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Volumn 127, Issue 19, 2014, Pages 4279-4291

Moonlighting cell-surface GAPDH recruits apotransferrin to effect iron egress from mammalian cells

Author keywords

Apotransferrin; Ferroportin; GAPDH; Higher order multifunctional protein; Iron export; Receptor

Indexed keywords

APOTRANSFERRIN; CARRIER PROTEIN; DEFEROXAMINE; FERROPORTIN; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; HOLOTRANSFERRIN; IRON; UNCLASSIFIED DRUG; APOPROTEIN; FERRIC ION; FERROUS ION; TRANSFERRIN;

EID: 84911921884     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.154005     Document Type: Article
Times cited : (42)

References (55)
  • 1
    • 0034572933 scopus 로고    scopus 로고
    • Iron homeostasis: insights from genetics and animal models
    • Andrews, N. C. (2000). Iron homeostasis: insights from genetics and animal models. Nat. Rev. Genet. 1, 208-217.
    • (2000) Nat. Rev. Genet. , vol.1 , pp. 208-217
    • Andrews, N.C.1
  • 2
    • 77956052050 scopus 로고    scopus 로고
    • Lipid raft-dependent endocytosis: a new route for hepcidin-mediated regulation of ferroportin in macrophages
    • Auriac, A., Willemetz, A. and Canonne-Hergaux, F. (2010). Lipid raft-dependent endocytosis: a new route for hepcidin-mediated regulation of ferroportin in macrophages. Haematologica 95, 1269-1277.
    • (2010) Haematologica , vol.95 , pp. 1269-1277
    • Auriac, A.1    Willemetz, A.2    Canonne-Hergaux, F.3
  • 4
    • 34548324815 scopus 로고    scopus 로고
    • Differential expression of stress-inducible proteins in chronic hepatic iron overload
    • Brown, K. E., Broadhurst, K. A., Mathahs, M. M. and Weydert, J. (2007). Differential expression of stress-inducible proteins in chronic hepatic iron overload. Toxicol. Appl. Pharmacol. 223, 180-186.
    • (2007) Toxicol. Appl. Pharmacol. , vol.223 , pp. 180-186
    • Brown, K.E.1    Broadhurst, K.A.2    Mathahs, M.M.3    Weydert, J.4
  • 5
    • 0035128199 scopus 로고    scopus 로고
    • Iron deficiency and iron overload: effects of diet and genes
    • Burke, W., Imperatore, G. and Reyes, M. (2001). Iron deficiency and iron overload: effects of diet and genes. Proc. Nutr. Soc. 60, 73-80.
    • (2001) Proc. Nutr. Soc. , vol.60 , pp. 73-80
    • Burke, W.1    Imperatore, G.2    Reyes, M.3
  • 6
    • 33644810795 scopus 로고    scopus 로고
    • Comparative studies of duodenal and macrophage ferroportin proteins
    • Canonne-Hergaux, F., Donovan, A., Delaby, C.,Wang, H. J. and Gros, P. (2006). Comparative studies of duodenal and macrophage ferroportin proteins. Am. J. Physiol. 290, G156-G163.
    • (2006) Am. J. Physiol. , vol.290 , pp. G156-G163
    • Canonne-Hergaux, F.1    Donovan, A.2    Delaby, C.3    Wang, H.J.4    Gros, P.5
  • 8
    • 0034078845 scopus 로고    scopus 로고
    • Specific phosphorylated forms of glyceraldehyde 3-phosphate dehydrogenase associate with human parainfluenza virus type 3 and inhibit viral transcription in vitro
    • Choudhary, S., De, B. P. and Banerjee, A. K. (2000). Specific phosphorylated forms of glyceraldehyde 3-phosphate dehydrogenase associate with human parainfluenza virus type 3 and inhibit viral transcription in vitro. J. Virol. 74, 3634-3641.
    • (2000) J. Virol. , vol.74 , pp. 3634-3641
    • Choudhary, S.1    De, B.P.2    Banerjee, A.K.3
  • 9
    • 28444488323 scopus 로고    scopus 로고
    • Presence of the iron exporter ferroportin at the plasma membrane of macrophages is enhanced by iron loading and down-regulated by hepcidin
    • Delaby, C., Pilard, N., Gonçalves, A. S., Beaumont, C. and Canonne-Hergaux, F. (2005). Presence of the iron exporter ferroportin at the plasma membrane of macrophages is enhanced by iron loading and down-regulated by hepcidin. Blood 106, 3979-3984.
