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Autoxidation of Amyloid Precursor Protein and Formation of Reactive Oxygen Species

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Copper Transport and Its Disorders

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 448))

Abstract

The major component of Alzheimer’s disease (AD) amyloid, amyloid Aß protein is derived from the transmembrane amyloid precursor protein APR The pathogenic mechanism leading to AD is not well understood. However, the central role of APP has emerged from the identification of genes that cosegregate with the disease. All of the identified susceptibilty genes linked to Alzheimer’s disease appear to influence Aß amyloid formation (Beyreuther et al., 1996; Selkoe, 1996).

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References

  • Beem, K. M., Rich, W. E., and Rajagopalan, K. V. (1974). Total reconstitution of copper-zinc Superoxide dismutase. J. Biol. Chem. 249, 7298–7305.

    PubMed  CAS  Google Scholar 

  • Beher, D., Hesse, L., Masters, C. L., and Multhaup, G. (1996). Regulation of amyloid protein precursor (APP) binding to collagen and mapping of the binding sites on APP and collagen type I. J Biol Chem 271, 1613–1620.

    Article  PubMed  CAS  Google Scholar 

  • Beyreuther, K., Multhaup, G., and Masters, C. L. (1996). Alzheimer’s disease: genesis of amyloid. Ciba Found Symp 199, 119–127; discussion 127-31.

    PubMed  CAS  Google Scholar 

  • Breen, K. C. (1992). APP-collagen interaction is mediated by a heparin bridge mechanism. Mol. Chem. Neuropathol. 16, 109–121.

    Article  PubMed  CAS  Google Scholar 

  • Brown, R. H., Jr. (1995). Amyotrophic lateral sclerosis: recent insights from genetics and transgenic mice. Cell 80, 687–692.

    Article  PubMed  CAS  Google Scholar 

  • Bush, A. I., Multhaup, G., Moir, R. D., Williamson, T. G., Small, D. H., Rumble, B., Pollwein, P., Beyreuther, K., and Masters, C. L. (1993). A novel zinc(II) binding site modulates the function of the beta A4 amyloid protein precursor of Alzheimer’s disease. J. Biol. Chem. 268, 16109–16112.

    PubMed  CAS  Google Scholar 

  • Bush, A. I., Pettingell, W. H., Multhaup, G., dParadis, M., Vonsattel, J. P., Gusella, J. F., Beyreuther, K., Masters, C. L., and Tanzi, R. E. (1994). Rapid induction of Alzheimer A beta amyloid formation by zinc. Science 265, 1464–1467.

    Article  PubMed  CAS  Google Scholar 

  • Camakaris, J., Petris, M. J., Bailey, L., Shen, P. Y., Lockhart, P., Glover, T. W., Barcroft, C. L., Patton, J., and Mercer, J. F. B. (1995). Gene amplification of the Menkes (Mnk ATP7a) P Type ATPase gene of CHO cells is associated with copper resistance and enhanced copper efflux. Hum. Mol. Genet. 4, 2117–2123.

    Article  PubMed  CAS  Google Scholar 

  • Cork, L. C., Masters, C., Beyreuther, K., and Price, D. L. (1990). Development of senile plaques. Relationships of neuronal abnormalities and amyloid deposits. Am J Pathol 137, 1383–1392.

    PubMed  CAS  Google Scholar 

  • Culotta, V. C., Klomp, L. W., Strain, J., Casareno, R. L., Krems, B., and Gitlin, J. D. (1997). The copper chaperone for Superoxide dismutase. J Biol Chem 272, 23469–23472.

    Article  PubMed  CAS  Google Scholar 

  • Giaccone, G., Tagliavini, F., Linoli, G., Bouras, C., Frigerio, L., Frangione, B., and Bugiani, O. (1989). Down patients: extracellular preamyloid deposits precede neuritic degeneration and senile plaques. Neurosci Lett 97, 232–238.

    Article  PubMed  CAS  Google Scholar 

  • Gurney, M. E., Pu, H., Chiu, A. Y., Dal Canto, M. C., Polchow, C. Y, Alexander, D. D., Caliendo, J., Hentati, A., Kwon, Y. W., Deng, H. X., Chen, W., Zhai, P., Sufit, R. L., and Siddique, T. (1994). Motor neuron degeneration in mice that express a human Cu,Zn Superoxide dismutase mutation. Science 264, 1772–1775.

