Abstract:
:In Alzheimer's disease, there is a major redistribution of the tau protein pool from soluble to PHF-bound forms. PHF-bound tau can be distinguished from normal tau by acid reversible occlusion of a generic tau epitope in the tandem repeat region and characteristic sedimentation in the if-II protocol developed in this laboratory. We show that 85% of tau bound in the PHF-like configuration can be recovered in the if-II PHF-fraction. Less than 1% of this material was phosphorylated at the mAb AT8 site in aged clinical controls or in cases with minimal or mild dementia. Of tau phosphorylated at the mAb AT8 site, only 12% was found to co-sediment with PHFs. These low levels could not be explained by postmortem dephosphorylation. As more than 95% of PHF-tau is not phosphorylated, even at early stages of pathology, it is misleading to use the terms "PHF-tau" and "phosphorylated tau" as though they were synonymous, particularly as this implies a pathogenetic role which phosphorylation need not have.
journal_name
Neurobiol Agingjournal_title
Neurobiology of agingauthors
Wischik CM,Edwards PC,Lai RY,Gertz HN,Xuereb JH,Paykel ES,Brayne C,Huppert FA,Mukaetova-Ladinska EB,Mena Rdoi
10.1016/0197-4580(95)97327-dsubject
Has Abstract,Author List Incompletepub_date
1995-05-01 00:00:00pages
409-17; discussion 418-31issue
3eissn
0197-4580issn
1558-1497pii
019745809597327Djournal_volume
16pub_type
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