Phenylalanine assembly into toxic fibrils suggests amyloid etiology in phenylketonuria

Nature Chemical Biology

Volumn 8, Issue 8, 2012, Pages 701-706

  Adler Abramovich, Lihi ^a   Vaks, Lilach ^a   Carny, Ohad ^a   Trudler, Dorit ^a   Magno, Andrea ^b   Caflisch, Amedeo ^b   Frenkel, Dan ^a   Gazit, Ehud ^a  

^a TEL AVIV UNIVERSITY   (Israel)

^b UNIVERSITY OF ZURICH   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; AMYLOID PROTEIN; PHENYLALANINE;

ALZHEIMER DISEASE; AMYLOIDOSIS; ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ANTIBODY PRODUCTION; ARTICLE; AUTOSOMAL RECESSIVE DISORDER; CHO CELL; CONTROLLED STUDY; CYTOTOXICITY; ELECTRON DIFFRACTION; HIPPOCAMPUS; HISTOLOGY; HUMAN; HUMAN TISSUE; IMMUNOPRECIPITATION; MENTAL DEFICIENCY; MORPHOLOGY; MOUSE; NEUROPATHOLOGY; NONHUMAN; PARIETAL CORTEX; PHENYLKETONURIA; PRIORITY JOURNAL;

MUS;

EID: 84864285157     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.1002     Document Type: Article

References (28)

1. Hanley, W.B. Adult phenylketonuria. Am. J. Med. 117, 590-595 (2004).
2. Surtees, R. & Blau, N. The neurochemistry of phenylketonuria. Eur. J. Pediatr. 159 (suppl.), S109-S113 (2000).
3. Choi, T.B. & Pardridge, W.M. Phenylalanine transport at the human blood-brain barrier. Studies with isolated human brain capillaries. J. Biol. Chem. 261, 6536-6541 (1986).
4. Krause, W. et al. Biochemical and neuropsychological effects of elevated plasma phenylalanine in patients with treated phenylketonuria. A model for the study of phenylalanine and brain function in man. J. Clin. Invest. 75, 40-48 (1985).
5. MacDonald, A., Gokmen-Ozel, H., Van Rijn, M. & Burgard, P. The reality of dietary compliance in the management of phenylketonuria. J. Inherit. Metab. Dis. 33, 665-670 (2010).
6. Chiti, F. & Dobson, C.M. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75, 333-366 (2006).
7. Rochet, J.C. & Lansbury, P.T. Amyloid fibrillogenesis: Themes and variations. Curr. Opin. Struct. Biol. 10, 60-68 (2000).
8. Inouye, H., Sharma, D., Goux, W.J. & Kirschner, D.A. Structure of core domain of fibril-forming PHF/Tau fragments. Biophys. J. 90, 1774-1789 (2006).
9. Gazit, E. A possible role for p-stacking in the self-assembly of amyloid fibrils. FASEB J. 16, 77-83 (2002).
10. Makin, O.S. & Serpell, L.C. Structures for amyloid fibrils. FEBS J. 272, 5950-5961 (2005).
11. Gazit, E. Global analysis of tandem aromatic octapeptide repeats: The significance of the aromatic-glycine motif. Bioinformatics 18, 880-883 (2002).
12. Reches, M., Porat, Y. & Gazit, E. Amyloid fibril formation by pentapeptide and tetrapeptide fragments of human calcitonin. J. Biol. Chem. 277, 35475-35480 (2002).
13. Reches, M. & Gazit, E. Casting metal nanowires within discrete self-assembled peptide nanotubes. Science 300, 625-627 (2003).
14. Tjernberg, L.O. et al. Arrest of β-amyloid fibril formation by a pentapeptide ligand. J. Biol. Chem. 271, 8545-8548 (1996).
15. Soto, C. β-sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: Implications for Alzheimer's therapy. Nat. Med. 4, 822-826 (1998).
16. Hörster, F. et al. Phenylalanine reduces synaptic density in mixed cortical cultures from mice. Pediatr. Res. 59, 544-548 (2006).
17. Makin, O.S., Atkins, E., Sikorski, P., Johansson, J. & Serpell, L.C. Molecular basis for amyloid fibril formation and stability. Proc. Natl. Acad. Sci. USA 102, 315-320 (2005).
18. Brooks, B.R. et al. CHARMM: The biomolecular simulation program. J. Comput. Chem. 30, 1545-1614 (2009).
19. Haberthür, U. & Caflisch, A. FACTS: Fast analytical continuum treatment of solvation. J. Comput. Chem. 29, 701-715 (2008).
20. Lesné, S. et al. A specific amyloid-β protein assembly in the brain impairs memory. Nature 440, 352-357 (2006).
21. Abramov, E. et al. Amyloid-β as a positive endogenous regulator of release probability at hippocampal synapses. Nat. Neurosci. 12, 1567-1576 (2009).
22. Shedlovsky, A., McDonald, J.D., Symula, D. & Dove, W.F. Mouse models of human phenylketonuria. Genetics 134, 1205-1210 (1993).
23. Gazit, V., Ben-Abraham, R., Pick, C.G. & Katz, Y. β-Phenylpyruvate induces long-term neurobehavioral damage and brain necrosis in neonatal mice. Behav. Brain Res. 143, 1-5 (2003).
24. Cordero, M.E., Trejo, M., Colombo, M. & Aranda, V. Histological maturation of the neocortex in phenylketonuric rats. Early Hum. Dev. 8, 157-173 (1983).
25. Lashuel, H.A., Hartley, D., Petre, B.M., Walz, T. & Lansbury, P.T. Neurodegenerative disease: Amyloid pores from pathogenic mutations. Nature 418, 291 (2002).
26. Bucciantini, M. et al. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416, 507-511 (2002).
27. Solomon, B. Clinical immunologic approaches for the treatment of Alzheimer's disease. Expert Opin. Investig. Drugs 16, 819-828 (2007).
28. Schenk, D. et al. Immunization with amyloid-β attenuates Alzheimer-disease-like pathology in the PDAPP mouse. Nature 400, 173-177 (1999).