Tau factor polymers are similar to paired helical filaments of Alzheimer's disease.
Tau factor, upon urea treatment, is able to polymerize in vitro. These polymers are composed of tau factor as shown by immunogold staining. The structure of tau polymers is very similar to that of paired helical filaments (PHFs) of Alzheimer's disease in their dimensions as well as in their periodicity. Metal shadowing of both polymers shows a similar twisting. Also, similar peptide maps were found for tau factor and a 33 kDa protein that is the main component of our PHF preparations.
Montejo de Garcini
E
E
Centro de Biología Molecular (CSIC-UAM), Universidad Autónoma, Madrid, Spain.
Carrascosa
J L
JL
Correas
I
I
Nieto
A
A
Avila
J
J
D000544:Alzheimer Disease / Q000378:metabolism* / Q000473:pathology; D000818:Animals; D004258:DNA Polymerase III; D006801:Humans; D007150:Immunohistochemistry; D008854:Microscopy, Electron; D009454:Neurofibrils / Q000032:analysis* / Q000378:metabolism / Q000648:ultrastructure; D010449:Peptide Mapping; D011108:Polymers; D014157:Transcription Factors / Q000032:analysis* / Q000378:metabolism; D014508:Urea / Q000494:pharmacology
D011108:Polymers; D014157:Transcription Factors; D014508:Urea; C041273:transcription factor tau; D004258:DNA Polymerase III