메뉴 건너뛰기




Volumn 12, Issue , 2015, Pages 450-457

Inhibition of toxic IAPP amyloid by extracts of common fruits

Author keywords

Amyloid inhibition; Diabetes; Natural product therapeutics

Indexed keywords

MAMMALIA;

EID: 84920735921     PISSN: 17564646     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jff.2014.12.013     Document Type: Article
Times cited : (15)

References (36)
  • 1
    • 84876021115 scopus 로고    scopus 로고
    • Mechanisms of islet amyloidosis toxicity in type 2 diabetes
    • Abedini A., Schmidt A.M. Mechanisms of islet amyloidosis toxicity in type 2 diabetes. FEBS Letters 2013, 587:1119-1127.
    • (2013) FEBS Letters , vol.587 , pp. 1119-1127
    • Abedini, A.1    Schmidt, A.M.2
  • 3
    • 47749117154 scopus 로고    scopus 로고
    • Structure of alpha-helical membrane-bound human islet amyloid polypeptide and its implications for membrane-mediated misfolding
    • Apostolidou M., Jayasinghe S.A., Langen R. Structure of alpha-helical membrane-bound human islet amyloid polypeptide and its implications for membrane-mediated misfolding. The Journal of Biological Chemistry 2008, 283:17205-17210.
    • (2008) The Journal of Biological Chemistry , vol.283 , pp. 17205-17210
    • Apostolidou, M.1    Jayasinghe, S.A.2    Langen, R.3
  • 4
    • 34548494605 scopus 로고    scopus 로고
    • Membrane fragmentation by an amyloidogenic fragment of human Islet Amyloid Polypeptide detected by solid-state NMR spectroscopy of membrane nanotubes
    • Brender J.R., Durr U.H., Heyl D., Budarapu M.B., Ramamoorthy A. Membrane fragmentation by an amyloidogenic fragment of human Islet Amyloid Polypeptide detected by solid-state NMR spectroscopy of membrane nanotubes. Biochimica et Biophysica Acta 2007, 1768:2026-2029.
    • (2007) Biochimica et Biophysica Acta , vol.1768 , pp. 2026-2029
    • Brender, J.R.1    Durr, U.H.2    Heyl, D.3    Budarapu, M.B.4    Ramamoorthy, A.5
  • 5
    • 43949107500 scopus 로고    scopus 로고
    • Amyloid fiber formation and membrane disruption are separate processes localized in two distinct regions of IAPP, the type-2-diabetes-related peptide
    • Brender J.R., Lee E.L., Cavitt M.A., Gafni A., Steel D.G., Ramamoorthy A. Amyloid fiber formation and membrane disruption are separate processes localized in two distinct regions of IAPP, the type-2-diabetes-related peptide. Journal of the American Chemical Society 2008, 130:6424-6429.
    • (2008) Journal of the American Chemical Society , vol.130 , pp. 6424-6429
    • Brender, J.R.1    Lee, E.L.2    Cavitt, M.A.3    Gafni, A.4    Steel, D.G.5    Ramamoorthy, A.6
  • 6
    • 84858632761 scopus 로고    scopus 로고
    • Membrane disruption and early events in the aggregation of the diabetes related peptide IAPP from a molecular perspective
    • Brender J.R., Salamekh S., Ramamoorthy A. Membrane disruption and early events in the aggregation of the diabetes related peptide IAPP from a molecular perspective. Accounts of Chemical Research 2012, 45:454-462.
    • (2012) Accounts of Chemical Research , vol.45 , pp. 454-462
    • Brender, J.R.1    Salamekh, S.2    Ramamoorthy, A.3
  • 7
    • 84873527000 scopus 로고    scopus 로고
    • Aggregation of islet amyloid polypeptide: From physical chemistry to cell biology
    • Cao P., Abedini A., Raleigh D.P. Aggregation of islet amyloid polypeptide: From physical chemistry to cell biology. Current Opinion in Structural Biology 2013, 23:82-89.
