Myricetin inhibits islet amyloid polypeptide (IAPP) aggregation and rescues living mammalian cells from IAPP toxicity

Open Biochemistry Journal

Volumn 6, Issue , 2012, Pages 66-70

  Zelus, Casey ^a   Fox, Ayano ^a   Calciano, Anastasia ^a   Faridian, Bianca S ^b   Nogaj, Luiza A ^b   Moffet, David A ^a  

^a LOYOLA MARYMOUNT UNIVERSITY   (United States)

^b Mount St Mary's College   (United States)

Author keywords

Amylin; Amyloid; Type 2 diebetes

Indexed keywords

AMYLIN; ENHANCED GREEN FLUORESCENT PROTEIN; MYRICETIN; THIOFLAVINE;

ARTICLE; ATOMIC FORCE MICROSCOPY; CELL PROTECTION; CONCENTRATION RESPONSE; CONTROLLED STUDY; DRUG CYTOTOXICITY; DRUG STRUCTURE; MAMMAL CELL; PRIORITY JOURNAL; PROTEIN AGGREGATION;

EID: 84863792805     PISSN: None     EISSN: 1874091X     Source Type: Journal    
DOI: 10.2174/1874091X01206010066     Document Type: Article

References (21)

1. Olzscha, H.; Schermann, S. M.; Woerner, A. C.; Pinkert, S.; Hecht, M. H.; Tartaglia, G. G.; Vendruscolo, M.; Hayer-Hartl, M.; Hartl, F. U.; Vabulas, R. M. Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions. Cell, 2011, 144, 67-78.
2. Apostolidou, M.; Jayasinghe, S. A.; Langen, R. Structure of alpha-helical membrane-bound human islet amyloid polypeptide and its implications for membrane-mediated misfolding. J. Biol. Chem., 2008, 283, 17205-17210.
3. Hull, R. L.; Westermark, G. T.; Westermark, P.; Kahn, S. E. Islet amyloid: a critical entity in the pathogenesis of type 2 diabetes. J. Clin. Endocrinol. Metab., 2004, 89, 3629-3643.
4. Kahn, S. E.; Andrikopoulos, S.; Verchere, C. B. Islet amyloid: A long-recognized but underappreciated pathological feature of type 2 diabetes. Diabetes, 1999, 48, 241-253.
5. Ritzel, R. A.; Meier, J. J.; Lin, C. Y.; Veldhuis, J. D.; Butler, P. C. Human islet amyloid polypeptide oligomers disrupt cell coupling, induce apoptosis, and impair insulin secretion in isolated human islets. Diabetes, 2007, 56, 65-71.
6. Porat, Y.; Abramowitz, A.; Gazit, E. Inhibition of amyloid fibril formation by polyphenols: structural similarity and aromatic interactions as a common inhibition mechanism. Chem. Biol. Drug Des., 2006, 67, 27-37.
7. Ono, K.; Yoshiike, Y.; Takashima, A.; Hasegawa, K.; Naiki, H.; Yamada, M. Potent anti-amyloidogenic and fibril-destabilizing effects of polyphenols in vitro: implications for the prevention and therapeutics of Alzheimer's disease. J. Neurochem., 2003, 87, 172-181.
8. Taniguchi, S.; Suzuki, N.; Masuda, M.; Hisanaga, S.; Iwatsubo, T.; Goedert, M.; Hasegawa, M. Inhibition of heparin-induced tau filament formation by phenothiazines, polyphenols, and porphyrins. J. Biol. Chem., 2005, 280, 7614-7623.
9. Meng, F. L.; Abedini, A.; Plesner, A.; Verchere, C. B.; Raleigh, D. P. The Flavanol (-)-Epigallocatechin 3-gallate inhibits amyloid formation by islet amyloid polypeptide, disaggregates amyloid fibrils, and protects cultured cells against iapp-induced toxicity. Bio-chemistry, 2010, 49, 8127-8133.
10. Noor, H.; Cao, P.; Raleigh, D. P. Morin hydrate inhibits amyloid formation by islet amyloid polypeptide and disaggregates amyloid fibers. Protein. Sci., 2012, 21, 373-382.
11. Levine, H. 3rd. Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci., 1993, 2, 404-410.
12. Yamin, G,;Ruchala, P. Teplow, D.B. A Peptide Hairpin Inhibitor of Amyloid beta-Protein Oligomerization and Fibrillogenesis. Bio-chemistry, 2009, 48, 11329-11331.
13. Ahn, J. S.; Lee, J. H.; Kim, J. H.; Paik, S. R. Novel method for quantitative determination of amyloid fibrils of alpha-synuclein and amyloid beta/A4 protein by using resveratrol. Anal. Biochem., 2007, 367, 259-265.
14. Baine, M.; Georgie, D. S.; Shiferraw, E. Z.; Nguyen, T. P. T.; Nogaj, L. A.; Moffet, D. A. Inhibition of A beta 42 aggregation using peptides selected from combinatorial libraries. J. Pept. Sci., 2009, 15, 499-503.
15. De Groot, N. S.; Aviles, F. X.; Vendrell, J.; Ventura, S. Mutagenesis of the central hydrophobic cluster in A beta 42 Alzheimer's pepticle -Side-chain properties correlate with aggregation propensities. FEBS J., 2006, 273, 658-668.
16. Kim, W.; Kim, Y.; Min, J.; Kim, D. J.; Chang, Y. T.; Hecht, M. H. A high-throughput screen for compounds that inhibit aggregation of the Alzheimer's peptide. ACS Chem. Bio., 2006, 1, 461-469.
17. Wurth, C.; Guimard, N. K.; Hecht, M. H. Mutations that reduce aggregation of the Alzheimer's Abeta42 peptide: an unbiased search for the sequence determinants of Abeta amyloidogenesis. J. Mol. Biol., 2002, 319, 1279-1290.
18. Wurth, C.; Kim, W.; Hecht, M. H. Combinatorial approaches to probe the sequence determinants of protein aggregation and amyloidogenicity. Protein Pept. Lett., 2006, 13, 279-286.
19. Kim, W.; Hecht, M. H. Generic hydrophobic residues are sufficient to promote aggregation of the Alzheimer's A beta 42 peptide. Proc. Natl. Acad. Sci. USA, 2006, 103, 15824-15829.
20. Kim, W.; Hecht, M. H. Mutations enhance the aggregation propensity of the Alzheimer's A beta peptide. J. Mol. Biol., 2008, 377, 565-574.
21. Fox, A.; Snollaerts, T.; Casanova, C. E.; Calciano, A.; Nogaj, L. A.; Moffet, D. A. Selection for Nonamyloidogenic Mutants of Islet Amyloid Polypeptide (IAPP) Identifies an Extended Region for Amyloidogenicity. Biochemistry, 2010, 49, 7783-7789.