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Enhancement of native and phosphorylated TDP‐43 immunoreactivity by proteinase K treatment following autoclave heating
Author(s) -
Mori Fumiaki,
Tanji Kunikazu,
Kakita Akiyoshi,
Takahashi Hitoshi,
Wakabayashi Koichi
Publication year - 2011
Publication title -
neuropathology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.701
H-Index - 61
eISSN - 1440-1789
pISSN - 0919-6544
DOI - 10.1111/j.1440-1789.2010.01184.x
Subject(s) - frontotemporal lobar degeneration , immunohistochemistry , amyotrophic lateral sclerosis , neuropil , pathology , phosphorylation , antigen retrieval , medicine , frontotemporal dementia , biology , biochemistry , disease , dementia , central nervous system
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.