    Article  PubMed  CAS  Google Scholar 

  • Haass, C., Schlossmacher, M. G., Hung, A. Y, Vigo-Pelfrey, C., Mellon, A., Ostaszewski, B. L., Lieberburg, I., Koo, E. H., Schenk, D., Teplow, D. B., and Selkoe, D. J. (1992). Amyloid beta-peptide is produced by cul-tured cells during normal metabolism. Nature 359, 322–325.

    Article  PubMed  CAS  Google Scholar 

  • Harris, E. D. (1991). Copper transport: an overview. Proc. Soc. Exp. Biol. Med. 196, 130–140.

    PubMed  CAS  Google Scholar 

  • Hesse, L., Beher, D., Masters, C. L., and Multhaup, G. (1994). The beta A4 amyloid precursor protein binding to copper. FEBS. Lett. 349, 109–116.

    Article  PubMed  CAS  Google Scholar 

  • Hodgson, E. K., and Fridovich, I. (1975). The interaction of bovine erythrocyte Superoxide dismutase with hydrogen peroxide: inactivation of the enzyme. Biochemistry 14, 5294–5299.

    Article  PubMed  CAS  Google Scholar 

  • Hottinger, A. F., Fine, E. G., Gurney, M. E., Zurn, A. D., and Aebischer, P. (1997). The copper chelator d-penicil-lamine delays onset of disease and extends survival in a transgenic mouse model of familial amyotrophic lateral sclerosis. Eur J Neurosci 9, 1548–1551.

    Article  PubMed  CAS  Google Scholar 

  • Hung, I. H., Suzuki, M, Yamaguchi, Y, Yuan, D. S., Klausner, R. D., and Gitlin, J. D. (1997). Biochemical characterization of the wilson disease protein and functional expression in the yeast saccharomyces cerevisiae. J. Biol. Chem. 272, 21461–21466.

    Article  PubMed  CAS  Google Scholar 

  • Komiyama, Y, Murakami, T., Egawa, H., Okubo, S., Yasunaga, K., and Murata, K. (1992). Purification of factor XIa inhibitor from human platelets. Thromb Res 66, 397–408.

    Article  PubMed  CAS  Google Scholar 

  • Koo, E. H., and Squazzo, S. L. (1994). Evidence that production and release of amyloid beta-protein involves the endocytic pathway. J. Biol. Chem. 269, 17386–17389.

    PubMed  CAS  Google Scholar 

  • Kounnas, M. Z., Moir, R. D., Rebeck, G. W., Bush, A. L, Argraves, W. S., Tanzi, R. E., Hyman, B. T., and Strickland, D. K. (1995). LDL receptor-related protein, a multifunctional ApoE receptor, binds secreted beta-amyloid precursor protein and mediates its degradation. Cell 82, 331–340.

    Article  PubMed  CAS  Google Scholar 

  • Li, Q. X., Evin, G., Small, D. H., Multhaup, G., Beyreuther, K., and Masters, C. L. (1995). Proteolytic processing of Alzheimer’s disease beta A4 amyloid precursor protein in human platelets. J. Biol. Chem. 270, 14140–14147

    Article  PubMed  CAS  Google Scholar 

  • Linder, M. C., and Hazegh Azam, M. (1996). Copper biochemistry and molecular biology. Am. J. Clin. Nutr. 63, 797s–811s.

    PubMed  CAS  Google Scholar 

  • Milward, E. A., Papadopoulos, R., Fuller, S. J., Moir, R. D., Small, D., Beyreuther, K., and Masters, C. L. (1992). The amyloid protein precursor of Alzheimer’s disease is a mediator of the effects of nerve growth factor on neurite outgrowth. Neuron 9, 129–137.

    Article  PubMed  CAS  Google Scholar 

  • Miyata, M., and Smith, J. D. (1996). Apolipoprotein E allele-specific antioxidant activity and effects on cytotoxicity by oxidative insults and beta-amyloid peptides. Nat. Genet. 14, 55–61.

    Article  PubMed  CAS  Google Scholar 

  • Multhaup, G. (1994). Identification and regulation of the high affinity binding site of the Alzheimer’s disease amyloid protein precursor (APP) to glycosaminoglycans. Biochimie 76, 304–311.

    Article  PubMed  CAS  Google Scholar 

  • Multhaup, G., Bush, A. I., Pollwein, P., and Masters, C. L. (1994). Interaction between the zinc (II) and the heparin binding site of the Alzheimer’s disease beta A4 amyloid precursor protein (APP). FEBS Lett 355, 151–154.

    Article  PubMed  CAS  Google Scholar 

  • Multhaup, G., Ruppert, T., Schlicksupp, A., Hesse, L., Beher, D., Masters, C. L., and Beyreuther, K. (1997). Reactive oxygen species and Alzheimer’s disease. Biochem Pharmacol 54, 533–539.

