老年斑
热休克蛋白
脑淀粉样血管病
热休克蛋白27
病理
发病机制
病态的
免疫组织化学
阿尔茨海默病
细胞外
生物
淀粉样蛋白(真菌学)
热休克蛋白70
医学
疾病
细胞生物学
生物化学
痴呆
基因
作者
Micha M.M. Wilhelmus,Irene Otte‐Höller,Pieter Wesseling,Robert M.W. de Waal,Wilbert C. Boelens,Marcel M. Verbeek
标识
DOI:10.1111/j.1365-2990.2006.00689.x
摘要
The small heat shock protein family (sHsp) comprises molecular chaperones able to interact with incorrectly folded proteins. Alzheimer's disease (AD) is characterized by pathological lesions such as senile plaques (SPs), cerebral amyloid angiopathy (CAA) and neurofibrillary tangles (NFTs), predominantly consisting of the incorrectly folded proteins amyloid‐β (Aβ) and tau respectively. The aim of this study was to investigate the association of the chaperones Hsp20, HspB2, αB‐crystallin and Hsp27 with the pathological lesions of AD brains. For this purpose, a panel of well‐characterized antibodies directed against these sHsps was used in immunohistochemistry and immunoblotting. We observed extracellular expression of Hsp20, Hsp27 and HspB2 in classic SPs, and Hsp20 expression in diffuse SPs. In addition, extracellular expression of HspB2 was observed in CAA. Both Hsp27 and αB‐crystallin were also observed in astrocytes associated with both SPs and CAA. Furthermore, none of the sHsps were observed in NFTs in AD brains. We conclude that specific sHsp species may be involved in the pathogenesis of either SPs or CAA in AD.
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