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本文引用的文献

1
Autophagy protects against human islet amyloid polypeptide-associated apoptosis.自噬可防止人胰岛淀粉样多肽相关凋亡。
J Diabetes Investig. 2011 Jan 24;2(1):48-55. doi: 10.1111/j.2040-1124.2010.00065.x.
2
Ionic strength effects on amyloid formation by amylin are a complicated interplay among Debye screening, ion selectivity, and Hofmeister effects.离子强度对胰岛淀粉样肽形成的影响是 Debye 屏蔽、离子选择性和Hofmeister 效应之间复杂的相互作用。
Biochemistry. 2012 Oct 30;51(43):8478-90. doi: 10.1021/bi300574r. Epub 2012 Oct 16.
3
Metabolic stress, IAPP and islet amyloid.代谢应激、IAPP 和胰岛淀粉样变。
Diabetes Obes Metab. 2012 Oct;14 Suppl 3:68-77. doi: 10.1111/j.1463-1326.2012.01657.x.
4
Deamidation accelerates amyloid formation and alters amylin fiber structure.脱酰胺加速了淀粉样蛋白的形成并改变了胰岛淀粉样多肽纤维的结构。
J Am Chem Soc. 2012 Aug 1;134(30):12658-67. doi: 10.1021/ja3039486. Epub 2012 Jul 17.
5
Diabetes mellitus and the β cell: the last ten years.糖尿病与β细胞:近十年的研究进展。
Cell. 2012 Mar 16;148(6):1160-71. doi: 10.1016/j.cell.2012.02.010.
6
The effect of Aβ on IAPP aggregation in the presence of an isolated β-cell membrane.Aβ 对分离胰岛β细胞膜中 IAPP 聚集的影响。
J Mol Biol. 2012 Aug 10;421(2-3):348-63. doi: 10.1016/j.jmb.2012.01.048. Epub 2012 Feb 1.
7
Deletion of Fas protects islet beta cells from cytotoxic effects of human islet amyloid polypeptide.Fas基因的缺失可保护胰岛β细胞免受人胰岛淀粉样多肽的细胞毒性作用。
Diabetologia. 2012 Feb 1. doi: 10.1007/s00125-012-2451-2.
8
The transthyretin amyloidoses: from delineating the molecular mechanism of aggregation linked to pathology to a regulatory-agency-approved drug.转甲状腺素淀粉样变性:从阐明与病理学相关的聚集分子机制到获得监管机构批准的药物。
J Mol Biol. 2012 Aug 10;421(2-3):185-203. doi: 10.1016/j.jmb.2011.12.060. Epub 2012 Jan 5.
9
Sensitivity of amyloid formation by human islet amyloid polypeptide to mutations at residue 20.人胰岛淀粉样多肽 20 位残基突变对淀粉样形成的敏感性。
J Mol Biol. 2012 Aug 10;421(2-3):282-95. doi: 10.1016/j.jmb.2011.12.032. Epub 2011 Dec 21.
10
Control of energy homeostasis by amylin.胰岛淀粉样多肽对能量平衡的调控。
Cell Mol Life Sci. 2012 Jun;69(12):1947-65. doi: 10.1007/s00018-011-0905-1. Epub 2011 Dec 23.

2 型糖尿病胰岛淀粉样变性毒性的机制。

Mechanisms of islet amyloidosis toxicity in type 2 diabetes.

机构信息

Diabetes Research Program, Division of Endocrinology, Department of Medicine, New York University Medical Center, 550 First Avenue, Smilow 906, New York, NY 10016, USA.

出版信息

FEBS Lett. 2013 Apr 17;587(8):1119-27. doi: 10.1016/j.febslet.2013.01.017. Epub 2013 Jan 18.

DOI:10.1016/j.febslet.2013.01.017
PMID:23337872
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4557799/
Abstract

Amyloid formation by the neuropancreatic hormone, islet amyloid polypeptide (IAPP or amylin), one of the most amyloidogenic sequences known, leads to islet amyloidosis in type 2 diabetes and to islet transplant failure. Under normal conditions, IAPP plays a role in the maintenance of energy homeostasis by regulating several metabolic parameters, such as satiety, blood glucose levels, adiposity and body weight. The mechanisms of IAPP amyloid formation, the nature of IAPP toxic species and the cellular pathways that lead to pancreatic β-cell toxicity are not well characterized. Several mechanisms of toxicity, including receptor and non-receptor-mediated events, have been proposed. Analogs of IAPP have been approved for the treatment of diabetes and are under investigation for the treatment of obesity.

摘要

神经胰腺激素、胰岛淀粉样多肽(IAPP 或胰岛淀粉样肽)的淀粉样形成,是已知最具淀粉样变性的序列之一,导致 2 型糖尿病的胰岛淀粉样变和胰岛移植失败。在正常情况下,IAPP 通过调节饱腹感、血糖水平、肥胖和体重等多种代谢参数,在维持能量平衡方面发挥作用。IAPP 淀粉样形成的机制、IAPP 毒性物质的性质以及导致胰腺β细胞毒性的细胞途径尚未得到很好的描述。已经提出了几种毒性机制,包括受体和非受体介导的事件。IAPP 的类似物已被批准用于治疗糖尿病,并正在研究用于治疗肥胖症。