In vitro inhibition of transthyretin aggregate-induced cytotoxicity by full and peptide derived forms of the soluble receptor for advanced glycation end products (RAGE)
In vitro inhibition of transthyretin aggregate-induced cytotoxicity by full and peptide derived forms of the soluble receptor for advanced glycation end products (RAGE)
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DOI：
10.1016/j.febslet.2006.05.020
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发表时间：
2006-06-12
期刊：
影响因子：
3.5
通讯作者：
Saraiva, Maria Joao
中科院分区：
文献类型：
--
作者：
Monteiro, Filipe Almeida;Cardoso, Isabel;Saraiva, Maria Joao
家族性淀粉样变性多发性神经病是一种神经退行性疾病，其特征是全身性细胞外跨甲状腺激素(TTR)淀粉样纤维沉积。后者被认为通过参与晚期糖基化终产物受体(RAGE)而触发神经退行性变。在这里，我们证明了TTR与RAGE的相互作用在小鼠和人类物种中是保守的，并且不依赖于RAGE的糖基化。此外，TTR结构的D链似乎对TTR-RAGE的相互作用以及位于V-结构域的RAGE中的一个基序(102-118残基)很重要；该基序在细胞培养中抑制了TTR聚集体诱导的细胞毒性。(C)2006年欧洲生化学会联合会。爱思唯尔出版，版权所有。
Familial amyloidotic polyneuropathy is a neurodegenerative disorder characterized by systemic extracellular deposition of transthyretin (TTR) amyloid fibrils. The latter have been proposed to trigger neurodegeneration through engagement of the receptor for advanced glycation end products (RAGE). Here we show that TTR interaction with RAGE is conserved across mouse and human species and is not dependent on RAGE glycosylation. Moreover, strand D of TTR structure seems important for the TTR-RAGE interaction as well as a motif in RAGE (residues 102-118) located within the V-domain; this motif suppressed TTR aggregate-induced cytotoxicity in cell culture. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.