Rutin suppresses human-amylin/hIAPP misfolding and oligomer formation in-vitro, and ameliorates diabetes and its impacts in human-amylin/hIAPP transgenic mice
Pancreatic islet β-cells secrete the hormones insulin and amylin, and defective β-cell function plays a central role in the pathogenesis of type-2 diabetes (T2D). Human amylin (hA, also termed hIAPP) misfolds and forms amyloid aggregates whereas orthologous mouse amylin does neither. Furthermore, hA...
Ausführliche Beschreibung
Autor*in: |
Aitken, Jacqueline F. [verfasserIn] |
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Englisch |
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2017transfer abstract |
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7 |
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Enthalten in: Preparation and characterization of glass-ceramics via co-sintering of coal fly ash and oil shale ash-derived amorphous slag - Zhang, Zhikun ELSEVIER, 2019, BBRC, Orlando, Fla |
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Übergeordnetes Werk: |
volume:482 ; year:2017 ; number:4 ; day:22 ; month:01 ; pages:625-631 ; extent:7 |
Links: |
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DOI / URN: |
10.1016/j.bbrc.2016.11.083 |
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520 | |a Pancreatic islet β-cells secrete the hormones insulin and amylin, and defective β-cell function plays a central role in the pathogenesis of type-2 diabetes (T2D). Human amylin (hA, also termed hIAPP) misfolds and forms amyloid aggregates whereas orthologous mouse amylin does neither. Furthermore, hA elicits apoptosis in cultured β-cells and β-cell death in ex-vivo islets. In addition, hA-transgenic mice that selectively express hA in their β-cells, manifest β-cell apoptosis and progressive islet damage that leads to diabetes closely resembling that in patients with T2D. Aggregation of hA is thus linked to the causation of diabetes. | ||
650 | 7 | |a Type-2 diabetes |2 Elsevier | |
650 | 7 | |a Ion-mobility mass-spectrometry |2 Elsevier | |
650 | 7 | |a Amylin |2 Elsevier | |
650 | 7 | |a Transgenic mice |2 Elsevier | |
650 | 7 | |a Rutin |2 Elsevier | |
700 | 1 | |a Loomes, Kerry M. |4 oth | |
700 | 1 | |a Riba-Garcia, Isabel |4 oth | |
700 | 1 | |a Unwin, Richard D. |4 oth | |
700 | 1 | |a Prijic, Gordana |4 oth | |
700 | 1 | |a Phillips, Ashley S. |4 oth | |
700 | 1 | |a Phillips, Anthony R.J. |4 oth | |
700 | 1 | |a Wu, Donghai |4 oth | |
700 | 1 | |a Poppitt, Sally D. |4 oth | |
700 | 1 | |a Ding, Ke |4 oth | |
700 | 1 | |a Barran, Perdita E. |4 oth | |
700 | 1 | |a Dowsey, Andrew W. |4 oth | |
700 | 1 | |a Cooper, Garth J.S. |4 oth | |
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10.1016/j.bbrc.2016.11.083 doi GBV00000000000101A.pica (DE-627)ELV01542801X (ELSEVIER)S0006-291X(16)31946-5 DE-627 ger DE-627 rakwb eng 570 570 DE-600 670 VZ 51.60 bkl 58.45 bkl Aitken, Jacqueline F. verfasserin aut Rutin suppresses human-amylin/hIAPP misfolding and oligomer formation in-vitro, and ameliorates diabetes and its impacts in human-amylin/hIAPP transgenic mice 2017transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Pancreatic islet β-cells secrete the hormones insulin and amylin, and defective β-cell function plays a central role in the pathogenesis of type-2 diabetes (T2D). Human amylin (hA, also termed hIAPP) misfolds and forms amyloid aggregates whereas orthologous mouse amylin does neither. Furthermore, hA elicits apoptosis in cultured β-cells and β-cell death in ex-vivo islets. In addition, hA-transgenic mice that selectively express hA in their β-cells, manifest β-cell apoptosis and progressive islet damage that leads to diabetes closely resembling that in patients with T2D. Aggregation of hA is thus linked to the causation of diabetes. Pancreatic islet β-cells secrete the hormones insulin and amylin, and defective β-cell function plays a central role in the pathogenesis of type-2 diabetes (T2D). Human amylin (hA, also termed