메뉴 건너뛰기




Volumn 110, Issue SUPPL. 5, 2002, Pages 695-698

Molecular mechanism of copper transport in Wilson disease

Author keywords

ATP7B ZntA chimera; Copper binding; Copper trafficking; Copper transport; Copper ATPase; Nucleotide binding domain; P type ATPases; Phosphorylation domain; Wilson disease; Wilson disease gene

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; BINDING PROTEIN; CARRIER PROTEIN; COPPER; CYSTEINE; HEAVY METAL; NUCLEOTIDE BINDING PROTEIN; ZINC;

EID: 0036801448     PISSN: 00916765     EISSN: None     Source Type: Journal    
DOI: 10.1289/ehp.02110s5695     Document Type: Article
Times cited : (43)

References (54)
  • 1
    • 84963072124 scopus 로고
    • Progressive lenticular degeneration: A familial nervous disease associated with cirrhosis of the liver
    • Wilson SAK. Progressive lenticular degeneration: a familial nervous disease associated with cirrhosis of the liver. Brain 34:295-508 (1912).
    • (1912) Brain , vol.34 , pp. 295-508
    • Wilson, S.A.K.1
  • 2
    • 0029874633 scopus 로고    scopus 로고
    • Wilson disease: Genetic basis of copper toxicity and natural history
    • Schilsky ML. Wilson disease: genetic basis of copper toxicity and natural history. Semin Liver Dis 16:83-95 (1996).
    • (1996) Semin. Liver Dis , vol.16 , pp. 83-95
    • Schilsky, M.L.1
  • 3
    • 77049283245 scopus 로고
    • Penicillamine, a new oral therapy for Wilson disease
    • Wlashe JM. Penicillamine, a new oral therapy for Wilson disease. Am J med 21:487-495 (1956).
    • (1956) Am. J. Med , vol.21 , pp. 487-495
    • Walshe, J.M.1
  • 4
    • 0033429466 scopus 로고    scopus 로고
    • Penicillamine: The treatment of first choice for patients with Wilson's disease
    • Walshe JM. Penicillamine: the treatment of first choice for patients with Wilson's disease. Mov Disord 14:545-550 (1999).
    • (1999) Mov. Disord , vol.14 , pp. 545-550
    • Walshe, J.M.1
  • 5
    • 0020086199 scopus 로고
    • Treatment of Wilson's disease with trientine (triethylene tetramine) dihydrochloride. Lancet
    • Walshe JM. Treatment of Wilson's disease with trientine (triethylene tetramine) dihydrochloride. Lancet 1:643-647 (1982).
    • (1982) , vol.1 , pp. 643-647
    • Walshe, J.M.1
  • 6
    • 0023262532 scopus 로고
    • The use of trientine in preventing the effects of interrupting penicillamine therapy in Wilson's disease
    • Scheinberg, IH, Jaffe ME, Sternlieb I. The use of trientine in preventing the effects of interrupting penicillamine therapy in Wilson's disease. N. Engl J Med 317:209-213 (1987).
    • (1987) N. Engl. J. Med , vol.317 , pp. 209-213
    • Scheinberg, I.H.1    Jaffe, M.E.2    Sternlieb, I.3
  • 7
    • 0032192556 scopus 로고    scopus 로고
    • Zinc treatment of Wilson's disease
    • Hoogenraad TU. Zinc treatment of Wilson's disease. J Lab Clin Med 132:240-241 (1998).
    • (1998) J. Lab. Clin. Med , vol.132 , pp. 240-241
    • Hoogenraad, T.U.1
  • 9
    • 0023219833 scopus 로고
    • Treatment of Wilson's disease: In D-penicillamine we trust-what about zinc?
    • Lipsky MA, Gollan JL. Treatment of Wilson's disease: in D-penicillamine we trust-what about zinc? Hepatology 7:593-595 (1987).
    • (1987) Hepatology , vol.7 , pp. 593-595
    • Lipsky, M.A.1    Gollan, J.L.2
  • 10
    • 0027452091 scopus 로고
    • The Wilson disease gene is putative copper transporting P-type ATPase similar to the Menkes gene
    • Bull PC, Thomas GR, Rommens JM, Forbes JR, Cox DW. The Wilson disease gene is putative copper transporting P-type ATPase similar to the MEnkes gene. Nat Genet 5:327-337 (1993).
