Li Dan's research group and collaborators at Shanghai Jiaotong University explained the molecular mechanism of Hsp27 inhibiting pathological aggregation and toxicity of pTau in Alzheimer's disease

Alzheimer's disease (AD) as the most common neurodegenerative disease, the current global confirmed patients have exceeded 50 million, there is no specific drug, which seriously affects human life and health (especially the elderly over 65 years old).

On September 1, 2022, li dan's research group at the Bio-X Research Institute of Shanghai Jiao Tong University, in collaboration with Grace Zhai and other research groups at the University of Miami, published a research paper entitled "Specific binding of Hsp27 and phosphorylated Tau mitigates abnormal Tau aggregation-induced pathology" in eLife magazine online

Figure 1.

In this work, the researchers first found that the expression of the chaperone Hsp27 was significantly upregulated in the frontal cortex of the brain of AD patients and co-localized with the pTau aggregate part (Figure 1

Figure 2.

Further in vitro studies have shown that Hsp27 is able to specifically recognize the pTau protein and inhibit its amyloid aggregation

Figure 3.

In summary, this work found that the chaperone Hsp27 in vivo and in vitro specifically identified pTau with pathological toxicity, inhibited its amyloid aggregation, and significantly delayed the neuropathological toxicity caused by it, revealing the molecular mechanism

Zhang Shengnan, associate researcher of Liu Cong's research group of the Interdisciplinary Research Center of Biology and Chemistry of the Shanghai Institute of Organic Sciences, Chinese Academy of Sciences, Zhu Yi, doctoral student of Grace Zhai research group, Lu Jinxia, doctoral student of Li Dan's research group, and Liu Zhenying, doctoral student of Liu Cong's research group, are co-first authors

Thesis link: https://elifesciences.