hIAPP) misfolds and forms amyloid aggregates whereas orthologous mouse amylin does neither. Furthermore, hA elicits apoptosis in cultured β-cells and β-cell death in ex-vivo islets. In addition, hA-transgenic mice that selectively express hA in their β-cells, manifest β-cell apoptosis and progressive islet damage that leads to diabetes closely resembling that in patients with T2D. Aggregation of hA is thus linked to the causation of diabetes. Type-2 diabetes Elsevier Ion-mobility mass-spectrometry Elsevier Amylin Elsevier Transgenic mice Elsevier Rutin Elsevier Loomes, Kerry M. oth Riba-Garcia, Isabel oth Unwin, Richard D. oth Prijic, Gordana oth Phillips, Ashley S. oth Phillips, Anthony R.J. oth Wu, Donghai oth Poppitt, Sally D. oth Ding, Ke oth Barran, Perdita E. oth Dowsey, Andrew W. oth Cooper, Garth J.S. oth Enthalten in Academic Press Zhang, Zhikun ELSEVIER Preparation and characterization of glass-ceramics via co-sintering of coal fly ash and oil shale ash-derived amorphous slag 2019 BBRC Orlando, Fla (DE-627)ELV002811154 volume:482 year:2017 number:4 day:22 month:01 pages:625-631 extent:7 https://doi.org/10.1016/j.bbrc.2016.11.083 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 51.60 Keramische Werkstoffe Hartstoffe Werkstoffkunde VZ 58.45 Gesteinshüttenkunde VZ AR 482 2017 4 22 0122 625-631 7 045F 570 |
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10.1016/j.bbrc.2016.11.083 doi GBV00000000000101A.pica (DE-627)ELV01542801X (ELSEVIER)S0006-291X(16)31946-5 DE-627 ger DE-627 rakwb eng 570 570 DE-600 670 VZ 51.60 bkl 58.45 bkl Aitken, Jacqueline F. verfasserin aut Rutin suppresses human-amylin/hIAPP misfolding and oligomer formation in-vitro, and ameliorates diabetes and its impacts in human-amylin/hIAPP transgenic mice 2017transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Pancreatic islet β-cells secrete the hormones insulin and amylin, and defective β-cell function plays a central role in the pathogenesis of type-2 diabetes (T2D). Human amylin (hA, also termed hIAPP) misfolds and forms amyloid aggregates whereas orthologous mouse amylin does neither. Furthermore, hA elicits apoptosis in cultured β-cells and β-cell death in ex-vivo islets. In addition, hA-transgenic mice that selectively express hA in their β-cells, manifest β-cell apoptosis and progressive islet damage that leads to diabetes closely resembling that in patients with T2D. Aggregation of hA is thus linked to the causation of diabetes. Pancreatic islet β-cells secrete the hormones insulin and amylin, and defective β-cell function plays a central role in the pathogenesis of type-2 diabetes (T2D). Human amylin (hA, also termed hIAPP) misfolds and forms amyloid aggregates whereas orthologous mouse amylin does neither. Furthermore, hA elicits apoptosis in cultured β-cells and β-cell death in ex-vivo islets. In addition, hA-transgenic mice that selectively express hA in their β-cells, manifest β-cell apoptosis and progressive islet damage that leads to diabetes closely resembling that in patients with T2D. Aggregation of hA is thus linked to the causation of diabetes. Type-2 diabetes Elsevier Ion-mobility mass-spectrometry Elsevier Amylin Elsevier Transgenic mice Elsevier Rutin Elsevier Loomes, Kerry M. oth Riba-Garcia, Isabel oth Unwin, Richard D. oth Prijic, Gordana oth Phillips, Ashley S. oth Phillips, Anthony R.J. oth Wu, Donghai oth Poppitt, Sally D. oth Ding, Ke oth Barran, Perdita E. oth Dowsey, Andrew W. oth Cooper, Garth J.S. oth Enthalten in Academic Press Zhang, Zhikun ELSEVIER Preparation and characterization of glass-ceramics via co-sintering of coal fly ash and oil shale ash-derived amorphous slag 2019 BBRC Orlando, Fla (DE-627)ELV002811154 volume:482 year:2017 number:4 day:22 month:01 pages:625-631 extent:7 https://doi.org/10.1016/j.bbrc.2016.11.083 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 51.60 Keramische Werkstoffe Hartstoffe Werkstoffkunde VZ 58.45 Gesteinshüttenkunde VZ AR 482 2017 4 22 0122 625-631 7 045F 570 |