    • (2005) Blood , vol.106 , pp. 3979-3984
    • Delaby, C.1    Pilard, N.2    Gonçalves, A.S.3    Beaumont, C.4    Canonne-Hergaux, F.5
  • 12
    • 84856292277 scopus 로고    scopus 로고
    • Iron overload in human disease
    • Fleming, R. E. and Ponka, P. (2012). Iron overload in human disease. N. Engl. J. Med. 366, 348-359.
    • (2012) N. Engl. J. Med. , vol.366 , pp. 348-359
    • Fleming, R.E.1    Ponka, P.2
  • 13
    • 0035003106 scopus 로고    scopus 로고
    • Elevated iron status increases bacterial invasion and survival and alters cytokine/chemokine mRNA expression in Caco-2 human intestinal cells
    • Foster, S. L., Richardson, S. H. and Failla, M. L. (2001). Elevated iron status increases bacterial invasion and survival and alters cytokine/chemokine mRNA expression in Caco-2 human intestinal cells. J. Nutr. 131, 1452-1458.
    • (2001) J. Nutr. , vol.131 , pp. 1452-1458
    • Foster, S.L.1    Richardson, S.H.2    Failla, M.L.3
  • 15
    • 84885768132 scopus 로고    scopus 로고
    • Systemic iron homeostasis
    • Ganz, T. (2013). Systemic iron homeostasis. Physiol. Rev. 93, 1721-1741.
    • (2013) Physiol. Rev. , vol.93 , pp. 1721-1741
    • Ganz, T.1
  • 16
    • 0029123674 scopus 로고
    • Rapid plasmenylethanolamine-selective fusion of membrane bilayers catalyzed by an isoform of glyceraldehyde-3-phosphate dehydrogenase: discrimination between glycolytic and fusogenic roles of individual isoforms
    • Glaser, P. E. and Gross, R. W. (1995). Rapid plasmenylethanolamine-selective fusion of membrane bilayers catalyzed by an isoform of glyceraldehyde-3-phosphate dehydrogenase: discrimination between glycolytic and fusogenic roles of individual isoforms. Biochemistry 34, 12193-12203.
    • (1995) Biochemistry , vol.34 , pp. 12193-12203
    • Glaser, P.E.1    Gross, R.W.2
  • 17
    • 5444265929 scopus 로고    scopus 로고
    • Cholesterol sensitivity of detergent resistance: a rapid flow cytometric test for detecting constitutive or induced raft association of membrane proteins
    • Gombos, I., Bacsó, Z., Detre, C., Nagy, H., Goda, K., Andrásfalvy, M., Szabó, G. and Matkó, J. (2004). Cholesterol sensitivity of detergent resistance: a rapid flow cytometric test for detecting constitutive or induced raft association of membrane proteins. Cytometry 61A, 117-126.
    • (2004) Cytometry , vol.61 A , pp. 117-126
    • Gombos, I.1    Bacsó, Z.2    Detre, C.3    Nagy, H.4    Goda, K.5    Andrásfalvy, M.6    Szabó, G.7    Matkó, J.8
  • 19
    • 0029086607 scopus 로고
    • Ascorbate offsets the inhibitory effect of inositol phosphates on iron uptake and transport by Caco-2 cells
    • Han, O., Failla, M. L., Hill, A. D., Morris, E. R. and Smith, J. C., Jr (1995). Ascorbate offsets the inhibitory effect of inositol phosphates on iron uptake and transport by Caco-2 cells. Proc. Soc. Exp. Biol. Med. 210, 50-56.
    • (1995) Proc. Soc. Exp. Biol. Med. , vol.210 , pp. 50-56
    • Han, O.1    Failla, M.L.2    Hill, A.D.3    Morris, E.R.4    Smith Jr, J.C.5
  • 20
    • 2042546096 scopus 로고    scopus 로고
    • Balancing acts: molecular control of mammalian iron metabolism
    • Hentze, M. W., Muckenthaler, M. U. and Andrews, N. C. (2004). Balancing acts: molecular control of mammalian iron metabolism. Cell 117, 285-297.
