...
首页> 外文期刊>Biochimica et biophysica acta. Biomembranes >Membrane interaction of islet amyloid polypeptide
【24h】

Membrane interaction of islet amyloid polypeptide

机译:胰岛淀粉样多肽的膜相互作用

获取原文
获取原文并翻译 | 示例

摘要

Increasing evidence suggests that the misfolding and deposition of IAPP plays an important role in the pathogenesis of type II, 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.
机译:越来越多的证据表明,IAPP的错误折叠和沉积在II型或非胰岛素依赖型糖尿病(T2DM)的发病机理中起着重要作用。膜已通过多种方式牵涉IAPP依赖性毒性:脂质膜已显示出可促进IAPP的错误折叠和聚集。因此,当IAPP与细胞膜相互作用时,可能会产生潜在毒性形式的IAPP。此外,膜被认为是IAPP毒性的靶标。 IAPP已显示破坏膜的完整性并透化膜。由于细胞膜的破坏是高度毒性的,因此已经提出了这种机制来解释所观察到的IAPP毒性。在这里,我们审查(1)催化IAPP错折叠和(2)是IAPP毒性的潜在来源的背景下IAPP膜相互作用。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号