • (1976) Ann. Clin. Res. , vol.8 , Issue.17 SUPPL. , pp. 223-232
    • Morgan, W.T.1
  • 36
    • 0015524032 scopus 로고
    • Interactions of porphyrins with rabbit hemopexin
    • Morgan, W.T., and Muller-Eberhard, U. (1972) Interactions of porphyrins with rabbit hemopexin. J. Biol. Chem., 247:7181-7187.
    • (1972) J. Biol. Chem. , vol.247 , pp. 7181-7187
    • Morgan, W.T.1    Muller-Eberhard, U.2
  • 37
    • 0017845559 scopus 로고
    • Magnetic and natural circular dichroism of metalloporphryrin complexes of human and rabbit hemopexin
    • Morgan, W.T., and Vickery, L.E. (1978) Magnetic and natural circular dichroism of metalloporphryrin complexes of human and rabbit hemopexin J. Biol. Chem., 253:2940-2945.
    • (1978) J. Biol. Chem. , vol.253 , pp. 2940-2945
    • Morgan, W.T.1    Vickery, L.E.2
  • 38
    • 0027391548 scopus 로고
    • Evidence for the localization of haemopexin immunoreactivity in neurones in the human brain
    • Morris, C.M., Candy, J.M., Edwardson, J.A., Bloxham, C.A., and Smith, A. (1993) Evidence for the localization of haemopexin immunoreactivity in neurones in the human brain. Neurosci. Lett., 149:141-144.
    • (1993) Neurosci. Lett. , vol.149 , pp. 141-144
    • Morris, C.M.1    Candy, J.M.2    Edwardson, J.A.3    Bloxham, C.A.4    Smith, A.5
  • 39
    • 0024562602 scopus 로고
    • The hemopexin receptor on the cell surface of human polymorphonuclear leukocytes
    • Okazaki, H., Taketani, S., Kohno, H., Tokunaga, R., and Kobayashi, Y. (1989) The hemopexin receptor on the cell surface of human polymorphonuclear leukocytes. Cell Struct. Funct., 14:129-140.
    • (1989) Cell Struct. Funct. , vol.14 , pp. 129-140
    • Okazaki, H.1    Taketani, S.2    Kohno, H.3    Tokunaga, R.4    Kobayashi, Y.5
  • 40
    • 0015257895 scopus 로고
    • Peroxidase diffusion in the normal and laser-coagulated primate retina
    • Peyman, G.A., and Bok, D. (1972) Peroxidase diffusion in the normal and laser-coagulated primate retina. Invest Ophthalmol. Vis. Sci., 11:35-45.
    • (1972) Invest Ophthalmol. Vis. Sci. , vol.11 , pp. 35-45
    • Peyman, G.A.1    Bok, D.2
  • 41
    • 0028884225 scopus 로고
    • Mechanism of metallothionein gene regulation by heme-hemopexin
    • Ren, Y., and Smith, A. (1995) Mechanism of metallothionein gene regulation by heme-hemopexin. J. Biol. Chem., 270:23988-23995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23988-23995
    • Ren, Y.1    Smith, A.2
  • 42
    • 84969001783 scopus 로고
    • The attractions of proteins for small molecules and ions
    • Scatchard, G. (1949) The attractions of proteins for small molecules and ions. Ann., N.Y. Acad. Sci., 51:660-672.
    • (1949) Ann., N.Y. Acad. Sci. , vol.51 , pp. 660-672
    • Scatchard, G.1
  • 43
    • 0001718051 scopus 로고
    • Transport of tetrapyrroles: Mechanisms and biological and regulatory consequences
    • H.A. Dailey, ed., McGraw Hill, New York
    • Smith, A. (1990) Transport of tetrapyrroles: Mechanisms and biological and regulatory consequences. In: Biosynthesis of Heme and Chlorophylls, H.A. Dailey, ed., McGraw Hill, New York, pp. 435-490.
    • (1990) Biosynthesis of Heme and Chlorophylls , pp. 435-490
    • Smith, A.1
  • 44
    • 0024208707 scopus 로고
    • Expression of the haemopexin-transport system in cultured mouse hepatoma cells. Links between haemopexin and iron metabolism
    • Smith, A., and Ledford, B. (1988) Expression of the haemopexin-transport system in cultured mouse hepatoma cells. Links between haemopexin and iron metabolism. Biochem. J., 256:941-950.