allfields_unstemmed |
10.1016/j.bbrc.2016.11.083 doi GBV00000000000101A.pica (DE-627)ELV01542801X (ELSEVIER)S0006-291X(16)31946-5 DE-627 ger DE-627 rakwb eng 570 570 DE-600 670 VZ 51.60 bkl 58.45 bkl Aitken, Jacqueline F. verfasserin aut Rutin suppresses human-amylin/hIAPP misfolding and oligomer formation in-vitro, and ameliorates diabetes and its impacts in human-amylin/hIAPP transgenic mice 2017transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Pancreatic islet β-cells secrete the hormones insulin and amylin, and defective β-cell function plays a central role in the pathogenesis of type-2 diabetes (T2D). Human amylin (hA, also termed hIAPP) misfolds and forms amyloid aggregates whereas orthologous mouse amylin does neither. Furthermore, hA elicits apoptosis in cultured β-cells and β-cell death in ex-vivo islets. In addition, hA-transgenic mice that selectively express hA in their β-cells, manifest β-cell apoptosis and progressive islet damage that leads to diabetes closely resembling that in patients with T2D. Aggregation of hA is thus linked to the causation of diabetes. Pancreatic islet β-cells secrete the hormones insulin and amylin, and defective β-cell function plays a central role in the pathogenesis of type-2 diabetes (T2D). Human amylin (hA, also termed hIAPP) misfolds and forms amyloid aggregates whereas orthologous mouse amylin does neither. Furthermore, hA elicits apoptosis in cultured β-cells and β-cell death in ex-vivo islets. In addition, hA-transgenic mice that selectively express hA in their β-cells, manifest β-cell apoptosis and progressive islet damage that leads to diabetes closely resembling that in patients with T2D. Aggregation of hA is thus linked to the causation of diabetes. Type-2 diabetes Elsevier Ion-mobility mass-spectrometry Elsevier Amylin Elsevier Transgenic mice Elsevier Rutin Elsevier Loomes, Kerry M. oth Riba-Garcia, Isabel oth Unwin, Richard D. oth Prijic, Gordana oth Phillips, Ashley S. oth Phillips, Anthony R.J. oth Wu, Donghai oth Poppitt, Sally D. oth Ding, Ke oth Barran, Perdita E. oth Dowsey, Andrew W. oth Cooper, Garth J.S. oth Enthalten in Academic Press Zhang, Zhikun ELSEVIER Preparation and characterization of glass-ceramics via co-sintering of coal fly ash and oil shale ash-derived amorphous slag 2019 BBRC Orlando, Fla (DE-627)ELV002811154 volume:482 year:2017 number:4 day:22 month:01 pages:625-631 extent:7 https://doi.org/10.1016/j.bbrc.2016.11.083 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 51.60 Keramische Werkstoffe Hartstoffe Werkstoffkunde VZ 58.45 Gesteinshüttenkunde VZ AR 482 2017 4 22 0122 625-631 7 045F 570 |
allfieldsGer |
10.1016/j.bbrc.2016.11.083 doi GBV00000000000101A.pica (DE-627)ELV01542801X (ELSEVIER)S0006-291X(16)31946-5 DE-627 ger DE-627 rakwb eng 570 570 DE-600 670 VZ 51.60 bkl 58.45 bkl Aitken, Jacqueline F. verfasserin aut Rutin suppresses human-amylin/hIAPP misfolding and oligomer formation in-vitro, and ameliorates diabetes and its impacts in human-amylin/hIAPP transgenic mice 2017transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Pancreatic islet β-cells secrete the hormones insulin and amylin, and defective β-cell function plays a central role in the pathogenesis of type-2 diabetes (T2D). Human amylin (hA, also termed hIAPP) misfolds and forms amyloid aggregates whereas orthologous mouse amylin does neither. Furthermore, hA elicits apoptosis in cultured β-cells and β-cell death in ex-vivo islets. In addition, hA-transgenic mice that selectively express hA in their β-cells, manifest β-cell apoptosis and progressive islet damage that leads to diabetes closely resembling that in patients with T2D. Aggregation of hA is thus linked to the causation of diabetes. Pancreatic islet β-cells secrete the hormones insulin and amylin, and defective β-cell function plays a central role in the pathogenesis of type-2 diabetes (T2D). Human amylin (hA, also termed hIAPP) misfolds and forms amyloid aggregates whereas orthologous mouse