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Volumn 57, Issue 9, 2005, Pages 645-650

Copper brain homeostasis: Role of amyloid precursor protein and prion protein

Author keywords

APP; Copper; Copper binding domain; Metal homeostasis; Prion protein

Indexed keywords

AMYLOID PRECURSOR PROTEIN; CHELATING AGENT; COPPER; COPPER CHLORIDE; COPPER ZINC CHELATOR; PENICILLAMINE; PRION PROTEIN; UNCLASSIFIED DRUG;

EID: 27444445191     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1080/15216540500264620     Document Type: Review
Times cited : (26)

References (41)
  • 1
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy, J., and Selkoe, D. J. (2002) The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics. Science 297, 353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 2
    • 0033844944 scopus 로고    scopus 로고
    • Characterization of copper interactions with Alzheimer amyloid β peptides: Identification of an attomolar-affinity copper binding site on amyloid β 1-42
    • Atwood, C. S., Scarpa, R. C., Huang, X., Moir, R. D., Jones, W. D., Fairlie, D. P., Tanzi, R. E., and Bush, A. I. (2000) Characterization of copper interactions with Alzheimer amyloid β peptides: Identification of an attomolar-affinity copper binding site on amyloid β 1-42. J. Neurochem. 75, 1219-1233.
    • (2000) J. Neurochem. , vol.75 , pp. 1219-1233
    • Atwood, C.S.1    Scarpa, R.C.2    Huang, X.3    Moir, R.D.4    Jones, W.D.5    Fairlie, D.P.6    Tanzi, R.E.7    Bush, A.I.8
  • 4
    • 0029935396 scopus 로고    scopus 로고
    • The amyloid precursor protein of Alzheimer's disease in the reduction of copper (II) to copper (I)
    • Multhaup, G., Schlicksupp, A., Hesse, L., Beher, D., Ruppert, T., Masters, C. L., and Beyreuther, K. (1996) The amyloid precursor protein of Alzheimer's disease in the reduction of copper (II) to copper (I). Science 271, 1406-1409.
    • (1996) Science , vol.271 , pp. 1406-1409
    • Multhaup, G.1    Schlicksupp, A.2    Hesse, L.3    Beher, D.4    Ruppert, T.5    Masters, C.L.6    Beyreuther, K.7
  • 5
    • 0345035452 scopus 로고    scopus 로고
    • Cysteine 144 is a key residue in the copper reduction by the β-amyloid precursor protein
    • Ruiz, F. H., Gonzalez, M., Bodini, M., Opazo, C., and Inestrosa, N. C. (1999) Cysteine 144 is a key residue in the copper reduction by the β-amyloid precursor protein. J. Neurochem. 73, 1288-1292.
    • (1999) J. Neurochem. , vol.73 , pp. 1288-1292
    • Ruiz, F.H.1    Gonzalez, M.2    Bodini, M.3    Opazo, C.4    Inestrosa, N.C.5
  • 7
    • 0033516677 scopus 로고    scopus 로고
    • Alterations of 3-nitrotyrosine concentration in the cerebrospinal fluid during aging and in patients with Alzheimer's disease
    • Tohgi, H., Abe, T., Yamazaki, K., Murata, T., Ishizaki, E., and Isobe, C. (1999) Alterations of 3-nitrotyrosine concentration in the cerebrospinal fluid during aging and in patients with Alzheimer's disease. Neurosci. Lett. 269, 52-54.
    • (1999) Neurosci. Lett. , vol.269 , pp. 52-54
    • Tohgi, H.1    Abe, T.2    Yamazaki, K.3    Murata, T.4    Ishizaki, E.5    Isobe, C.6
  • 8
    • 0026648872 scopus 로고
    • Axonal sprouting induced in the sciatic nerve by the amyloid precursor protein (APP) and other antiproteases
    • Alvarez, J., Moreno, R. D., Llanos, O., Inestrosa, N. C., Brandan, E., Colby, T., and Esch, F. S. (1992) Axonal sprouting induced in the sciatic nerve by the amyloid precursor protein (APP) and other antiproteases. Neurosci. Lett. 144, 130-134.
    • (1992) Neurosci. Lett. , vol.144 , pp. 130-134
    • Alvarez, J.1    Moreno, R.D.2    Llanos, O.3    Inestrosa, N.C.4    Brandan, E.5    Colby, T.6    Esch, F.S.7
  • 9
    • 0027478347 scopus 로고
    • Evidence for excitoprotective and intraneuronal calcium-regulating roles for secreted forms of the β-amyloid precursor protein
    • Mattson, M. P., Cheng, B., Culwell, A. R., Esch, F. S., Lieberburg, I., and Rydel, R. E. (1993) Evidence for excitoprotective and intraneuronal calcium-regulating roles for secreted forms of the β-amyloid precursor protein. Neuron 10, 243-254.
    • (1993) Neuron , vol.10 , pp. 243-254
    • Mattson, M.P.1    Cheng, B.2    Culwell, A.R.3    Esch, F.S.4    Lieberburg, I.5    Rydel, R.E.6
