Fe(II) formation after interaction of the amyloid β-peptide with iron-storage protein ferritin

Journal of Biological Physics

Volumn 44, Issue 3, 2018, Pages 237-243

  Balejcikova, Lucia ^a   Siposova, Katarina ^a   Kopcansky, Peter ^a   Safarik, Ivo ^b,c  

^a INSTITUTE OF EXPERIMENTAL PHYSICS   (Slovakia)

^b INSTITUTE OF MATHEMATICS   (Czech Republic)

^c PALACKÝ UNIVERSITY   (Czech Republic)

Author keywords

Alzheimer s disease; A ; Ferritin; Iron reduction; Magnetite; Metallochaperone

Indexed keywords

AMYLOID BETA PROTEIN; FERRIC HYDROXIDE; FERRITIN; IRON; AMYLOID;

ARTICLE; CONTROLLED STUDY; IN VITRO STUDY; MOLECULAR SIZE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN PROTEIN INTERACTION; CHEMISTRY; HUMAN; METABOLISM; OXIDATION REDUCTION REACTION;

AMYLOID; AMYLOID BETA-PEPTIDES; FERRITINS; HUMANS; IRON; OXIDATION-REDUCTION;

EID: 85046652384     PISSN: 00920606     EISSN: 15730689     Source Type: Journal    
DOI: 10.1007/s10867-018-9498-3     Document Type: Article

References (25)

1. Jarrett, J.T., Berger, E.P., Lansbury, P.T.: The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer’s disease. Biochemistry 32, 4693–4697 (1993)
2. El-Agnaf, O.M.A., Mahil, D.S., Patel, B.P., Austen, B.M.: Oligomerization and toxicity of β-amyloid-42 implicated in Alzheimer’s disease. Biochem. Biophys. Res. Commun. 273, 1003–1007 (2000)
3. Selkoe, D.J.: Alzheimer’s disease: genes, proteins, and therapy. Physiol. Rev. 81, 741–766 (2001)
4. Hilbich, C., Kisterswoike, B., Reed, J., Masters, C.L., Beyreuther, K.: Substitutions of hydrophobic amino acids reduce the amyloidogenicity of Alzheimer’s disease βA4 peptides. J. Mol. Biol. 228, 460–473 (1992)
5. Soto, C., Castaño, E.M., Kumar, R.A., Beavis, R.C., Frangione, B.: Fibrillogenesis of synthetic amyloid-β peptides is dependent on their initial secondary structure. Neurosci. Lett. 200, 105–108 (1995)
6. Tjernberg, L.O., Naslund, J., Lindqvist, F., Johansson, J., Karlstrom, A.R., Thyberg, J., Terenius, L., Nordstedt, C.: Arrest of β-amyloid fibril formation by a pentapeptide ligand. J. Biol. Chem. 271, 8545–8548 (1996)
7. Everett, J., Cespedes, E., Shelford, L.R., Exley, C., Collingwood, J.F., Dobson, J., van der Laan, G., Jenkins, C.A., Arenholz, E., Telling, N.D.: Evidence of redox-active iron formation following aggregation of ferrihydrite and the Alzheimer’s disease peptide β-amyloid. Inorg. Chem. 53, 2803–2809 (2014)
8. Scarpini, E., Scheltens, P., Feldman, H.: Treatment of Alzheimer’s disease: current status and new perspectives. Lancet Neurol. 2, 539–547 (2003)
9. Pankhurst, Q., Hautot, D., Khan, N., Dobson, J.: Increased levels of magnetic iron compounds in Alzheimer's disease. J. Alzheimers Dis. 13, 49–52 (2008)
10. Brillas, E., Sirés, I., Oturan, M.A.: Electro-Fenton process and related electrochemical technologies based on Fenton’s reaction chemistry. Chem. Rev. 109, 6570–6631 (2009)
11. Crichton, R.R., Dexter, D.T., Ward, R.J.: Brain iron metabolism and its perturbation in neurological diseases. J. Neural Transm. 118, 301–314 (2011)
12. Zecca, L., Youdim, M.B.H., Riederer, P., Connor, J.R., Crichton, R.R.: Iron, brain ageing and neurodegenerative disorders. Nat. Rev. Neurosci. 5, 863–873 (2004)
13. Everett, J., Cespedes, E., Shelford, L.R., Exley, C., Collingwood, J.F., Dobson, J., van der Laan, G., Jenkins, C.A., Arenholz, E., Telling, N.D.: Ferrous iron formation following the co-aggregation of ferric iron and the Alzheimer’s disease peptide β-amyloid (1-42). J. Royal Soc. Interface 11, 20140165 (2014)
14. Riemer, J., Hoepken, H.H., Czerwinska, H., Robinson, S.R., Dringen, R.: Colorimetric ferrozine-based assay for the quantitation of iron in cultured cells. Anal. Biochem. 331, 370–375 (2004)
15. Khan, A., Dobson, J.P., Exley, C.: Redox cycling of iron by Aβ42. Free Radic. Biol. Med. 40, 557–569 (2006)
16. Jutz, G., van Rijn, P., Santos Miranda, B., Böker, A.: Ferritin: a versatile building block for bionanotechnology. Chem. Rev. 115, 1653–1701 (2015)
17. Watt, R.K., Hilton, R.J., Graff, D.M.: Oxido-reduction is not the only mechanism allowing ions to traverse the ferritin protein shell. Biochim. Biophys. Acta Gen. Subj. 1800, 745–759 (2010)
18. Carmona, F., Palacios, O., Galvez, N., Cuesta, R., Atrian, S., Capdevila, M., Dominguez-Vera, J.M.: Ferritin iron uptake and release in the presence of metals and metalloproteins: chemical implications in the brain. Coor. Chem. Rev. 257, 2752–2764 (2013)
19. Philpott, C.C., Ryu, M.-S.: Special delivery: distributing iron in the cytosol of mammalian cells. Front. Pharmacol. 5, 173 (2014)
20. Tahirbegi, I.B., Pardo, W.A., Alvira, M., Mir, M., Samitier, J.: Amyloid Aβ 42, a promoter of magnetite nanoparticle formation in Alzheimer’s disease. Nanotechnology 27, 465102 (2016)
21. Laurent, S., Forge, D., Port, M., Roch, A., Robic, C., Elst, L.V., Muller, R.N.: Magnetic iron oxide nanoparticles: synthesis, stabilization, vectorization, physicochemical characterizations, and biological applications. Chem. Rev. 108, 2064–2110 (2008)
22. Khurana, R., Coleman, C., Ionescu-Zanetti, C., Carter, S.A., Krishna, V., Grover, R.K., Roy, R., Singh, S.: Mechanism of thioflavin T binding to amyloid fibrils. J. Struct. Biol. 151, 229–238 (2005)
23. Vassar, P.S., Culling, C.F.: Fluorescent stains, with special reference to amyloid and connective tissues. Arch. Pathol. 68, 487–498 (1959)
24. LeVine III, H.: Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 2, 404–410 (1993)
25. Huang, X., Atwood, C.S., Hartshorn, M.A., Multhaup, G., Goldstein, L.E., Scarpa, R.C., Cuajungco, M.P., Gray, D.N., Lim, J., Moir, R.D., Tanzi, R.E., Bush, A.I.: The Aβ peptide of Alzheimer’s disease directly produces hydrogen peroxide through metal ion reduction. Biochemistry 38, 7609–7616 (1999)