메뉴 건너뛰기




Volumn 380, Issue 5, 2008, Pages 900-916

Cobalt and the Iron Acquisition Pathway: Competition towards Interaction with Receptor 1

Author keywords

endocytosis; HFE; kinetics; protein protein interactions

Indexed keywords

CD71 ANTIGEN; COBALT; IRON; TRANSFERRIN;

EID: 45849117939     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.05.045     Document Type: Article
Times cited : (27)

References (45)
  • 3
    • 45849088873 scopus 로고    scopus 로고
    • Zuccola, H. J. (1992). The crystal structure of monoferric human serum transferrin, Ph.D. Thesis, Georgia Institute of Technology, Ann Arbor.
    • Zuccola, H. J. (1992). The crystal structure of monoferric human serum transferrin, Ph.D. Thesis, Georgia Institute of Technology, Ann Arbor.
  • 4
    • 33747641642 scopus 로고    scopus 로고
    • The crystal structure of iron-free human serum transferrin provides insight into inter-lobe communication and receptor binding
    • Wally J., Halbrooks P.J., Vonrhein C., Rould M.A., Everse S.J., Mason A.B., and Buchanan S.K. The crystal structure of iron-free human serum transferrin provides insight into inter-lobe communication and receptor binding. J. Biol. Chem. (2006)
    • (2006) J. Biol. Chem.
    • Wally, J.1    Halbrooks, P.J.2    Vonrhein, C.3    Rould, M.A.4    Everse, S.J.5    Mason, A.B.6    Buchanan, S.K.7
  • 5
    • 0037794014 scopus 로고    scopus 로고
    • Structural and functional consequences of binding site mutations in transferrin: crystal structures of the Asp63Glu and Arg124Ala mutants of the N-lobe of human transferrin
    • Baker H.M., He Q.Y., Briggs S.K., Mason A.B., and Baker E.N. Structural and functional consequences of binding site mutations in transferrin: crystal structures of the Asp63Glu and Arg124Ala mutants of the N-lobe of human transferrin. Biochemistry 42 (2003) 7084-7089
    • (2003) Biochemistry , vol.42 , pp. 7084-7089
    • Baker, H.M.1    He, Q.Y.2    Briggs, S.K.3    Mason, A.B.4    Baker, E.N.5
  • 6
    • 0000241799 scopus 로고
    • pH and the recycling of transferrin during receptor-mediated endocytosis
    • Dautry-Varsat A., Ciechanover A., and Lodish H.F. pH and the recycling of transferrin during receptor-mediated endocytosis. Proc. Natl Acad. Sci. USA 80 (1983) 2258-2262
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , pp. 2258-2262
    • Dautry-Varsat, A.1    Ciechanover, A.2    Lodish, H.F.3
  • 8
    • 0023899377 scopus 로고
    • A high yield purification of the human transferrin receptor and properties of its major extracellular fragment
    • Turkewitz A.P., Amatruda J.F., Borhani D., Harrison S.C., and Schwartz A.L. A high yield purification of the human transferrin receptor and properties of its major extracellular fragment. J. Biol. Chem. 263 (1988) 8318-8325
    • (1988) J. Biol. Chem. , vol.263 , pp. 8318-8325
    • Turkewitz, A.P.1    Amatruda, J.F.2    Borhani, D.3    Harrison, S.C.4    Schwartz, A.L.5
  • 9
    • 1342264310 scopus 로고    scopus 로고
    • Structure of the human transferrin receptor-transferrin complex
    • Cheng Y., Zak O., Aisen P., Harrison S.C., and Walz T. Structure of the human transferrin receptor-transferrin complex. Cell 116 (2004) 565-576
    • (2004) Cell , vol.116 , pp. 565-576
    • Cheng, Y.1    Zak, O.2    Aisen, P.3    Harrison, S.C.4    Walz, T.5
  • 10
    • 0033550262 scopus 로고    scopus 로고
    • Transferrin is a mixed chelate-protein ternary complex involved in the mechanism of iron uptake by serum-transferrin in vitro?
    • Pakdaman R., Abdallah F.B., and El Hage Chahine J.M. Transferrin is a mixed chelate-protein ternary complex involved in the mechanism of iron uptake by serum-transferrin in vitro?. J. Mol. Biol. 293 (1999) 1273-1284
    • (1999) J. Mol. Biol. , vol.293 , pp. 1273-1284
    • Pakdaman, R.1    Abdallah, F.B.2    El Hage Chahine, J.M.3
