A Tau PET tracer PBB3 binds to TMEM106B amyloid fibril in brain

作者：Qinyue Zhao, Yun Fan, Wanbing Zhao, You Ni, Youqi Tao, Jiang Bian, Wencheng Xia, Wenbo Yu, Zhen Fan, Cong Liu, Bo Sun, Weidong Le, Wensheng Li, Jian Wang, Dan Li · 发表于：Cell Discovery · 年份：2024 · DOI：10.1038/s41421-024-00674-z · 被引用次数：24 · 研究领域：Alzheimer's disease research and treatments、Prion Diseases and Protein Misfolding、S100 Proteins and Annexins

Neurodegenerative diseases (NDs) are defined by pathological amyloid aggregates, such as Tau tangles and amyloid β (Aβ) plaques in Alzheimer’s disease (AD) 1 , 2 . The emergence of positron emission tomography (PET) imaging, using tracers like 11 C-PBB3 for Tau and 11 C-PiB for Aβ, offers significant diagnostic promise 3 , 4 , 5 . The challenge in achieving selective binding with PET tracers is exacerbated by the structural similarities among amyloid fibrils 6 , 7 . The recently identified transmembrane protein 106B (TMEM106B) fibril, prevalent in both NDs and normal elderly individuals, complicates the landscape 8 , 9 , 10 , 11 . This revelation prompts critical question regarding whether existing PET tracers, initially designed for Tau and Aβ, might also recognize TMEM106B fibril.