Literature DB >> 22366091

Silibinin inhibits the toxic aggregation of human islet amyloid polypeptide.

Biao Cheng1, Hao Gong, Xiaochao Li, Yue Sun, Xin Zhang, Hong Chen, Xinran Liu, Ling Zheng, Kun Huang.   

Abstract

In type 2 diabetes mellitus (T2DM), misfolded human islet amyloid polypeptide (hIAPP) forms amyloid deposits in pancreatic islets. These amyloid deposits contribute to the dysfunction of β-cells and the loss of β-cell mass in T2DM patients. Inhibition of hIAPP fibrillization has been regarded as a potential therapeutic approach for T2DM. Silibinin, a major active flavonoid extracted from herb milk thistle (Silybum marianum), has been used for centuries to treat diabetes in Asia and Europe with unclear mechanisms. In this study, we tested whether silibinin has any effect on the amyloidogenicity of hIAPP. Our results provide first evidence that silibinin inhibits hIAPP fibrillization via suppressing the toxic oligomerization of hIAPP and enhances the viability of pancreatic β-cells, therefore silibinin may serve as a potential therapeutic agent for T2DM. Copyright Â
© 2012 Elsevier Inc. All rights reserved.

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Year:  2012        PMID: 22366091     DOI: 10.1016/j.bbrc.2012.02.042

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  23 in total

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7.  Bisphenol A accelerates toxic amyloid formation of human islet amyloid polypeptide: a possible link between bisphenol A exposure and type 2 diabetes.

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9.  Silymarin effect on amyloid-β plaque accumulation and gene expression of APP in an Alzheimer's disease rat model.

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10.  Ion mobility spectrometry-mass spectrometry defines the oligomeric intermediates in amylin amyloid formation and the mode of action of inhibitors.

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