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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• 作者：Jacqueline F. Aitken^a ; Kerry M. Loomes^a ; ^b ; Isabel Riba-Garcia^d ; Richard D. Unwin^d ; Gordana Prijic^a ; Ashley S. Phillips^e ; Anthony R.J. Phillips^a ; ^b ; ^c ; Donghai Wu^f ; ^g ; Sally D. Poppitt^a ; Ke Ding^h ; Perdita E. Barran^e ; Andrew W. Dowsey^d ; ⁱ ; ¹ ; Garth J.S. Cooper^a ; ^b ; ^d ; ¹ ; ^{g.cooper@auckland.ac.nz}
• 关键词：Amylin ; Rutin ; Ion-mobility mass-spectrometry ; Transgenic mice ; Type-2 diabetes
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2017
• 出版时间：22 January 2017
• 年：2017
• 卷：482
• 期：4
• 页码：625-631
• 全文大小：951 K
• 卷排序：482

文摘

Defective islet beta-cell function is central to the causation of type 2 diabetes. Human amylin aggregation is closely linked to the mechanism of β-cell death. Rutin bound to amylin suppressed misfolding, and disaggregated amylin oligomers. Rutin markedly delays diabetes progression with doubling of lifespan in mice.