    Article  PubMed  CAS  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • Narindrasorasak, S., Lowery, D. E., Altman, R. A., Gonzalez De Whitt, P. A., Greenberg, B. D., and Kisilevsky, R. (1992). Characterization of high affinity binding between laminin and Alzheimer’s disease amyloid precursor proteins. Lab. Invest. 67, 643–652.

    PubMed  CAS  Google Scholar 

  • Ooi, C. E., Rabinovich, E., Dancis, A., Bonifacino, J. S., and Klausner, R. D. (1996). Copper-dependent degradation of the Saccharomyces cerevisiae plasma membrane copper transporter Ctrlp in the apparent absence of endocytosis. EMBO J 15, 3515–3523.

    PubMed  CAS  Google Scholar 

  • Percival, S. S., and Harris, E. D. (1989). Ascorbate enhances copper transport from ceruloplasmin into human K562 cells. J. Nutr. 119, 779–784.

    PubMed  CAS  Google Scholar 

  • Pufahl, R. A., Singer, C. P., Peariso, K. L., Lin, S., Schmidt, P. J., Fahrni, C. J., Culotta, V. C., Penner-Hahn, J. E., and O’Halloran, T. V. (1997). Metal ion chaperone function of the soluble Cu(I) receptor atx 1. Science 278, 853–856.

    Article  PubMed  CAS  Google Scholar 

  • Roch, J. M., Shapiro, I. P., Sundsmo, M. P., Otero, D. A., Refolo, L. M, Robakis, N. K., and Saitoh, T. (1992). Bacterial expression, purification, and functional mapping of the amyloid beta/A4 protein precursor. J. Biol. Chem. 267, 2214–2221.

    PubMed  CAS  Google Scholar 

  • Saitoh, T., Sundsmo, M., Roch, J. M., Kimura, N., Cole, G., Schubert, D., Oltersdorf, T., and Schenk, D. B. (1989). Secreted form of amyloid beta protein precursor is involved in the growth regulation of fibroblasts. Cell 58, 615–622.

    Article  PubMed  CAS  Google Scholar 

  • Sato, K., Akaike, T., Kohno, M., Ando, M., and Maeda, H. (1992). Hydroxyl radical production by H2O2 plus Cu,Zn-superoxide dismutase reflects the activity of free copper released from the oxidatively damaged enzyme. J Biol Chem 267, 25371–25377.

    PubMed  CAS  Google Scholar 

  • Selkoe, D. J. (1996). Amyloid beta-protein and the genetics of Alzheimer’s disease. J Biol Chem 271, 18295–18298.

    PubMed  CAS  Google Scholar 

  • Shivers, B. D., Hilbich, C., Multhaup, G., Salbaum, M., Beyreuther, K., and Seeburg, P. H. (1988). Alzheimer’s disease amyloidogenic glycoprotein: expression pattern in rat brain suggests a role in cell contact. Embo J 7, 1365–1370.

    PubMed  CAS  Google Scholar 

  • Simons, M., Ikonen, E., Tienari, P. J., Cidarregui, A., Monning, U., Beyreuther, K., and Dotti, C. G. (1995). Intracellular routing of human amyloid protein precursor: Axonal delivery followed by transport to the dendrites. J. Neurosci. Res. 41, 121–128.

    Article  PubMed  CAS  Google Scholar 

  • Sisodia, S. S., Koo, E. H., Beyreuther, K., Unterbeck, A., and Price, D. L. (1990). Evidence that beta-amyloid protein in Alzheimer’s disease is not derived by normal processing. Science 248, 492–495.

    Article  PubMed  CAS  Google Scholar 

  • Small, D. H., Nurcombe, V., Reed, G., Clarris, H., Moir, R., Beyreuther, K., and Masters, C. L. (1994). Aheparinbinding domain in the amyloid protein precursor of Alzheimer’s disease is involved in the regulation of neurite outgrowth. J. Neurosci. 14, 2117–2127.

    PubMed  CAS  Google Scholar 

  • Stewart, L. C., and Klinman, J. P. (1988). Dopamine beta-hydroxylase of adrenal chromaffin granules: structure and function. Annu. Rev. Biochem. 57, 551–592.

    Article  PubMed  CAS  Google Scholar 

  • Van Nostrand, W. E. (1995). Zinc (II) selectively enhances the inhibition of coagulation factor XIa by protease nexin-2/amyloid beta-protein precursor. Thromb Res 78, 43–53.