  • 12
    • 33745020924 scopus 로고    scopus 로고
    • The mechanism of iron release from the transferrin-receptor 1 adduct
    • Hemadi M., Ha-Duong N.T., and El Hage Chahine J.M. The mechanism of iron release from the transferrin-receptor 1 adduct. J. Mol. Biol. 358 (2006) 1125-1136
    • (2006) J. Mol. Biol. , vol.358 , pp. 1125-1136
    • Hemadi, M.1    Ha-Duong, N.T.2    El Hage Chahine, J.M.3
  • 13
    • 0001231645 scopus 로고    scopus 로고
    • Transferrin as a metal ion mediator
    • Sun H., Li H., and Sadler P.J. Transferrin as a metal ion mediator. Chem. Rev. 99 (1999) 2817-2842
    • (1999) Chem. Rev. , vol.99 , pp. 2817-2842
    • Sun, H.1    Li, H.2    Sadler, P.J.3
  • 14
    • 0014670580 scopus 로고
    • The chromium, manganese, and cobalt complexes of transferrin
    • Aisen P., Aasa R., and Redfield A.G. The chromium, manganese, and cobalt complexes of transferrin. J. Biol. Chem. 244 (1969) 4628-4633
    • (1969) J. Biol. Chem. , vol.244 , pp. 4628-4633
    • Aisen, P.1    Aasa, R.2    Redfield, A.G.3
  • 15
    • 39549102641 scopus 로고    scopus 로고
    • Reconsideration of serum Ti(IV) transport: albumin and transferrin trafficking of Ti(IV) and its complexes
    • Tinoco A.D., Eames E.V., and Valentine A.M. Reconsideration of serum Ti(IV) transport: albumin and transferrin trafficking of Ti(IV) and its complexes. J. Am. Chem. Soc. 130 (2008) 2262-2270
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 2262-2270
    • Tinoco, A.D.1    Eames, E.V.2    Valentine, A.M.3
  • 17
    • 2442657217 scopus 로고    scopus 로고
    • Mechanism for multiple ligand recognition by the human transferrin receptor
    • Giannetti A.M., Snow P.M., Zak O., and Bjorkman P.J. Mechanism for multiple ligand recognition by the human transferrin receptor. PLoS Biol. 1 (2003) E51
    • (2003) PLoS Biol. , vol.1
    • Giannetti, A.M.1    Snow, P.M.2    Zak, O.3    Bjorkman, P.J.4
  • 18
    • 2942554825 scopus 로고    scopus 로고
    • HFE and transferrin directly compete for transferrin receptor in solution and at the cell surface
    • Giannetti A.M., and Bjorkman P.J. HFE and transferrin directly compete for transferrin receptor in solution and at the cell surface. J. Biol. Chem. 279 (2004) 25866-25875
    • (2004) J. Biol. Chem. , vol.279 , pp. 25866-25875
    • Giannetti, A.M.1    Bjorkman, P.J.2
  • 20
    • 34250329981 scopus 로고    scopus 로고
    • Non platinum metal complexes as anti-cancer drugs
    • Ott I., and Gust R. Non platinum metal complexes as anti-cancer drugs. Arch. Pharm. (Weinheim) 340 (2007) 117-126
    • (2007) Arch. Pharm. (Weinheim) , vol.340 , pp. 117-126
    • Ott, I.1    Gust, R.2
  • 21
    • 33947254611 scopus 로고    scopus 로고
    • Use of isotopes in the diagnosis of hematopoietic disorders
    • Shreeve W.W. Use of isotopes in the diagnosis of hematopoietic disorders. Exp. Hematol. 35 (2007) 173-179
    • (2007) Exp. Hematol. , vol.35 , pp. 173-179
    • Shreeve, W.W.1
  • 22
  • 23
    • 0016140936 scopus 로고
    • 13C nuclear magnetic resonance study of the spatial relation of the metal- and anion-binding sites of human transferrin
    • 13C nuclear magnetic resonance study of the spatial relation of the metal- and anion-binding sites of human transferrin. J. Biol. Chem. 249 (1974) 5261-5264
    • (1974) J. Biol. Chem. , vol.249 , pp. 5261-5264
    • Harris, D.C.1    Gray, G.A.2    Aisen, P.3
  • 24
    • 0036026807 scopus 로고    scopus 로고
    • Complexes of cobalt(III) with phenolate-containing polydentate ligands and bovine serum apo-transferrin: towards creating spectroscopic models for cobalt(III)-tyrosinate interactions
    • Shongwe M.S., Al-Hatmi S.K., Marques H.M., Smith R., Nukada R., and Mikuriya M. Complexes of cobalt(III) with phenolate-containing polydentate ligands and bovine serum apo-transferrin: towards creating spectroscopic models for cobalt(III)-tyrosinate interactions. J. Chem. Soc. Dalton Trans. (2002) 4064-4069
