Rutin suppresses human-amylin/hIAPP misfolding and oligomer formation in-vitro, and ameliorates diabetes and its impacts in human-amylin/hIAPP transgenic mice

Biochemical and Biophysical Research Communications

Volumn 482, Issue 4, 2017, Pages 625-631

  Aitken, Jacqueline F ^a   Loomes, Kerry M ^a,b   Riba Garcia, Isabel ^c   Unwin, Richard D ^c   Prijic, Gordana ^a   Phillips, Ashley S ^d   Phillips, Anthony R J ^a,b   Wu, Donghai ^e,f   Poppitt, Sally D ^a   Ding, Ke ^g   Barran, Perdita E ^d   Dowsey, Andrew W ^c,h   Cooper, Garth J S ^a,b,c  

^a UNIVERSITY OF AUCKLAND   (New Zealand)

^b UNIVERSITY OF AUCKLAND   (New Zealand)

^c UNIVERSITY OF MANCHESTER   (United Kingdom)

^d UNIVERSITY OF MANCHESTER   (United Kingdom)

^e GUANGZHOU INSTITUTES OF BIOMEDICINE AND HEALTH   (China)

^f GUANGZHOU MEDICAL UNIVERSITY   (China)

^g JINAN UNIVERSITY   (China)

^h UNIVERSITY OF BRISTOL   (United Kingdom)

Author keywords

Amylin; Ion mobility mass spectrometry; Rutin; Transgenic mice; Type 2 diabetes

Indexed keywords

AMYLIN; CARBOHYDRATE; DIMER; FORMIC ACID; GLUCOSE; MONOMER; OLIGOMER; QUERCETIN; RAFFINOSE; RUTOSIDE; AMYLOID; ANTIDIABETIC AGENT; GLUCOSE BLOOD LEVEL;

AMINO ACID SEQUENCE; ANIMAL EXPERIMENT; ANIMAL MODEL; ANTIDIABETIC ACTIVITY; ARTICLE; BODY WEIGHT; CARBOHYDRATE ANALYSIS; CHEMICAL STRUCTURE; CONTROLLED STUDY; DIABETES MELLITUS; DISEASE COURSE; FLUID INTAKE; FLUORESCENCE ANALYSIS; GLUCOSE BLOOD LEVEL; IN VITRO STUDY; MASS SPECTROMETRY; MOUSE; NONHUMAN; ORAC ASSAY; PRIORITY JOURNAL; PROTEIN MISFOLDING; ANIMAL; DIABETES MELLITUS, EXPERIMENTAL; DIABETES MELLITUS, TYPE 2; DRUG EFFECTS; GENETICS; HUMAN; MALE; METABOLISM; PANCREAS ISLET; PATHOLOGY; PROTEIN AGGREGATION, PATHOLOGICAL; PROTEIN FOLDING; PROTEOSTASIS DEFICIENCIES; TRANSGENIC MOUSE;

AMYLOID; ANIMALS; BLOOD GLUCOSE; DIABETES MELLITUS, EXPERIMENTAL; DIABETES MELLITUS, TYPE 2; HUMANS; HYPOGLYCEMIC AGENTS; ISLET AMYLOID POLYPEPTIDE; ISLETS OF LANGERHANS; MALE; MICE, TRANSGENIC; PROTEIN AGGREGATION, PATHOLOGICAL; PROTEIN FOLDING; PROTEOSTASIS DEFICIENCIES; RUTIN;

EID: 85007110620     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2016.11.083     Document Type: Article

References (28)

