期刊
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
卷 1768, 期 8, 页码 2002-2009出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamem.2007.01.022
关键词
islet amyloid polypeptide; IAPP; membranes; aggregation; membrane damage
资金
- NIA NIH HHS [AG027936] Funding Source: Medline
Increasing evidence suggests that the misfolding and deposition of IAPP plays an important role in the pathogenesis of type 11, or non-insulin-dependent diabetes mellitus (T2DM). Membranes have been implicated in IAPP-dependent toxicity in several ways: Lipid membranes have been shown to promote the misfolding and aggregation of IAPP. Thus, potentially toxic forms of IAPP can be generated when IAPP interacts with cellular membranes. In addition, membranes have been implicated as the target of IAPP toxicity. IAPP has been shown to disrupt membrane integrity and to permeabilize membranes. Since disruption of cellular membranes is highly toxic, such a mechanism has been suggested to explain the observed IAPP toxicity. Here, we review IAPP-membrane interaction in the context of (1) catalyzing IAPP misfolding and (2) being a potential origin of IAPP toxicity. (c) 2007 Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据