    • (1993) Nat. Genet , vol.5 , pp. 327-337
    • Bull, P.C.1    Thomas, G.R.2    Rommens, J.M.3    Forbes, J.R.4    Cox, D.W.5
  • 12
    • 0028040512 scopus 로고
    • Characterization of the Wilson disease gene encoding a P-type copper transporting ATPase: Genomic organization, alternative splicing, and structure/function predictions
    • Petrukhin K, Lutsenko S, Chernov I, Ross BM, Kaplan JH, Gilliam TC. Characterization of the Wilson disease gene encoding a P-type copper transporting ATPase: genomic organization, alternative splicing, and structure/function predictions. Hum Mol Genet 3:1647-1656 (1994).
    • (1994) Hum. Mol. Genet , vol.3 , pp. 1647-1656
    • Petrukhin, K.1    Lutsenko, S.2    Chernov, I.3    Ross, B.M.4    Kaplan, J.H.5    Gilliam, T.C.6
  • 13
    • 0030803730 scopus 로고    scopus 로고
    • Biochemical characterization of the Wilson disease protein and functional expression in the yeast Saccharomyces cerevisiae
    • Hung IH, Suzuki M, Yamaguchi Y, Yuan DS, Klausner RD, Gitlin JD. Biochemical characterization of the Wilson disease protein and functional expression in the yeast Saccharomyces cerevisiae. J Biol Chem 272:21461-21466 (1997).
    • (1997) J. Biol. Chem , vol.272 , pp. 21461-21466
    • Hung, I.H.1    Suzuki, M.2    Yamaguchi, Y.3    Yuan, D.S.4    Klausner, R.D.5    Gitlin, J.D.6
  • 14
    • 0031952914 scopus 로고    scopus 로고
    • Intracellular distribution of the Wilson's disease gene product (ATPase7B) after in vitro and in vivo exogenous expression in hepatocytes from the LEC rat, an animal model of Wilson's disease
    • Nagano K, Nakamura K, Urakami KI, Umeyama K, Uchiyama H, Koiwai K, Hattori S, Yamamoto T, Matsuda I, Endo F. Intracellular distribution of the Wilson's disease gene product (ATPase7B) after in vitro and in vivo exogenous expression in hepatocytes from the LEC rat, an animal model of Wilson's disease. Hepatology 27:799-807 (1998).
    • (1998) Hepatology , vol.27 , pp. 799-807
    • Nagano, K.1    Nakamura, K.2    Urakami, K.I.3    Umeyama, K.4    Uchiyama, H.5    Koiwai, K.6    Hattori, S.7    Yamamoto, T.8    Matsuda, I.9    Endo, F.10
  • 17
    • 0031475157 scopus 로고    scopus 로고
    • The zntA gene of Escherichia coli encodes a Zn(II)-translocating P-type ATPase
    • Rensing C, Mitra B, Rosen BP. The zntA gene of Escherichia coli encodes a Zn(II)-translocating P-type ATPase. Proc Natl Acad Sci USA 94:14326-14331 (1997).
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14326-14331
    • Rensing, C.1    Mitra, B.2    Rosen, B.P.3
  • 20
    • 0027446365 scopus 로고
    • Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper-transporting ATPase
    • Vulpe C, Levinson B, Whitney S, Packman S, Gitschier J. Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper-transporting ATPase. Nat Genet 3:7-13 (1993).
    • (1993) Nat. Genet , vol.3 , pp. 7-13
    • Vulpe, C.1    Levinson, B.2    Whitney, S.3    Packman, S.4    Gitschier, J.5
  • 24
    • 0035395798 scopus 로고    scopus 로고
    • Structure-function analysis of purified Enterococcus hirae CopB copper ATPase: Effect of Menkes/Wilson disease mutation homologues
    • Bissig KD, Wunderli-Ye H, Duda PW, Solioz M. Structure-function analysis of purified Enterococcus hirae CopB copper ATPase: effect of Menkes/Wilson disease mutation homologues. Biochem J 357:217-223 (2001).
    • (2001) Biochem. J , vol.357 , pp. 217-223
    • Bissig, K.D.1    Wunderli-Ye, H.2    Duda, P.W.3    Solioz, M.4
  • 27
    • 0032995679 scopus 로고    scopus 로고
    • Biliary excretion of copper in LEC rat after introduction of copper transporting P-type ATPase, ATP7B
    • Terad AK, Aiba N, Yang XL, Iida M, Nakai M, Miura N, Sugiyama T. Biliary excretion of copper in LEC rat after introduction of copper transporting P-type ATPase, ATP7B. FEBS Lett 448:53-56 (1999).