    • (2004) Cell , vol.117 , pp. 285-297
    • Hentze, M.W.1    Muckenthaler, M.U.2    Andrews, N.C.3
  • 21
    • 0034595856 scopus 로고    scopus 로고
    • Transferrin receptor 2-α supports cell growth both in iron-chelated cultured cells and in vivo
    • Kawabata, H., Germain, R. S., Vuong, P. T., Nakamaki, T., Said, J. W. and Koeffler, H. P. (2000). Transferrin receptor 2-α supports cell growth both in iron-chelated cultured cells and in vivo. J. Biol. Chem. 275, 16618-16625.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16618-16625
    • Kawabata, H.1    Germain, R.S.2    Vuong, P.T.3    Nakamaki, T.4    Said, J.W.5    Koeffler, H.P.6
  • 23
    • 13444252281 scopus 로고    scopus 로고
    • Iron release from macrophages after erythrophagocytosis is upregulated by ferroportin 1 overexpression and down-regulated by hepcidin
    • Knutson, M. D., Oukka, M., Koss, L. M., Aydemir, F. and Wessling-Resnick, M. (2005). Iron release from macrophages after erythrophagocytosis is upregulated by ferroportin 1 overexpression and down-regulated by hepcidin. Proc. Natl. Acad. Sci. USA 102, 1324-1328.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 1324-1328
    • Knutson, M.D.1    Oukka, M.2    Koss, L.M.3    Aydemir, F.4    Wessling-Resnick, M.5
  • 24
    • 0023876497 scopus 로고
    • Iron metabolism in the erythrophagocytosing Kupffer cell
    • Kondo, H., Saito, K., Grasso, J. P. and Aisen, P. (1988). Iron metabolism in the erythrophagocytosing Kupffer cell. Hepatology 8, 32-38.
    • (1988) Hepatology , vol.8 , pp. 32-38
    • Kondo, H.1    Saito, K.2    Grasso, J.P.3    Aisen, P.4
  • 25
    • 54549092697 scopus 로고    scopus 로고
    • Iron metabolism in the mononuclear phagocyte system
    • Kong, W., Duan, X., Shi, Z. and Chang, Y. (2008). Iron metabolism in the mononuclear phagocyte system. Progr. Nat. Sci. 18, 1197-1202.
    • (2008) Progr. Nat. Sci. , vol.18 , pp. 1197-1202
    • Kong, W.1    Duan, X.2    Shi, Z.3    Chang, Y.4
  • 26
    • 83555162529 scopus 로고    scopus 로고
    • Characterization of glyceraldehyde-3-phosphate dehydrogenase as a novel transferrin receptor
    • Kumar, S., Sheokand, N., Mhadeshwar, M. A., Raje, C. I. and Raje, M. (2012). Characterization of glyceraldehyde-3-phosphate dehydrogenase as a novel transferrin receptor. Int. J. Biochem. Cell Biol. 44, 189-199.
    • (2012) Int. J. Biochem. Cell Biol. , vol.44 , pp. 189-199
    • Kumar, S.1    Sheokand, N.2    Mhadeshwar, M.A.3    Raje, C.I.4    Raje, M.5
  • 27
    • 34948834723 scopus 로고    scopus 로고
    • Increased steady-state levels of CUGBP1 in myotonic dystrophy 1 are due to PKCmediated hyperphosphorylation
    • Kuyumcu-Martinez, N. M., Wang, G.-S. and Cooper, T. A. (2007). Increased steady-state levels of CUGBP1 in myotonic dystrophy 1 are due to PKCmediated hyperphosphorylation. Mol. Cell 28, 68-78.
    • (2007) Mol. Cell , vol.28 , pp. 68-78
    • Kuyumcu-Martinez, N.M.1    Wang, G.-S.2    Cooper, T.A.3
  • 28
    • 84884534252 scopus 로고    scopus 로고
    • Structure-function analysis of the human ferroportin iron exporter (SLC40A1): effect of hemochromatosis type 4 disease mutations and identification of critical residues
    • Le Gac, G., Ka, C., Joubrel, R., Gourlaouen, I., Lehn, P., Mornon, J. P., Férec, C. and Callebaut, I. (2013). Structure-function analysis of the human ferroportin iron exporter (SLC40A1): effect of hemochromatosis type 4 disease mutations and identification of critical residues. Hum. Mutat. 34, 1371-1380.
    • (2013) Hum. Mutat. , vol.34 , pp. 1371-1380
    • Le Gac, G.1    Ka, C.2    Joubrel, R.3    Gourlaouen, I.4    Lehn, P.5    Mornon, J.P.6    Férec, C.7    Callebaut, I.8
  • 32
    • 0031824078 scopus 로고    scopus 로고
    • Receptormediated recognition and uptake of iron from human transferrin by Staphylococcus aureus and Staphylococcus epidermidis
    • Modun, B., Evans, R. W., Joannou, C. L. and Williams, P. (1998). Receptormediated recognition and uptake of iron from human transferrin by Staphylococcus aureus and Staphylococcus epidermidis. Infect. Immun. 66, 3591-3596.