amylin does neither. Furthermore, hA elicits apoptosis in cultured β-cells and β-cell death in ex-vivo islets. In addition, hA-transgenic mice that selectively express hA in their β-cells, manifest β-cell apoptosis and progressive islet damage that leads to diabetes closely resembling that in patients with T2D. Aggregation of hA is thus linked to the causation of diabetes. Type-2 diabetes Elsevier Ion-mobility mass-spectrometry Elsevier Amylin Elsevier Transgenic mice Elsevier Rutin Elsevier Loomes, Kerry M. oth Riba-Garcia, Isabel oth Unwin, Richard D. oth Prijic, Gordana oth Phillips, Ashley S. oth Phillips, Anthony R.J. oth Wu, Donghai oth Poppitt, Sally D. oth Ding, Ke oth Barran, Perdita E. oth Dowsey, Andrew W. oth Cooper, Garth J.S. oth Enthalten in Academic Press Zhang, Zhikun ELSEVIER Preparation and characterization of glass-ceramics via co-sintering of coal fly ash and oil shale ash-derived amorphous slag 2019 BBRC Orlando, Fla (DE-627)ELV002811154 volume:482 year:2017 number:4 day:22 month:01 pages:625-631 extent:7 https://doi.org/10.1016/j.bbrc.2016.11.083 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 51.60 Keramische Werkstoffe Hartstoffe Werkstoffkunde VZ 58.45 Gesteinshüttenkunde VZ AR 482 2017 4 22 0122 625-631 7 045F 570 |
allfieldsSound |
10.1016/j.bbrc.2016.11.083 doi GBV00000000000101A.pica (DE-627)ELV01542801X (ELSEVIER)S0006-291X(16)31946-5 DE-627 ger DE-627 rakwb eng 570 570 DE-600 670 VZ 51.60 bkl 58.45 bkl Aitken, Jacqueline F. verfasserin aut Rutin suppresses human-amylin/hIAPP misfolding and oligomer formation in-vitro, and ameliorates diabetes and its impacts in human-amylin/hIAPP transgenic mice 2017transfer abstract 7 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Pancreatic islet β-cells secrete the hormones insulin and amylin, and defective β-cell function plays a central role in the pathogenesis of type-2 diabetes (T2D). Human amylin (hA, also termed hIAPP) misfolds and forms amyloid aggregates whereas orthologous mouse amylin does neither. Furthermore, hA elicits apoptosis in cultured β-cells and β-cell death in ex-vivo islets. In addition, hA-transgenic mice that selectively express hA in their β-cells, manifest β-cell apoptosis and progressive islet damage that leads to diabetes closely resembling that in patients with T2D. Aggregation of hA is thus linked to the causation of diabetes. Pancreatic islet β-cells secrete the hormones insulin and amylin, and defective β-cell function plays a central role in the pathogenesis of type-2 diabetes (T2D). Human amylin (hA, also termed hIAPP) misfolds and forms amyloid aggregates whereas orthologous mouse amylin does neither. Furthermore, hA elicits apoptosis in cultured β-cells and β-cell death in ex-vivo islets. In addition, hA-transgenic mice that selectively express hA in their β-cells, manifest β-cell apoptosis and progressive islet damage that leads to diabetes closely resembling that in patients with T2D. Aggregation of hA is thus linked to the causation of diabetes. Type-2 diabetes Elsevier Ion-mobility mass-spectrometry Elsevier Amylin Elsevier Transgenic mice Elsevier Rutin Elsevier Loomes, Kerry M. oth Riba-Garcia, Isabel oth Unwin, Richard D. oth Prijic, Gordana oth Phillips, Ashley S. oth Phillips, Anthony R.J. oth Wu, Donghai oth Poppitt, Sally D. oth Ding, Ke oth Barran, Perdita E. oth Dowsey, Andrew W. oth Cooper, Garth J.S. oth Enthalten in Academic Press Zhang, Zhikun ELSEVIER Preparation and characterization of glass-ceramics via co-sintering of coal fly ash and oil shale ash-derived amorphous slag 2019 BBRC Orlando, Fla (DE-627)ELV002811154 volume:482 year:2017 number:4 day:22 month:01 pages:625-631 extent:7 https://doi.org/10.1016/j.bbrc.2016.11.083 Volltext GBV_USEFLAG_U GBV_ELV SYSFLAG_U 51.60 Keramische Werkstoffe Hartstoffe Werkstoffkunde VZ 58.45 Gesteinshüttenkunde VZ AR 482 2017 4 22 0122 625-631 7 045F 570 |