    • (2013) Current Opinion in Structural Biology , vol.23 , pp. 82-89
    • Cao, P.1    Abedini, A.2    Raleigh, D.P.3
  • 9
    • 84859379008 scopus 로고    scopus 로고
    • Analysis of the inhibition and remodeling of islet amyloid polypeptide amyloid fibers by flavanols
    • Cao P., Raleigh D.P. Analysis of the inhibition and remodeling of islet amyloid polypeptide amyloid fibers by flavanols. Biochemistry 2012, 51:2670-2683.
    • (2012) Biochemistry , vol.51 , pp. 2670-2683
    • Cao, P.1    Raleigh, D.P.2
  • 10
    • 84898029812 scopus 로고    scopus 로고
    • Camellia sinensis fruit peel extract inhibits angiogenesis and ameliorates obesity induced by high-fat diet in rats
    • Chaudhary N., Bhardwaj J., Seo H.J., Kim M.Y., Shin T.S., Kim J.D. Camellia sinensis fruit peel extract inhibits angiogenesis and ameliorates obesity induced by high-fat diet in rats. Journal of Functional Foods 2014, 7:479-486.
    • (2014) Journal of Functional Foods , vol.7 , pp. 479-486
    • Chaudhary, N.1    Bhardwaj, J.2    Seo, H.J.3    Kim, M.Y.4    Shin, T.S.5    Kim, J.D.6
  • 11
    • 84920747411 scopus 로고    scopus 로고
    • Apple polyphenol inhibits colon carcinoma metastasis via disrupting snail binding to focal adhesion kinase
    • Chia-Hung H., Chi-Chou H., Hsu L.-S., Kao S.-H., Wang C.-J. Apple polyphenol inhibits colon carcinoma metastasis via disrupting snail binding to focal adhesion kinase. Journal of Functional Foods 2015, 12:80-91.
    • (2015) Journal of Functional Foods , vol.12 , pp. 80-91
    • Chia-Hung, H.1    Chi-Chou, H.2    Hsu, L.-S.3    Kao, S.-H.4    Wang, C.-J.5
  • 12
    • 77956395740 scopus 로고    scopus 로고
    • Selection for nonamyloidogenic mutants of islet amyloid polypeptide (IAPP) identifies an extended region for amyloidogenicity
    • 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.
    • (2010) Biochemistry , vol.49 , pp. 7783-7789
    • Fox, A.1    Snollaerts, T.2    Casanova, C.E.3    Calciano, A.4    Nogaj, L.A.5    Moffet, D.A.6
  • 13
    • 28244458451 scopus 로고    scopus 로고
    • Mechanisms of amyloid fibril self-assembly and inhibition
    • Gazit E. Mechanisms of amyloid fibril self-assembly and inhibition. FEBS Journal 2005, 272:5971-5978.
    • (2005) FEBS Journal , vol.272 , pp. 5971-5978
    • Gazit, E.1
  • 14
    • 43549100675 scopus 로고    scopus 로고
    • Islet amyloid in type 2 diabetes, and the toxic oligomer hypothesis
    • Haataja L., Gurlo T., Huang C.J., Butler P.C. Islet amyloid in type 2 diabetes, and the toxic oligomer hypothesis. Endocrine Reviews 2008, 29:303-316.
    • (2008) Endocrine Reviews , vol.29 , pp. 303-316
    • Haataja, L.1    Gurlo, T.2    Huang, C.J.3    Butler, P.C.4
  • 16
    • 0032969276 scopus 로고    scopus 로고
    • Islet amyloid: A long-recognized but underappreciated pathological feature of type 2 diabetes
    • 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.
    • (1999) Diabetes , vol.48 , pp. 241-253
    • Kahn, S.E.1    Andrikopoulos, S.2    Verchere, C.B.3
  • 18
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: Detection of amyloid aggregation in solution
    • LeVine H. Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: Detection of amyloid aggregation in solution. Protein Science 1993, 2:404-410.
    • (1993) Protein Science , vol.2 , pp. 404-410
    • LeVine, H.1
  • 19
    • 15044340251 scopus 로고    scopus 로고