    • (1998) Infect. Immun. , vol.66 , pp. 3591-3596
    • Modun, B.1    Evans, R.W.2    Joannou, C.L.3    Williams, P.4
  • 33
    • 0034193246 scopus 로고    scopus 로고
    • The staphylococcal transferrin receptor: a glycolytic enzyme with novel functions
    • Modun, B., Morrissey, J. and Williams, P. (2000). The staphylococcal transferrin receptor: a glycolytic enzyme with novel functions. Trends Microbiol. 8, 231-237.
    • (2000) Trends Microbiol. , vol.8 , pp. 231-237
    • Modun, B.1    Morrissey, J.2    Williams, P.3
  • 34
    • 0020401560 scopus 로고
    • Uptake of transferrin by rat peritoneal macrophages
    • Nishisato, T. and Aisen, P. (1982). Uptake of transferrin by rat peritoneal macrophages. Br. J. Haematol. 52, 631-640.
    • (1982) Br. J. Haematol. , vol.52 , pp. 631-640
    • Nishisato, T.1    Aisen, P.2
  • 35
    • 0024289343 scopus 로고
    • Effect of enzymatic methylation of yeast iso-1-cytochrome c on its isoelectric point
    • Park, K. S., Frost, B. F., Shin, S., Park, I. K., Kim, S. and Paik, W. K. (1988). Effect of enzymatic methylation of yeast iso-1-cytochrome c on its isoelectric point. Arch. Biochem. Biophys. 267, 195-204.
    • (1988) Arch. Biochem. Biophys. , vol.267 , pp. 195-204
    • Park, K.S.1    Frost, B.F.2    Shin, S.3    Park, I.K.4    Kim, S.5    Paik, W.K.6
  • 37
    • 0028838037 scopus 로고
    • The effect of iron status on glyceraldehyde 3-phosphate dehydrogenase expression in rat liver
    • Quail, E. A. and Yeoh, G. C. (1995). The effect of iron status on glyceraldehyde 3-phosphate dehydrogenase expression in rat liver. FEBS Lett. 359, 126-128.
    • (1995) FEBS Lett. , vol.359 , pp. 126-128
    • Quail, E.A.1    Yeoh, G.C.2
  • 38
    • 34047254111 scopus 로고    scopus 로고
    • The macrophage cell surface glyceraldehyde-3-phosphate dehydrogenase is a novel transferrin receptor
    • Raje, C. I., Kumar, S., Harle, A., Nanda, J. S. and Raje, M. (2007). The macrophage cell surface glyceraldehyde-3-phosphate dehydrogenase is a novel transferrin receptor. J. Biol. Chem. 282, 3252-3261.
    • (2007) J. Biol. Chem. , vol.282 , pp. 3252-3261
    • Raje, C.I.1    Kumar, S.2    Harle, A.3    Nanda, J.S.4    Raje, M.5
  • 39
    • 0024290839 scopus 로고
    • Iron mobilization from cultured rat bone marrow macrophages
    • Rama, R., Sánchez, J. and Octave, J. N. (1988). Iron mobilization from cultured rat bone marrow macrophages. Biochim. Biophys. Acta 968, 51-58.
    • (1988) Biochim. Biophys. Acta , vol.968 , pp. 51-58
    • Rama, R.1    Sánchez, J.2    Octave, J.N.3
  • 41
    • 84861386961 scopus 로고    scopus 로고
    • The multifunctional glycolytic protein glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a novel macrophage lactoferrin receptor
    • Rawat, P., Kumar, S., Sheokand, N., Raje, C. I. and Raje, M. (2012). The multifunctional glycolytic protein glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a novel macrophage lactoferrin receptor. Biochem. Cell Biol. 90, 329-338.
    • (2012) Biochem. Cell Biol. , vol.90 , pp. 329-338
    • Rawat, P.1    Kumar, S.2    Sheokand, N.3    Raje, C.I.4    Raje, M.5
  • 42
    • 0022638812 scopus 로고
    • Interaction of transferrin with iron-loaded rat peritoneal macrophages
    • Saito, K., Nishisato, T., Grasso, J. A. and Aisen, P. (1986). Interaction of transferrin with iron-loaded rat peritoneal macrophages. Br. J. Haematol. 62, 275-286.
    • (1986) Br. J. Haematol. , vol.62 , pp. 275-286
    • Saito, K.1    Nishisato, T.2    Grasso, J.A.3    Aisen, P.4
  • 45
    • 39749099462 scopus 로고    scopus 로고
    • Strategy for comprehensive identification of post-translational modifications in cellular proteins, including low abundant modifications: application to glyceraldehyde-3-phosphate dehydrogenase
    • Seo, J., Jeong, J., Kim, Y. M., Hwang, N., Paek, E. and Lee, K.-J. (2008). Strategy for comprehensive identification of post-translational modifications in cellular proteins, including low abundant modifications: application to glyceraldehyde-3-phosphate dehydrogenase. J. Proteome Res. 7, 587-602.