  • 10
    • 0037355742 scopus 로고    scopus 로고
    • Copper reduction by copper binding proteins and its relation to neurodegenerative diseases
    • Opazo, C., Barria, M. I., Ruiz, F. H., and Inestrosa, N. C. (2003) Copper reduction by copper binding proteins and its relation to neurodegenerative diseases. Biometals 16, 91-98.
    • (2003) Biometals , vol.16 , pp. 91-98
    • Opazo, C.1    Barria, M.I.2    Ruiz, F.H.3    Inestrosa, N.C.4
  • 11
    • 0034643831 scopus 로고    scopus 로고
    • Metal binding modes of Alzheimer's amyloid β-peptide in insoluble aggregates and soluble complexes
    • Miura, T., Suzuki, K., Kohata, N., and Takeuchi, H. (2000) Metal binding modes of Alzheimer's amyloid β-peptide in insoluble aggregates and soluble complexes. Biochemistry 39, 7024-7031.
    • (2000) Biochemistry , vol.39 , pp. 7024-7031
    • Miura, T.1    Suzuki, K.2    Kohata, N.3    Takeuchi, H.4
  • 15
    • 0037096251 scopus 로고    scopus 로고
    • A novel function of monomeric amyloid β-protein sarving as an antioxidant molecule against metal induced oxidative damage
    • Zou, K., Gong, J. S., Yanagisawa, K., and Michikawa, M. (2002) A novel function of monomeric amyloid β-protein sarving as an antioxidant molecule against metal induced oxidative damage. J. Neurosci. 22, 4833-4841.
    • (2002) J. Neurosci. , vol.22 , pp. 4833-4841
    • Zou, K.1    Gong, J.S.2    Yanagisawa, K.3    Michikawa, M.4
  • 16
    • 0141702360 scopus 로고    scopus 로고
    • Trace amounts of copper in water induce β-amyloid plaques and learning deficits in a rabbit model of Alzheimer's disease
    • Sparks, D. L., and Schreurs, B. G. (2003) Trace amounts of copper in water induce β-amyloid plaques and learning deficits in a rabbit model of Alzheimer's disease. Proc. Natl. Acad. Sci. USA 100, 11065-11069.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 11065-11069
    • Sparks, D.L.1    Schreurs, B.G.2
  • 21
    • 0025991466 scopus 로고
    • The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive
    • Caughey, B., and Raymond, G. J. (1991) The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive. J. Biol. Chem. 266, 18217-18223.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18217-18223
    • Caughey, B.1    Raymond, G.J.2
  • 23
    • 0023663071 scopus 로고
    • Scrapie prion protein contains a phosphatidylinositol glycolipid
    • Stahl, N., Borchelt, D. R., Hsiao, K., and Prusiner, S. B. (1987) Scrapie prion protein contains a phosphatidylinositol glycolipid. Cell 51, 229-240.
    • (1987) Cell , vol.51 , pp. 229-240
    • Stahl, N.1    Borchelt, D.R.2    Hsiao, K.3    Prusiner, S.B.4
  • 25
    • 0033515029 scopus 로고    scopus 로고
    • Copper binding to the prion protein: Structural implications of four identical cooperative binding sites
    • Viles, J. H., Cohen, F. E., Prusiner, S. B., Goodin, D. B., Wright, P. E., and Dyson, H. J. (1999) Copper binding to the prion protein: Structural implications of four identical cooperative binding sites. Proc. Natl. Acad. Sci. USA 96, 2042-2047.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 2042-2047
    • Viles, J.H.1    Cohen, F.E.2    Prusiner, S.B.3    Goodin, D.B.4    Wright, P.E.5    Dyson, H.J.6
  • 27
    • 0034673578 scopus 로고    scopus 로고
    • The N-terminal tandem repeat region of human prion protein reduces copper: Role of tryptophan residues
    • Ruiz, F. H., Silva, E., and Inestrosa, N. C. (2000) The N-terminal tandem repeat region of human prion protein reduces copper: Role of tryptophan residues. Biochem. Biophys. Res. Commun. 269, 491-495.
    • (2000) Biochem. Biophys. Res. Commun. , vol.269 , pp. 491-495
    • Ruiz, F.H.1    Silva, E.2    Inestrosa, N.C.3
  • 28
    • 20544450600 scopus 로고    scopus 로고
    • Copper reduction by the octapeptide repeat region of prion protein: PH dependence and implications in cellular copper uptake
    • Miura, T., Sasaki, S., Toyama, A., and Takeuchi, H. (2005) Copper reduction by the octapeptide repeat region of prion protein: pH dependence and implications in cellular copper uptake. Biochemistry 44, 8712-8720.
    • (2005) Biochemistry , vol.44 , pp. 8712-8720
    • Miura, T.1    Sasaki, S.2    Toyama, A.3    Takeuchi, H.4
  • 29