    • (1999) FEBS Lett , vol.448 , pp. 53-56
    • Terada, A.K.1    Aiba, N.2    Yang, X.L.3    Iida, M.4    Nakai, M.5    Miura, N.6    Sugiyama, T.7
  • 28
    • 0033862878 scopus 로고    scopus 로고
    • Copper-induced apical trafficking of ATP7B in polarized hepatoma cells provides a mechanism for biliary copper excretion
    • Roelofsen H, Wolters H, Van Luyn MJ, Miura N, Kuipers F, Vonk RJ. Copper-induced apical trafficking of ATP7B in polarized hepatoma cells provides a mechanism for biliary copper excretion. Gastroenterology 119:782-793 (2000).
    • (2000) Gastroenterology , vol.119 , pp. 782-793
    • Roelofsen, H.1    Wolters, H.2    Van Luyn, M.J.3    Miura, N.4    Kuipers, F.5    Vonk, R.J.6
  • 29
    • 0033617198 scopus 로고    scopus 로고
    • Role of the copper-binding domain in the copper transport function of ATP7B, the P-type TPase defective in Wilson disease
    • Forbes JR, Hsi G, Cox DW. Role of the copper-binding domain in the copper transport function of ATP7B, the P-type TPase defective in Wilson disease. J Biol Chem 274:12408-12413 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 12408-12413
    • Forbes, J.R.1    Hsi, G.2    Cox, D.W.3
  • 30
    • 0033574576 scopus 로고    scopus 로고
    • The role of GMXCXXC metal binding sites in the copper-induced redistribution of the Menkes protein
    • Strausak D, La Fontaine S, Hill J, Firth SD, Lockhart PJ, Mercer JF. The role of GMXCXXC metal binding sites in the copper-induced redistribution of the Menkes protein. J Biol Chem 274:11170-11177 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 11170-11177
    • Strausak, D.1    La Fontaine, S.2    Hill, J.3    Firth, S.D.4    Lockhart, P.J.5    Mercer, J.F.6
  • 31
    • 0031730641 scopus 로고    scopus 로고
    • A C-terminal di-leucine is required for localization of the Menkes protein in the trans-Golgi network
    • Petris MJ, Camakaris J, Greenough M, LaFontaine S, Mercer JF. A C-terminal di-leucine is required for localization of the Menkes protein in the trans-Golgi network. Hum Mol Genet 7:2063-2071 (1998).
    • (1998) Hum. Mol. Genet , vol.7 , pp. 2063-2071
    • Petris, M.J.1    Camakaris, J.2    Greenough, M.3    LaFontaine, S.4    Mercer, J.F.5
  • 32
    • 0032981423 scopus 로고    scopus 로고
    • Identification of a di-leucine motif within the C terminus domain of the Menkes disease protein that mediates endocytosis from the plasma membrane
    • Francis MJ, Jones EE, Levy ER, Martin RL, Ponnambalam S, Monaco AP. Identification of a di-leucine motif within the C terminus domain of the Menkes disease protein that mediates endocytosis from the plasma membrane. J Cell Sci 112:1721-1732 (1999).
    • (1999) J. Cell Sci , vol.112 , pp. 1721-1732
    • Francis, M.J.1    Jones, E.E.2    Levy, E.R.3    Martin, R.L.4    Ponnambalam, S.5    Monaco, A.P.6
  • 33
    • 0031455381 scopus 로고    scopus 로고
    • Expression, purification, and metal binding properties of the N-terminal domain from the Wilson disease putative copper-transporting ATPase (ATP7B)
    • DiDonato M, Narindrasorasak S, Forbes JR, Cox DW, Sarkar B. Expression, purification, and metal binding properties of the N-terminal domain from the Wilson disease putative copper-transporting ATPase (ATP7B). J Biol Chem 272:33279-33282 (1997).