    • (2002) J. Chem. Soc. Dalton Trans. , pp. 4064-4069
    • Shongwe, M.S.1    Al-Hatmi, S.K.2    Marques, H.M.3    Smith, R.4    Nukada, R.5    Mikuriya, M.6
  • 25
    • 0037452915 scopus 로고    scopus 로고
    • Aluminum exchange between citrate and human serum transferrin and interaction with transferrin receptor 1
    • Hemadi M., Miquel G., Kahn P.H., and El Hage Chahine J.M. Aluminum exchange between citrate and human serum transferrin and interaction with transferrin receptor 1. Biochemistry 42 (2003) 3120-3130
    • (2003) Biochemistry , vol.42 , pp. 3120-3130
    • Hemadi, M.1    Miquel, G.2    Kahn, P.H.3    El Hage Chahine, J.M.4
  • 26
    • 8744244433 scopus 로고    scopus 로고
    • Mechanism of formation of the complex between transferrin and bismuth, and interaction with transferrin receptor 1
    • Miquel G., Nekaa T., Kahn P.H., Hemadi M., and El Hage Chahine J.M. Mechanism of formation of the complex between transferrin and bismuth, and interaction with transferrin receptor 1. Biochemistry 43 (2004) 14722-14731
    • (2004) Biochemistry , vol.43 , pp. 14722-14731
    • Miquel, G.1    Nekaa, T.2    Kahn, P.H.3    Hemadi, M.4    El Hage Chahine, J.M.5
  • 31
    • 0005967181 scopus 로고
    • Kinetics and mechanism of aquation and formation reactions of carbonato complexes: VII. Acid-catalyzed aquation of carbonato(nitrilotriacetato)cobaltate(III) ion
    • Dasgupta T.P., and Harris G.M. Kinetics and mechanism of aquation and formation reactions of carbonato complexes: VII. Acid-catalyzed aquation of carbonato(nitrilotriacetato)cobaltate(III) ion. Inorg. Chem. 13 (1974) 1275-1281
    • (1974) Inorg. Chem. , vol.13 , pp. 1275-1281
    • Dasgupta, T.P.1    Harris, G.M.2
  • 32
    • 20444507925 scopus 로고    scopus 로고
    • Human serum transferrin cobalt complex: stability and cellular uptake of cobalt
    • Smith T.A. Human serum transferrin cobalt complex: stability and cellular uptake of cobalt. Bioorg. Med. Chem. 13 (2005) 4576-4579
    • (2005) Bioorg. Med. Chem. , vol.13 , pp. 4576-4579
    • Smith, T.A.1
  • 33
    • 0017100245 scopus 로고
    • The detection of four molecular forms of human transferrin during the iron binding process
    • Makey D.G., and Seal U.S. The detection of four molecular forms of human transferrin during the iron binding process. Biochim. Biophys. Acta 453 (1976) 250-256
    • (1976) Biochim. Biophys. Acta , vol.453 , pp. 250-256
    • Makey, D.G.1    Seal, U.S.2
  • 34
    • 0000514950 scopus 로고    scopus 로고
    • Apotransferrin proton dissociation and interactions with hydrogen carbonate in neutral media
    • Bellounis L., Pakdaman R., and El Hage Chahine J.M. Apotransferrin proton dissociation and interactions with hydrogen carbonate in neutral media. J. Phys. Org. Chem. 9 (1996) 111-118
    • (1996) J. Phys. Org. Chem. , vol.9 , pp. 111-118
    • Bellounis, L.1    Pakdaman, R.2    El Hage Chahine, J.M.3
  • 35
    • 0345487829 scopus 로고    scopus 로고
    • Transferrin, a mechanism for iron uptake from nitrilotriacetatoFe(III) in the presence of bicarbonate
    • El Hage Chahine J.M., and Pakdaman R. Transferrin, a mechanism for iron uptake from nitrilotriacetatoFe(III) in the presence of bicarbonate. J. Chim. Phys. 93 (1996) 283-299
    • (1996) J. Chim. Phys. , vol.93 , pp. 283-299
    • El Hage Chahine, J.M.1    Pakdaman, R.2
  • 36
    • 0016669917 scopus 로고
    • 3 + by transferrin. Implications for the interlocking sites hypothesis
    • 3 + by transferrin. Implications for the interlocking sites hypothesis. J. Biol. Chem. 250 (1975) 2182-2188
    • (1975) J. Biol. Chem. , vol.250 , pp. 2182-2188
    • Schlabach, M.R.1    Bates, G.W.2
  • 37
    • 37049075545 scopus 로고
    • The mechanism of iron transferrin interactions. Uptake of the iron nitrilotriacetic acid complex