    • Protective effects of oligomers of grape seed polyphenols against beta-amyloid-induced oxidative cell death
    • Li M.H., Jang J.H., Sun B., Surh Y.J. Protective effects of oligomers of grape seed polyphenols against beta-amyloid-induced oxidative cell death. Annals of the New York Academy of Sciences 2004, 1030:317-329.
    • (2004) Annals of the New York Academy of Sciences , vol.1030 , pp. 317-329
    • Li, M.H.1    Jang, J.H.2    Sun, B.3    Surh, Y.J.4
  • 22
    • 67650533782 scopus 로고    scopus 로고
    • Three-dimensional structure and orientation of rat islet amyloid polypeptide protein in a membrane environment by solution NMR spectroscopy
    • Nanga R.P., Brender J.R., Xu J., Hartman K., Subramanian V., Ramamoorthy A. Three-dimensional structure and orientation of rat islet amyloid polypeptide protein in a membrane environment by solution NMR spectroscopy. Journal of the American Chemical Society 2009, 131:8252-8261.
    • (2009) Journal of the American Chemical Society , vol.131 , pp. 8252-8261
    • Nanga, R.P.1    Brender, J.R.2    Xu, J.3    Hartman, K.4    Subramanian, V.5    Ramamoorthy, A.6
  • 23
    • 57049174009 scopus 로고    scopus 로고
    • Structures of rat and human islet amyloid polypeptide IAPP(1-19) in micelles by NMR spectroscopy
    • Nanga R.P., Brender J.R., Xu J., Veglia G., Ramamoorthy A. Structures of rat and human islet amyloid polypeptide IAPP(1-19) in micelles by NMR spectroscopy. Biochemistry 2008, 47:12689-12697.
    • (2008) Biochemistry , vol.47 , pp. 12689-12697
    • Nanga, R.P.1    Brender, J.R.2    Xu, J.3    Veglia, G.4    Ramamoorthy, A.5
  • 24
    • 84903686602 scopus 로고    scopus 로고
    • Prevalence of obesity among adults: United States
    • 2011-2012. NCHS Data Brief, 1-8.
    • Ogden, C. L., Carroll, M. D., Kit, B. K., & Flegal, K. M. (2014a). Prevalence of obesity among adults: United States, 2011-2012. NCHS Data Brief, 1-8.
    • (2014)
    • Ogden, C.L.1    Carroll, M.D.2    Kit, B.K.3    Flegal, K.M.4
  • 25
    • 84862005859 scopus 로고    scopus 로고
    • Prevalence of obesity in the United States
    • 2009-2010. NCHS Data Brief, 1-8.
    • Ogden, C. L., Carroll, M. D., Kit, B. K., & Flegal, K. M. (2014b). Prevalence of obesity in the United States, 2009-2010. NCHS Data Brief, 1-8.
    • (2014)
    • Ogden, C.L.1    Carroll, M.D.2    Kit, B.K.3    Flegal, K.M.4
  • 27
    • 78449248935 scopus 로고    scopus 로고
    • Potential therapeutic agents against Alzheimer's disease from natural sources
    • Park S.Y. Potential therapeutic agents against Alzheimer's disease from natural sources. Archives of Pharmacal Research 2010, 33:1589-1609.
    • (2010) Archives of Pharmacal Research , vol.33 , pp. 1589-1609
    • Park, S.Y.1
  • 29
    • 33847012626 scopus 로고    scopus 로고
    • Human islet amyloid polypeptide oligomers disrupt cell coupling, induce apoptosis, and impair insulin secretion in isolated human islets
    • 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.
    • (2007) Diabetes , vol.56 , pp. 65-71
    • Ritzel, R.A.1    Meier, J.J.2    Lin, C.Y.3    Veldhuis, J.D.4    Butler, P.C.5
  • 30
    • 34249279788 scopus 로고    scopus 로고
    • Beneficial effects of fruit extracts on neuronal function and behavior in a rodent model of accelerated aging