    Article  PubMed  Google Scholar 

  • Wang, D., and Munoz, D. G. (1995). Qualitative and quantitative differences in senile plaque dystrophic neurites of Alzheimer’s disease and normal aged brain. J Neuropathol Exp Neurol 54, 548–556.

    Article  PubMed  CAS  Google Scholar 

  • Whyte, S., Jones, L., Coulson, E. J., Moir, R. D., Bush, A. I., Beyreuther, K., and Masters, C. L. (1997). The metabolism of the amyloid precursor protein of Alzheimer’s disease and dietary zinc. In Alzheimer’s Disease: Biology, Diagnosis and Therapeutics, K. Iqbal, B. Winblad, T. Nishimura, M. Takeda and H. M. Wisniewski, eds. (Chichester: John Wiley & Sons Ltd), pp. 417–422.

    Google Scholar 

  • Wiedau-Pazos, M., Goto, J. J., Rabizadeh, S., Gralla, E. B., Roe, J. A., Lee, M. K., Valentine, J. S., and Bredesen, D. E. (1996). Altered reactivity of Superoxide dismutase in familial amyotrophic lateral sclerosis. Science 277,515–518.

    Article  Google Scholar 

  • Wong, P. C., Pardo, C. A., Borchelt, D. R., Lee, M. K., Copeland, N. G., Jenkins, N. A., Sisodia, S. S., Cleveland, D. W., and Price, D. L. (1995). An adverse property of a familial ALS-linked Cu/Zn-SOD mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria. Neuron 14, 1105–1116.

    Article  PubMed  CAS  Google Scholar 

  • Yamazaki, T., Selkoe, D. J., and Koo, E. H. (1995). Trafficking of cell surface beta-amyloid precursor protein: retrograde and transcytotic transport in cultured neurons. J. Cell. Biol. 129, 431–442.

    Article  PubMed  CAS  Google Scholar 

  • Yim, H. S., Kang, J. H., Chock, P. B., Stadtman, E. R., and Yim, M. B. (1997). A familial amyotrophic lateral sclerosis-associated A4V Cu,Zn-Superoxide dismutase mutant has a lower K-m for hydrogen peroxide. J Biol Chem 272, 8861–8863.

    Article  PubMed  CAS  Google Scholar 

  • Yim, M. B., Kang, J. H., Yim, H. S., Kwak, H. S., Chock, P. B., and Stadtman, E. R. (1996). A gain-of-function of an amyotrophic lateral sclerosis-associated Cu,Zn-superoxide dismutase mutant: An enhancement of free radical formation due to a decrease in K-m for hydrogen peroxide. Proc Natl Acad Sci USA 93, 5709–5714.

    Article  PubMed  CAS  Google Scholar 

  • Zhou, B., and Gitschier, J. (1997). hCTRl: a human gene for copper uptake identified by complementation in yeast. Proc Natl Acad Sci U S A 94, 7481–7486.

    Article  PubMed  CAS  Google Scholar 

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Authors and Affiliations

  1. ZMBH-Center for Molecular Biology Heidelberg, University of Heidelberg, Im Neuenheimer Feld 282, D-69120, Heidelberg, Germany

    G. Multhaup, L. Hesse, T. Borchardt & K. Beyreuther

  2. Max von Pettenkofer-Institute for Virology, Ludwig-Maximilians University, 80336, Munich, Germany

    Thomas Ruppert

  3. Department of Pathology, University of Melbourne, Parkville, Victoria, 3052, Australia

    R. Cappai & C. L. Masters

  4. Australia and Neuropathology Laboratory, Mental Health Research Institute of Victoria, Parkville, Victoria, 3052, Australia

    R. Cappai & C. L. Masters

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  1. G. Multhaup
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  2. L. Hesse
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  3. T. Borchardt
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  4. Thomas Ruppert
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  5. R. Cappai
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  6. C. L. Masters
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  7. K. Beyreuther
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Editor information

Editors and Affiliations

  1. University of Salerno, Salerno, Italy

    Arturo Leone

  2. The Murdoch Institute for Research into Birth Defects, Royal Children’s Hospital, Parkville, Australia

    Julian F. B. Mercer

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Multhaup, G. et al. (1999). Autoxidation of Amyloid Precursor Protein and Formation of Reactive Oxygen Species. In: Leone, A., Mercer, J.F.B. (eds) Copper Transport and Its Disorders. Advances in Experimental Medicine and Biology, vol 448. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-4859-1_16

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  • DOI: https://doi.org/10.1007/978-1-4615-4859-1_16

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