  • 30
    • 0032509499 scopus 로고    scopus 로고
    • Copper stimulates endocytosis of the prion protein
    • Pauly, P. C., and Harris, D. A. (1998) Copper stimulates endocytosis of the prion protein. J. Biol. Chem. 273, 33107-33110.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33107-33110
    • Pauly, P.C.1    Harris, D.A.2
  • 31
    • 0037715143 scopus 로고    scopus 로고
    • Expression of prion protein increases cellular copper binding and antioxidant enzyme activities but not copper delivery
    • Rachidi, W., Vilette, D., Guiraud, P., Arlotto, M., Riondel, J., Laude, H., Lehmann, S., and Favier, A. (2003) Expression of prion protein increases cellular copper binding and antioxidant enzyme activities but not copper delivery. J. Biol. Chem. 278, 9064-9072.
    • (2003) J. Biol. Chem. , vol.278 , pp. 9064-9072
    • Rachidi, W.1    Vilette, D.2    Guiraud, P.3    Arlotto, M.4    Riondel, J.5    Laude, H.6    Lehmann, S.7    Favier, A.8
  • 33
    • 3542999252 scopus 로고    scopus 로고
    • 2+ coordination by His96 and His111 induces β-sheet formation in the unstructured amyloidogenic region of the prion protein
    • 2+ coordination by His96 and His111 induces β-sheet formation in the unstructured amyloidogenic region of the prion protein. J. Biol. Chem. 279, 32018-32027.
    • (2004) J. Biol. Chem. , vol.279 , pp. 32018-32027
    • Jones, C.E.1    Abdelraheim, S.R.2    Brown, D.R.3    Viles, J.H.4
  • 34
    • 0035815738 scopus 로고    scopus 로고
    • Copper converts the cellular prion protein into a protease-resistant species that is distinct from the scrapie isoform
    • Quaglio, E., Chiesa, R., and Harris, D. A. (2001) Copper converts the cellular prion protein into a protease-resistant species that is distinct from the scrapie isoform. J. Biol. Chem. 276, 11432-11438.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11432-11438
    • Quaglio, E.1    Chiesa, R.2    Harris, D.A.3
  • 35
    • 2642553049 scopus 로고    scopus 로고
    • Copper induces increased β-sheet content in the scrapie-susceptible ovine prion protein PrPVRQ compared with the resistant allelic variant PrPARR
    • Wong, E., Thackray, A. M., and Bujdoso, R. (2004) Copper induces increased β-sheet content in the scrapie-susceptible ovine prion protein PrPVRQ compared with the resistant allelic variant PrPARR. Biochem. J. 380, 273-282.
    • (2004) Biochem. J. , vol.380 , pp. 273-282
    • Wong, E.1    Thackray, A.M.2    Bujdoso, R.3
  • 38
    • 2942672188 scopus 로고    scopus 로고
    • Misfolding of the prion protein at the plasma membrane induces endocytosis, intracellular retention and degradation
    • Kiachopoulos, S., Heske, J., Tatzeit, J., and Winklhofer, K. F. (2004) Misfolding of the prion protein at the plasma membrane induces endocytosis, intracellular retention and degradation. Traffic 5, 426-436.
    • (2004) Traffic , vol.5 , pp. 426-436
    • Kiachopoulos, S.1    Heske, J.2    Tatzeit, J.3    Winklhofer, K.F.4
  • 39
    • 27444438077 scopus 로고    scopus 로고
    • Role of copper on prion diseases: Misfolding versus trafficking effects on prion protein
    • in press
    • Varela-Nallar, L., Gonzalez, A., and Inestrosa, N. C. (2005) Role of copper on prion diseases: Misfolding versus trafficking effects on prion protein. Curr. Pharm. Design (in press).
    • (2005) Curr. Pharm. Design
    • Varela-Nallar, L.1    Gonzalez, A.2    Inestrosa, N.C.3
  • 40
    • 0037195617 scopus 로고    scopus 로고
    • Conversion of PrP to a self-perpetuating PrPSc-like conformation in the cytosol
    • Ma, J., and Lindquist, S. (2002) Conversion of PrP to a self-perpetuating PrPSc-like conformation in the cytosol. Science 298, 1785-1788.
    • (2002) Science , vol.298 , pp. 1785-1788
    • Ma, J.1    Lindquist, S.2
  • 41
    • 0345714734 scopus 로고    scopus 로고
    • Copper binding to PrPC may inhibit prion disease propagation
    • Hijazi, N., Shaked, Y., Rosenmann, H., Ben-Hur, T., and Gabizon, R. (2003) Copper binding to PrPC may inhibit prion disease propagation. Brain Res. 993, 192-200.
    • (2003) Brain Res. , vol.993 , pp. 192-200
    • Hijazi, N.1    Shaked, Y.2    Rosenmann, H.3    Ben-Hur, T.4    Gabizon, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.