    • (1997) J. Biol. Chem , vol.272 , pp. 33279-33282
    • DiDonato, M.1    Narindrasorasak, S.2    Forbes, J.R.3    Cox, D.W.4    Sarkar, B.5
  • 34
    • 0034700982 scopus 로고    scopus 로고
    • Copper-induced conformational changes in the N-terminal domain of the Wilson disease copper-transporting ATPase
    • DiDonato M, Hsu HF, Narindrasorasak S, Que L Jr, Sarkar B. Copper-induced conformational changes in the N-terminal domain of the Wilson disease copper-transporting ATPase. Biochemistry 39:1890-1896 (2000).
    • (2000) Biochemistry , vol.39 , pp. 1890-1896
    • DiDonato, M.1    Hsu, H.F.2    Narindrasorasak, S.3    Que L., Jr.4    Sarkar, B.5
  • 35
    • 0032583440 scopus 로고    scopus 로고
    • The Menkes disease protein binds copper via novel 2-coordinate Cu(I)-cysteinates in the N-terminal domain
    • Ralle M, Copper MJ, Lutsenko S, Blackburn NJ. The Menkes disease protein binds copper via novel 2-coordinate Cu(I)-cysteinates in the N-terminal domain. J Am Chem Soc 120:13525-13526 (1998).
    • (1998) J. Am. Chem. Soc , vol.120 , pp. 13525-13526
    • Ralle, M.1    Copper, M.J.2    Lutsenko, S.3    Blackburn, N.J.4
  • 36
    • 0037133926 scopus 로고    scopus 로고
    • Zinc binding to the N-terminal domain of the Wilson disease copper-transporting ATPase: Implications for in vivo metal ion mediated regulation of ATPase activity
    • DiDonato M, Zhang J, Que L Jr, Sarkar B. Zinc binding to the N-terminal domain of the Wilson disease copper-transporting ATPase: implications for in vivo metal ion mediated regulation of ATPase activity. J Biol Chem 277:13409-13414 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 13409-13414
    • DiDonato, M.1    Zhang, J.2    Que L., Jr.3    Sarkar, B.4
  • 37
    • 0035798632 scopus 로고    scopus 로고
    • Functional analysis of chimeric proteins of the Wilson Cu(I)-ATPase (ATP7B) and ZntA, a PB(II)Zn(II)/Cd(II)-ATPase from Escherichia coli
    • Hou Z-J, Narindrasorasak S, Bhushan B, Sarkar B, Mitra B. Functional analysis of chimeric proteins of the Wilson Cu(I)-ATPase (ATP7B) and ZntA, a PB(II)Zn(II)/Cd(II)-ATPase from Escherichia coli. J Biol Chem 276:40858-40863 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 40858-40863
    • Hou, Z.-J.1    Narindrasorasak, S.2    Bhushan, B.3    Sarkar, B.4    Mitra, B.5
  • 38
    • 0344132580 scopus 로고    scopus 로고
    • Expression and mutagenesis of ZntA, a zinc-transporting P-type ATPase from Escherichia coli
    • Okkeri J, Haltia T. Expression and mutagenesis of ZntA, a zinc-transporting P-type ATPase from Escherichia coli. Biochemistry 38:14109-14116 (1999).
    • (1999) Biochemistry , vol.38 , pp. 14109-14116
    • Okkeri, J.1    Haltia, T.2
  • 39
    • 0034621834 scopus 로고    scopus 로고
    • Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution
    • Toyoshima C, Nakasako M, Nomura H, Ogawa H. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution. Nature 405:647-655 (2000).
    • (2000) Nature , vol.405 , pp. 647-655
    • Toyoshima, C.1    Nakasako, M.2    Nomura, H.3    Ogawa, H.4
  • 41
    • 0033952734 scopus 로고    scopus 로고
    • Crystallization, structure and dynamics of the proton-translocating P-type ATPase
    • Scarborough GA. Crystallization, structure and dynamics of the proton-translocating P-type ATPase. J Exp Biol 203(pt 1):147-154 (2000).
    • (2000) J. Exp. Biol , vol.203 , Issue.PART 1 , pp. 147-154
    • Scarborough, G.A.1
  • 42
    • 0035875154 scopus 로고    scopus 로고
    • Structural similarities of Na,K-ATPase and SERCA, the Ca(2+)-ATPase of the sarcoplasmic reticulum
    • Sweadner KJ, Donnet C. Structural similarities of Na,K-ATPase and SERCA, the Ca(2+)-ATPase of the sarcoplasmic reticulum. Biochem J 356:685-704 (2001).