    • (2008) J. Proteome Res. , vol.7 , pp. 587-602
    • Seo, J.1    Jeong, J.2    Kim, Y.M.3    Hwang, N.4    Paek, E.5    Lee, K.-J.6
  • 46
    • 84857374333 scopus 로고    scopus 로고
    • The long history of iron in the Universe and in health and disease
    • Sheftel, A. D., Mason, A. B. and Ponka, P. (2012). The long history of iron in the Universe and in health and disease. Biochim. Biophys. Acta 1820, 161-187.
    • (2012) Biochim. Biophys. Acta , vol.1820 , pp. 161-187
    • Sheftel, A.D.1    Mason, A.B.2    Ponka, P.3
  • 47
    • 84876161526 scopus 로고    scopus 로고
    • Secreted glyceraldehye-3-phosphate dehydrogenase is a multifunctional autocrine transferrin receptor for cellular iron acquisition
    • Sheokand, N., Kumar, S., Malhotra, H., Tillu, V., Raje, C. I. and Raje, M. (2013). Secreted glyceraldehye-3-phosphate dehydrogenase is a multifunctional autocrine transferrin receptor for cellular iron acquisition. Biochim. Biophys. Acta 1830, 3816-3827.
    • (2013) Biochim. Biophys. Acta , vol.1830 , pp. 3816-3827
    • Sheokand, N.1    Kumar, S.2    Malhotra, H.3    Tillu, V.4    Raje, C.I.5    Raje, M.6
  • 49
    • 79959226194 scopus 로고    scopus 로고
    • On the functional diversity of glyceraldehyde-3-phosphate dehydrogenase: biochemical mechanisms and regulatory control
    • Sirover, M. A. (2011). On the functional diversity of glyceraldehyde-3-phosphate dehydrogenase: biochemical mechanisms and regulatory control. Biochim. Biophys. Acta 1810, 741-751.
    • (2011) Biochim. Biophys. Acta , vol.1810 , pp. 741-751
    • Sirover, M.A.1
  • 50
    • 84861065569 scopus 로고    scopus 로고
    • Subcellular dynamics of multifunctional protein regulation: mechanisms of GAPDH intracellular translocation
    • Sirover, M. A. (2012). Subcellular dynamics of multifunctional protein regulation: mechanisms of GAPDH intracellular translocation. J. Cell. Biochem. 113, 2193-2200.
    • (2012) J. Cell. Biochem. , vol.113 , pp. 2193-2200
    • Sirover, M.A.1
  • 51
    • 0346461664 scopus 로고    scopus 로고
    • Ferroportin/IREG-1/MTP-1/SLC40A1 modulates the uptake of iron at the apical membrane of enterocytes
    • Thomas, C. and Oates, P. S. (2004). Ferroportin/IREG-1/MTP-1/SLC40A1 modulates the uptake of iron at the apical membrane of enterocytes. Gut 53, 44-49.
    • (2004) Gut , vol.53 , pp. 44-49
    • Thomas, C.1    Oates, P.S.2
  • 52
    • 14644389345 scopus 로고    scopus 로고
    • Iron deficiency: a concise review
    • Umbreit, J. (2005). Iron deficiency: a concise review. Am. J. Hematol. 78, 225-231.
    • (2005) Am. J. Hematol. , vol.78 , pp. 225-231
    • Umbreit, J.1
  • 53
    • 33644792074 scopus 로고    scopus 로고
    • Iron imports. III. Transfer of iron from the mucosa into circulation
    • Wessling-Resnick, M. (2006). Iron imports. III. Transfer of iron from the mucosa into circulation. Am. J. Physiol. 290, G1-G6.
    • (2006) Am. J. Physiol. , vol.290 , pp. G1-G6
    • Wessling-Resnick, M.1
  • 55
    • 79956259342 scopus 로고    scopus 로고
    • Analysis of nitroso-proteomes in normotensive and severe preeclamptic human placentas
    • Zhang, H.-h., Wang, Y.-p. and Chen, D.-b. (2011). Analysis of nitroso-proteomes in normotensive and severe preeclamptic human placentas. Biol. Reprod. 84, 966-975.
    • (2011) Biol. Reprod. , vol.84 , pp. 966-975
    • Zhang, H.-H.1    Wang, Y.-P.2    Chen, D.-B.3


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