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Enthalten in Preparation and characterization of glass-ceramics via co-sintering of coal fly ash and oil shale ash-derived amorphous slag Orlando, Fla volume:482 year:2017 number:4 day:22 month:01 pages:625-631 extent:7 |
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Preparation and characterization of glass-ceramics via co-sintering of coal fly ash and oil shale ash-derived amorphous slag |
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Rutin suppresses human-amylin/hIAPP misfolding and oligomer formation in-vitro, and ameliorates diabetes and its impacts in human-amylin/hIAPP transgenic mice |
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Rutin suppresses human-amylin/hIAPP misfolding and oligomer formation in-vitro, and ameliorates diabetes and its impacts in human-amylin/hIAPP transgenic mice |
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Preparation and characterization of glass-ceramics via co-sintering of coal fly ash and oil shale ash-derived amorphous slag |
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rutin suppresses human-amylin/hiapp misfolding and oligomer formation in-vitro, and ameliorates diabetes and its impacts in human-amylin/hiapp transgenic mice |
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Rutin suppresses human-amylin/hIAPP misfolding and oligomer formation in-vitro, and ameliorates diabetes and its impacts in human-amylin/hIAPP transgenic mice |
abstract |
Pancreatic islet β-cells secrete the hormones insulin and amylin, and defective β-cell function plays a central role in the pathogenesis of type-2 diabetes (T2D). Human amylin (hA, also termed hIAPP) misfolds and forms amyloid aggregates whereas orthologous mouse amylin does neither. Furthermore, hA elicits apoptosis in cultured β-cells and β-cell death in ex-vivo islets. In addition, hA-transgenic mice that selectively express hA in their β-cells, manifest β-cell apoptosis and progressive islet damage that leads to diabetes closely resembling that in patients with T2D. Aggregation of hA is thus linked to the causation of diabetes. |
abstractGer |
Pancreatic islet β-cells secrete the hormones insulin and amylin, and defective β-cell function plays a central role in the pathogenesis of type-2 diabetes (T2D). Human amylin (hA, also termed hIAPP) misfolds and forms amyloid aggregates whereas orthologous mouse amylin does neither. Furthermore, hA elicits apoptosis in cultured β-cells and β-cell death in ex-vivo islets. In addition, hA-transgenic mice that selectively express hA in their β-cells, manifest β-cell apoptosis and progressive islet damage that leads to diabetes closely resembling that in patients with T2D. Aggregation of hA is thus linked to the causation of diabetes. |
abstract_unstemmed |
Pancreatic islet β-cells secrete the hormones insulin and amylin, and defective β-cell function plays a central role in the pathogenesis of type-2 diabetes (T2D). Human amylin (hA, also termed hIAPP) misfolds and forms amyloid aggregates whereas orthologous mouse amylin does neither. Furthermore, hA elicits apoptosis in cultured β-cells and β-cell death in ex-vivo islets. In addition, hA-transgenic mice that selectively express hA in their β-cells, manifest β-cell apoptosis and progressive islet damage that leads to diabetes closely resembling that in patients with T2D. Aggregation of hA is thus linked to the causation of diabetes. |
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Rutin suppresses human-amylin/hIAPP misfolding and oligomer formation in-vitro, and ameliorates diabetes and its impacts in human-amylin/hIAPP transgenic mice |
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https://doi.org/10.1016/j.bbrc.2016.11.083 |
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Loomes, Kerry M. Riba-Garcia, Isabel Unwin, Richard D. Prijic, Gordana Phillips, Ashley S. Phillips, Anthony R.J. Wu, Donghai Poppitt, Sally D. Ding, Ke Barran, Perdita E. Dowsey, Andrew W. Cooper, Garth J.S. |
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