    • (2001) Biochem. J , vol.356 , pp. 685-704
    • Sweadner, K.J.1    Donnet, C.2
  • 43
    • 0034695687 scopus 로고    scopus 로고
    • Residues of the fourth transmemebrane segments of the Na,K-ATpase and the gastric H,K-ATPase contribute to cation selectivity
    • Mense M, Dunbar LA, Blostein R, Caplan MJ. Residues of the fourth transmemebrane segments of the Na,K-ATpase and the gastric H,K-ATPase contribute to cation selectivity. J Biol Chem 275:1749-1756 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 1749-1756
    • Mense, M.1    Dunbar, L.A.2    Blostein, R.3    Caplan, M.J.4
  • 44
    • 0032471911 scopus 로고    scopus 로고
    • Functional characterization of missence mutations in ATP7B: Wilson disease mutation or normal variant?
    • Forbes JR, Cox DW. Functional characterization of missence mutations in ATP7B: Wilson disease mutation or normal variant? AM J Hum Genet 63:1663-1674 (1998).
    • (1998) AM. J. Hum. Genet , vol.63 , pp. 1663-1674
    • Forbes, J.R.1    Cox, D.W.2
  • 47
    • 0035875164 scopus 로고    scopus 로고
    • What the structure of a calcium pump tell us about its mechanism
    • Lee AG, East JM. What the structure of a calcium pump tell us about its mechanism. Biochem J 356:665-683 (2001).
    • (2001) Biochem. J , vol.356 , pp. 665-683
    • Lee, A.G.1    East, J.M.2
  • 48
    • 0031916833 scopus 로고    scopus 로고
    • HAH1 is a copper-binding protein with distinct amino acid residues mediating cooper homeostasis and antioxidant defence
    • Hung IH, Casareno RL, Labesse G, Mathews FS, Gitlin JD. HAH1 is a copper-binding protein with distinct amino acid residues mediating cooper homeostasis and antioxidant defence. J Biol Chem 273:1749-1754 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 1749-1754
    • Hung, I.H.1    Casareno, R.L.2    Labesse, G.3    Mathews, F.S.4    Gitlin, J.D.5
  • 49
    • 0033214908 scopus 로고    scopus 로고
    • Characterization of the interaction between the Wilson and Menkes disease proteins and the cytoplasmic copper chaperone, HAH1p
    • Larin D, Mekios C, Das K, Ross B, Yang AS, Gilliam TC. Characterization of the interaction between the Wilson and Menkes disease proteins and the cytoplasmic copper chaperone, HAH1p. J Biol Chem 274:28497-28504 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 28497-28504
    • Larin, D.1    Mekios, C.2    Das, K.3    Ross, B.4    Yang, A.S.5    Gilliam, T.C.6
  • 50
    • 0033539566 scopus 로고    scopus 로고
    • Interaction of the copper chaperone HAH1 with the Wilson disease protein is essential for copper homeostasis
    • Hamza I, Schaefer M, Klomp LW, Gitlin JD. Interaction of the copper chaperone HAH1 with the Wilson disease protein is essential for copper homeostasis. Proc Natl Acad Sci USA 96:13363-13368 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13363-13368
    • Hamza, I.1    Schaefer, M.2    Klomp, L.W.3    Gitlin, J.D.4
  • 51
    • 0034913058 scopus 로고    scopus 로고
    • Function, structure, and mechanism of intracellular copper trafficking proteins. Annu
    • Huffman DL, O'Halloran TV. Function, structure, and mechanism of intracellular copper trafficking proteins. Annu Rev Biochem 70:677-701 (2001).
    • (2001) Rev. Biochem , vol.70 , pp. 677-701
    • Huffman, D.L.1    O'Halloran, T.V.2
  • 54
    • 0035910261 scopus 로고    scopus 로고
    • The Lys1010-Lys1325 fragment of the Wilson's disease protein binds nucleotides and interacts with the N-terminal domain of this protein in a copper-dependent manner
    • Tsivkovskii R, MacArthur BC, Lutsenko S. The Lys1010-Lys1325 fragment of the Wilson's disease protein binds nucleotides and interacts with the N-terminal domain of this protein in a copper-dependent manner. J Biol Chem 276:2234-2242 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 2234-2242
    • Tsivkovskii, R.1    MacArthur, B.C.2    Lutsenko, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.