    • (1988) Biochem. J. , vol.256 , pp. 941-950
    • Smith, A.1    Ledford, B.2
  • 45
    • 0018082852 scopus 로고
    • Transport of heme by hemopexin to the liver: Evidence for receptor-mediated uptake
    • Smith, A., and Morgan, W.T. (1978) Transport of heme by hemopexin to the liver: Evidence for receptor-mediated uptake. Biochem. Biophys. Res. Commun., 84:151-157.
    • (1978) Biochem. Biophys. Res. Commun. , vol.84 , pp. 151-157
    • Smith, A.1    Morgan, W.T.2
  • 46
    • 0018634705 scopus 로고
    • Haem transport to the liver by haemopexin. Receptor-mediated recycling of the protein
    • Smith, A., and Morgan, W.T. (1979) Haem transport to the liver by haemopexin. Receptor-mediated recycling of the protein. Biochem. J., 182:47-54.
    • (1979) Biochem. J. , vol.182 , pp. 47-54
    • Smith, A.1    Morgan, W.T.2
  • 47
    • 0021127103 scopus 로고
    • Hemopexin-mediated heme uptake by liver. Characterization of the interaction of heme-hemopexin with isolated rabbit liver plasma membranes
    • Smith, A., and Morgan, W.T. (1984) Hemopexin-mediated heme uptake by liver. Characterization of the interaction of heme-hemopexin with isolated rabbit liver plasma membranes. J. Biol. Chem., 259:12049-12053.
    • (1984) J. Biol. Chem. , vol.259 , pp. 12049-12053
    • Smith, A.1    Morgan, W.T.2
  • 48
    • 0023950446 scopus 로고
    • Importance of ligand-induced conformational changes in hemopexin for receptor-mediated heme transport
    • Smith, A., Tatum, F.M., Muster, P., Burch, M.K., and Morgan, W.T. (1988) Importance of ligand-induced conformational changes in hemopexin for receptor-mediated heme transport. J. Biol. Chem., 263:5224-5229.
    • (1988) J. Biol. Chem. , vol.263 , pp. 5224-5229
    • Smith, A.1    Tatum, F.M.2    Muster, P.3    Burch, M.K.4    Morgan, W.T.5
  • 49
    • 0025764614 scopus 로고
    • The murine haemopexin receptor. Evidence that the haemopexin binding site resides on a 20 kDa subunit and that receptor recycling is regulated by protein kinase C
    • Smith, A., Farooqui, S.M., and Morgan, W.T. (1991) The murine haemopexin receptor. Evidence that the haemopexin binding site resides on a 20 kDa subunit and that receptor recycling is regulated by protein kinase C. Biochem. J., 276:417-425.
    • (1991) Biochem. J. , vol.276 , pp. 417-425
    • Smith, A.1    Farooqui, S.M.2    Morgan, W.T.3
  • 50
    • 0027406116 scopus 로고
    • Regulation of heme oxygenase and metallothionein gene expression by the heme analogs, cobalt-, and tin-protoporphyrin
    • Smith, A., Alam, J., Escriba, P.V., and Morgan, W.T. (1993) Regulation of heme oxygenase and metallothionein gene expression by the heme analogs, cobalt-, and tin-protoporphyrin. J. Biol. Chem., 268:7365-7371.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7365-7371
    • Smith, A.1    Alam, J.2    Escriba, P.V.3    Morgan, W.T.4
  • 51
    • 0026448548 scopus 로고
    • Relationships between thermotolerance, oxidative stress responses and induction of stress proteins in human tumour cell lines
    • Steels, E.L., Watson, K., and Parsons, P.G. (1992) Relationships between thermotolerance, oxidative stress responses and induction of stress proteins in human tumour cell lines. Biochem. Pharmacol., 44:2123-2129.
    • (1992) Biochem. Pharmacol. , vol.44 , pp. 2123-2129
    • Steels, E.L.1    Watson, K.2    Parsons, P.G.3
  • 52
  • 53
    • 0027996689 scopus 로고
    • The testicular iron shuttle: A "nurse" function of the Sertoli cells
    • Sylvester, S.R., and Griswold, M.D. (1994) The testicular iron shuttle: A "nurse" function of the Sertoli cells. J. Androl., 15:381-385.
