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PHF‐tau from Alzheimer's brain comprises four species on SDS‐PAGE which can be mimicked by in vitro phosphorylation of human brain tau by glycogen synthase kinase‐3β
Author(s) -
Mulot S.F.C.,
Hughes K.,
Woodgett J.R.,
Anderton B.H.,
Hanger D.P.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00702-0
Subject(s) - gene isoform , phosphorylation , in vitro , gsk 3 , recombinant dna , human brain , kinase , glycogen synthase , biochemistry , biology , microbiology and biotechnology , chemistry , neuroscience , gene
Extensive in vitro phosphorylation of a purified preparation of control human brain tau consistently produces four rather than, as previously believed, three tau species on SDS‐PAGE. The species thus generated are shifted on SDS‐PAGE to positions that match those of PHF‐tau isolated from Alzheimer's disease brain. A mixture of recombinant human tau isoforms phosphorylated by GSK‐3β gave similar results to those obtained with control human brain tau. In vitro phosphorylation of the individual recombinant isoforms by GSK‐3β showed that the four bands of PHF‐tau are likely to consist of isoforms 3R,0 alone; 4R,0 with 3R,29; 4R,29 with 3R,58 and 4R,58 alone.