    • El Hage Chahine J.M., and Fain D. The mechanism of iron transferrin interactions. Uptake of the iron nitrilotriacetic acid complex. J. Chem. Soc. Dalton Trans. (1993) 3137-3143
    • (1993) J. Chem. Soc. Dalton Trans. , pp. 3137-3143
    • El Hage Chahine, J.M.1    Fain, D.2
  • 38
    • 34547237579 scopus 로고    scopus 로고
    • Kinetics of formation and dissociation of aquocobalt(III) complexes with some carboxylic acids in acid perchlorate solution
    • Davies G. Kinetics of formation and dissociation of aquocobalt(III) complexes with some carboxylic acids in acid perchlorate solution. J. Phys. Chem. B 111 (2007) 6955-6961
    • (2007) J. Phys. Chem. B , vol.111 , pp. 6955-6961
    • Davies, G.1
  • 39
    • 4244056182 scopus 로고
    • Kinetics and mechanism of aquation and formation reactions of carbonato complexes: 14. Base-catalyzed carbonato ring opening of carbonato (β,β′,β″-triaminotriethylamine) cobalt(III) perchlorate and spontaneous decarboxylation of aquobicarbonato (β,B′,B″-triaminotriethylamine) cobalt(III)
    • Dasgupta T.P., and Harris G.M. Kinetics and mechanism of aquation and formation reactions of carbonato complexes: 14. Base-catalyzed carbonato ring opening of carbonato (β,β′,β″-triaminotriethylamine) cobalt(III) perchlorate and spontaneous decarboxylation of aquobicarbonato (β,B′,B″-triaminotriethylamine) cobalt(III). Inorg. Chem. 17 (1978) 3123-3127
    • (1978) Inorg. Chem. , vol.17 , pp. 3123-3127
    • Dasgupta, T.P.1    Harris, G.M.2
  • 40
    • 0029007802 scopus 로고
    • Transferrin, a mechanism for iron release
    • El Hage Chahine J.M., and Pakdaman R. Transferrin, a mechanism for iron release. Eur. J. Biochem. 230 (1995) 1102-1110
    • (1995) Eur. J. Biochem. , vol.230 , pp. 1102-1110
    • El Hage Chahine, J.M.1    Pakdaman, R.2
  • 41
    • 0034692904 scopus 로고    scopus 로고
    • Transferrins: iron release from lactoferrin
    • Bou Abdallah F., and El Hage Chahine J.M. Transferrins: iron release from lactoferrin. J. Mol. Biol. 303 (2000) 255-266
    • (2000) J. Mol. Biol. , vol.303 , pp. 255-266
    • Bou Abdallah, F.1    El Hage Chahine, J.M.2
  • 43
    • 0039778186 scopus 로고    scopus 로고
    • Interaction kinetics of tetramethylrhodamine transferrin with human transferrin receptor studied by fluorescence correlation spectroscopy
    • Schuler J., Frank J., Trier U., Schafer-Korting M., and Saenger W. Interaction kinetics of tetramethylrhodamine transferrin with human transferrin receptor studied by fluorescence correlation spectroscopy. Biochemistry 38 (1999) 8402-8408
    • (1999) Biochemistry , vol.38 , pp. 8402-8408
    • Schuler, J.1    Frank, J.2    Trier, U.3    Schafer-Korting, M.4    Saenger, W.5
  • 44
    • 0029078010 scopus 로고
    • Functional reconstitution of the human placental transferrin receptor into phospholipid bilayers leads to long tubular structures proceeding from the vesicle surface
    • Fuchs H., Gessner R., Tauber R., and Ghosh R. Functional reconstitution of the human placental transferrin receptor into phospholipid bilayers leads to long tubular structures proceeding from the vesicle surface. Biochemistry 34 (1995) 6196-6207
    • (1995) Biochemistry , vol.34 , pp. 6196-6207
    • Fuchs, H.1    Gessner, R.2    Tauber, R.3    Ghosh, R.4
  • 45
    • 0037018151 scopus 로고    scopus 로고
    • Transferrin receptor recycling in the absence of perinuclear recycling endosomes
    • Sheff D., Pelletier L., O'Connell C.B., Warren G., and Mellman I. Transferrin receptor recycling in the absence of perinuclear recycling endosomes. J. Cell Biol. 156 (2002) 797-804
    • (2002) J. Cell Biol. , vol.156 , pp. 797-804
    • Sheff, D.1    Pelletier, L.2    O'Connell, C.B.3    Warren, G.4    Mellman, I.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.