Enhancement of native and phosphorylated TDP-43 immunoreactivity by proteinase K treatment following autoclave heating
Enhancement of native and phosphorylated TDP-43 immunoreactivity by proteinase K treatment following autoclave heating
复制标题
高压灭菌后通过蛋白酶 K 处理增强天然和磷酸化 TDP-43 免疫反应性
DOI:
10.1111/j.1440-1789.2010.01184.x
复制
发表时间:
2011
期刊:
影响因子:
2.3
通讯作者:
et al.
中科院分区:
文献类型:
--
作者:
Mori F;et al.
TDP‐43 is a major disease protein in amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration with TDP‐43 (FTLD‐TDP). To evaluate the effectiveness of proteinase K (PK) treatment in antigen retrieval for native and phosphorylated TDP‐43 protein, we examined the temporal cortex and spinal cord from patients with sporadic ALS and FTLD‐TDP and control subjects. PK treatment following heat retrieval enhanced the immunoreactivity for native TDP‐43 in controls as well as for native and phosphorylated TDP‐43 in ALS and FTLD‐TDP. A significant number of TDP‐43‐positive neuropil threads were demonstrated in lesions, in which routine immunohistochemistry revealed that the predominant inclusions are cytoplasmic. This retrieval method is the best of immunohistochemical techniques for demonstrating TDP‐43 pathology, especially in the neuropil.