    • (1994) J. Androl. , vol.15 , pp. 381-385
    • Sylvester, S.R.1    Griswold, M.D.2
  • 54
    • 0023221126 scopus 로고
    • Cell surface receptor for hemopexin in human leukemia HL60 cells. Specific binding, affinity labeling and fate of heme
    • Taketani, S., Kohno, H., and Tokunaga, R. (1987a) Cell surface receptor for hemopexin in human leukemia HL60 cells. Specific binding, affinity labeling and fate of heme. J. Biol. Chem., 262:4639-4643.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4639-4643
    • Taketani, S.1    Kohno, H.2    Tokunaga, R.3
  • 55
    • 0023189468 scopus 로고
    • Isolation of the hemopexin receptor from human placenta
    • Taketani, S., Kohno, H., Naitoh, Y., and Tokunaga, R. (1987b) Isolation of the hemopexin receptor from human placenta. J. Biol. Chem , 262:8668-8671.
    • (1987) J. Biol. Chem , vol.262 , pp. 8668-8671
    • Taketani, S.1    Kohno, H.2    Naitoh, Y.3    Tokunaga, R.4
  • 56
    • 0025108856 scopus 로고
    • Hemopexin-dependent down-regulation of expression of the human transferrin receptor
    • Taketani, S., Kohno, H., Sawamura, T., and Tokunaga, R. (1990) Hemopexin-dependent down-regulation of expression of the human transferrin receptor. J. Biol. Chem., 265:13981-13985.
    • (1990) J. Biol. Chem. , vol.265 , pp. 13981-13985
    • Taketani, S.1    Kohno, H.2    Sawamura, T.3    Tokunaga, R.4
  • 57
    • 0025354340 scopus 로고
    • Developmental changes in transferrin and iron uptake by the brain in the rat
    • Taylor, E.M., and Morgan, E.H. (1990) Developmental changes in transferrin and iron uptake by the brain in the rat. Dev. Brain Res., 55:35-42.
    • (1990) Dev. Brain Res. , vol.55 , pp. 35-42
    • Taylor, E.M.1    Morgan, E.H.2
  • 58
    • 0000366607 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels onto nitrocellulose sheets: Procedure and some applications
    • Towbin, H., Staehelin, T., and Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels onto nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U.S.A., 81:4683-4687.
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.81 , pp. 4683-4687
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 59
    • 0025301493 scopus 로고
    • Tau fraction of transferrin is present in human aqueous humor and is not unique to cerebrospinal fluid
    • Tripathi, R.C., Millard, C.B., Tripathi, B.J., and Noronha, A. (1990) Tau fraction of transferrin is present in human aqueous humor and is not unique to cerebrospinal fluid. Exp. Eye Res., 50:541-547.
    • (1990) Exp. Eye Res. , vol.50 , pp. 541-547
    • Tripathi, R.C.1    Millard, C.B.2    Tripathi, B.J.3    Noronha, A.4
  • 60
    • 0023255877 scopus 로고
    • Iron metabolism in Be Wo chorion carcinoma cells: Transferrin-mediated uptake and release of iron
    • Van der Ende, A., Du Maine, A., Simmons, C.F., Schwartz, A.L., and Strous, G.J. (1987) Iron metabolism in Be Wo chorion carcinoma cells: Transferrin-mediated uptake and release of iron. J. Biol. Chem., 262:8910-8916.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8910-8916
    • Van Der Ende, A.1    Du Maine, A.2    Simmons, C.F.3    Schwartz, A.L.4    Strous, G.J.5
  • 62
    • 0017665882 scopus 로고
    • The use of wheat-germ lectin-Sepharose for the purification of human haemopexin
    • Vretblad, P., and Hjorth, R. (1977) The use of wheat-germ lectin-Sepharose for the purification of human haemopexin. Biochem. J., 167:759-764.
    • (1977) Biochem. J. , vol.167 , pp. 759-764
    • Vretblad, P.1    Hjorth, R.2
  • 64
    • 0028157860 scopus 로고
    • Identification and characterization of an iron-regulated hemopexin receptor in Haemophilus influenzae type b
    • Wong, J.C., Holland, J., Parsons, T., Smith, A., and Williams, P. (1994) Identification and characterization of an iron-regulated hemopexin receptor in Haemophilus influenzae type b. Infect. Immunol., 62:48-59.
    • (1994) Infect. Immunol. , vol.62 , pp. 48-59
    • Wong, J.C.1    Holland, J.2    Parsons, T.3    Smith, A.4    Williams, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.