1. [1] IDF, The Global Burden: Diabetes and Impaired Glucose Tolerance International Diabetes Federation. 2013.
2. [2] Stumvoll, M., Goldstein, B.J., van Haeften, T.W., Type 2 diabetes: principles of pathogenesis and therapy. Lancet 365 (2005), 1333–1346.
3. [3] Zimmet, P., Alberti, K.G.M.M., Shaw, J., Global and societal implications of the diabetes epidemic. Nature 414 (2001), 782–787.
4. [4] Muoio, D.M., Newgard, C.B., Molecular and metabolic mechanisms of insulin resistance and β-cell failure in type 2 diabetes. Mol. Cell Biol. 9 (2008), 193–205.
5. [5] Cooper, G.J., Willis, A.C., Clark, A., Turner, R.C., Sim, R.B., Reid, K.B., Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients. Proc. Natl. Acad. Sci. U. S. A. 84 (1987), 8628–8632.
6. [6] Cooper, G.J.S., Amylin compared with calcitonin gene-related peptide: structure, biology, and relevance to metabolic disease. Endocr. Rev. 15 (1994), 163–201.
7. [7] Guardado-Mendoza, R., Davalli, A.M., Chavez, A.O., Hubbard, G.B., Dick, E.J., Majluf-Cruz, A., Tene-Perez, C.E., Goldschmidt, L., Hart, J., Perego, C., Comuzzie, A.G., Tejero, M.E., Finzi, G., Placidi, C., La Rosai, S., Capellai, C., Halff, G., Gastaldelli, A., DeFronzo, R.A., Follia, F., Pancreatic islet amyloidosis, β-cell apoptosis, and α-cell proliferation are determinants of islet remodeling in type-2 diabetic baboons. Proc. Natl. Acad. Sci. U. S. A. 106 (2009), 13992–13997.
8. [8] Zhang, S., Liu, H., Chuang, C.L., Li, X., Au, M., Zhang, L., Phillips, A.R.J., Scott, D.W., Cooper, G.J.S., The pathogenic mechanism of diabetes varies with the degree of overexpression and oligomerization of human amylin in the pancreatic islet beta-cells. FASEB J. 28 (2014), 5083–5096.
9. [9] Aitken, J.F., Loomes, K.M., Scott, D.W., Reddy, S., Phillips, A.R.J., Prijic, G., Fernando, C., Zhang, S., Broadhurst, R., L'Huillier, P., Cooper, G.J.S., Tetracycline treatment retards the onset and slows the progression of diabetes in human amylin/hIAPP transgenic mice. Diabetes 59 (2010), 161–171.
10. [10] Aitken, J.F., Loomes, K.M., Konarkowska, B., Cooper, G.J.S., Suppression by polycyclic compounds of the conversion of human amylin into insoluble amyloid. Biochem. J. 374 (2003), 779–784.
11. [11] Kilkenny, C., Browne, W.J., Cuthill, I.C., Emerson, M., Altman, D.G., Improving bioscience research reporting: the ARRIVE guidelines for reporting animal research. PLoS Biol., 8, 2010.
12. [12] Wong, W.P., Scott, D.W., Chuang, C.L., Zhang, S., Liu, H., Ferreira, A., Saafi, E.L., Choong, Y.S., Cooper, G.J.S., Spontaneous diabetes in hemizygous human amylin transgenic mice that developed neither islet amyloid nor peripheral insulin resistance. Diabetes 57 (2008), 2737–2744.
13. [13] Green, J., Goldsbury, C., Mini, T., Sunderji, S., Frey, P., Kistler, J., Cooper, G.J.S., Aebi, U., Full-length rat amylin forms fibrils following substitution of single residues from human amylin. J. Mol. Biol. 326 (2003), 1147–1156.
14. [14] Roberts, A.N., Leighton, B., Todd, J.A., Cockburn, D., Schofield, P.N., Sutton, R., Holt, S., Boyd, Y., Day, A.J., Foot, E.A., Willis, A.C., Reid, K.B., Cooper, G.J., Molecular and functional characterization of amylin, a peptide associated with type 2 diabetes mellitus. Proc. Natl. Acad. Sci. U. S. A. 86 (1989), 9662–9666.