    • Shukitt-Hale B., Carey A.N., Jenkins D., Rabin B.M., Joseph J.A. Beneficial effects of fruit extracts on neuronal function and behavior in a rodent model of accelerated aging. Neurobiology of Aging 2007, 28:1187-1194.
    • (2007) Neurobiology of Aging , vol.28 , pp. 1187-1194
    • Shukitt-Hale, B.1    Carey, A.N.2    Jenkins, D.3    Rabin, B.M.4    Joseph, J.A.5
  • 31
    • 70149116768 scopus 로고    scopus 로고
    • Association of highly compact type II diabetes related islet amyloid polypeptide intermediate species at physiological temperature revealed by diffusion NMR spectroscopy
    • Soong R., Brender J.R., Macdonald P.M., Ramamoorthy A. Association of highly compact type II diabetes related islet amyloid polypeptide intermediate species at physiological temperature revealed by diffusion NMR spectroscopy. Journal of the American Chemical Society 2009, 131:7079-7085.
    • (2009) Journal of the American Chemical Society , vol.131 , pp. 7079-7085
    • Soong, R.1    Brender, J.R.2    Macdonald, P.M.3    Ramamoorthy, A.4
  • 32
    • 84867488912 scopus 로고    scopus 로고
    • Alternative pathways of human islet amyloid polypeptide aggregation distinguished by (19)f nuclear magnetic resonance-detected kinetics of monomer consumption
    • Suzuki Y., Brender J.R., Hartman K., Ramamoorthy A., Marsh E.N. Alternative pathways of human islet amyloid polypeptide aggregation distinguished by (19)f nuclear magnetic resonance-detected kinetics of monomer consumption. Biochemistry 2012, 51:8154-8162.
    • (2012) Biochemistry , vol.51 , pp. 8154-8162
    • Suzuki, Y.1    Brender, J.R.2    Hartman, K.3    Ramamoorthy, A.4    Marsh, E.N.5
  • 33
    • 33746883879 scopus 로고    scopus 로고
    • Determination of total phenolic and flavonoid contents in selected fruits and vegetables, as well as their stimulatory effects on mouse splenocyte proliferation
    • Tang J.L.A.C. Determination of total phenolic and flavonoid contents in selected fruits and vegetables, as well as their stimulatory effects on mouse splenocyte proliferation. Food Chemistry 2007, 101:140-147.
    • (2007) Food Chemistry , vol.101 , pp. 140-147
    • Tang, J.L.A.C.1
  • 34
    • 84920734429 scopus 로고    scopus 로고
    • Type 2 Diabetes Facts and Figs, American Diabetes Association.
    • Type 2 Diabetes Facts and Figs. (2011). American Diabetes Association.
    • (2011)
  • 35
    • 54249154215 scopus 로고    scopus 로고
    • Blueberry opposes beta-amyloid peptide-induced microglial activation via inhibition of p44/42 mitogen-activation protein kinase
    • Zhu Y., Bickford P.C., Sanberg P., Giunta B., Tan J. Blueberry opposes beta-amyloid peptide-induced microglial activation via inhibition of p44/42 mitogen-activation protein kinase. Rejuvenation Research 2008, 11:891-901.
    • (2008) Rejuvenation Research , vol.11 , pp. 891-901
    • Zhu, Y.1    Bickford, P.C.2    Sanberg, P.3    Giunta, B.4    Tan, J.5
  • 36
    • 77955654198 scopus 로고    scopus 로고
    • Berry fruit extracts inhibit growth and induce apoptosis of high-risk acute lymphoblastic leukemia cells in vitro
    • Zunino S.J., Zhang Y.J., Seeram N.P., Storms D.H. Berry fruit extracts inhibit growth and induce apoptosis of high-risk acute lymphoblastic leukemia cells in vitro. Journal of Functional Foods 2010, 2:187-195.
    • (2010) Journal of Functional Foods , vol.2 , pp. 187-195
    • Zunino, S.J.1    Zhang, Y.J.2    Seeram, N.P.3    Storms, D.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.