15. [15] Phillips, A.S., Gomes, A.F., Kalapothakis, J.M., Gillam, J.E., Gasparavicius, J., Gozzo, F.C., Kunath, T., MacPhee, C., Barran, P.E., Conformational dynamics of alpha-synuclein: insights from mass spectrometry. Analyst 140 (2015), 3070–3081.
16. [16] Riba, I., Barran, P.E., Cooper, G.J.S., Unwin, R.D., On the structure of the copper-amylin complex. Int. J. Mass Spectrom. 391 (2015), 47–53.
17. [17] Aitken, J.F., Loomes, K.M., Riba-Garcia, I., Unwin, R.D., Prijic, G., Phillips, A.S., Phillips, A.R.J., Barran, P.E., Dowsey, A.W., Cooper, G.J.S., Data Describing the Impact of the Flavonol Rutin, on the Blood-glucose Profiles, Fluid-intake Profiles and Survival of Human Amylin Transgenic Mice. 2016 Data in Brief, submitted.
18. [18] Egert, S., Wolffram, S., Bosy-Westphal, A., Boesch-Saadatmandi, C., Wagner, A.E., Frank, J., Rimbach, G., Mueller, M.J., Daily quercetin supplementation dose-dependently increases plasma quercetin concentrations in healthy humans. J. Nutr. 138 (2008), 1615–1621.
19. [19] Kuhnau, J., The flavonoids. A class of semi-essential food components: their role in human nutrition. World Rev. Nutr. Diet. 24 (1976), 117–191.
20. [20] Hollman, P.C.H., Bijsman, M.N.C.P., van Gameren, Y., Cnossen, E.P.J., de Vries, J.H.M., Katan, M.B., The sugar moiety is a major determinant of the absorption of dietary flavonoid glycosides in man. Free Radic. Res. 31 (1999), 569–573.
21. [21] Graefe, E.U., Wittig, J., Mueller, S., Riethling, A.K., Uehleke, B., Drewelow, B., Pforte, H., Jacobasch, G., Derendorf, H., Veit, M., Pharmacokinetics and bioavailability of quercetin glycosides in humans. J. Clin. Pharmacol. 41 (2001), 492–499.
22. [22] Butler, A.E., Janson, J., Soeller, W.C., Butler, P.C., Increased beta-cell apoptosis prevents adaptive increase in beta-cell mass in mouse model of type 2 diabetes: evidence for role of islet amyloid formation rather than direct action of amyloid. Diabetes 52 (2003), 2304–2314.
23. [23] Butler, A.E., Jang, J., Gurlo, T., Carty, M.D., Soeller, W.C., Butler, P.C., Diabetes due to a progressive defect in beta-cell mass in rats transgenic for human islet amyloid polypeptide (HIP Rat): a new model for type 2 diabetes. Diabetes 53 (2004), 1509–1516.
24. [24] Janson, J., Soeller, W.C., Roche, P.C., Nelson, R.T., Torchia, A.J., Kreutter, D.K., Butler, P.C., Spontaneous diabetes mellitus in transgenic mice expressing human islet amyloid polypeptide. Proc. Natl. Acad. Sci. U. S. A. 93 (1996), 7283–7288.
25. [25] Hardy, J., Selkoe, D.J., The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297 (2002), 353–356.
26. [26] Goldberg, M.S., Lansbury, P.T. Jr., Is there a cause-and-effect relationship between alpha-synuclein fibrillization and Parkinson's disease?. Nat. Cell Biol. 2 (2000), E115–E119.
27. [27] Sousa, M.M., Cardoso, I., Fernandes, R., Guimaraes, A., Saraiva, M.J., Deposition of transthyretin in early stages of familial amyloidotic polyneuropathy: evidence for toxicity of nonfibrillar aggregates. Am. J. Pathol. 159 (2001), 1993–2000.
28. [28] Coskun, O., Kanter, M., Korkmaz, A., Oter, S., Quercetin, a flavonoid antioxidant, prevents and protects streptozotocin-induced oxidative stress and β-cell damage in rat pancreas. Pharmacol. Res. 51 (2005), 117–123.