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Distribution of isoforms of the microtubule‐associated protein tau in grey and white matter areas of human brain: A two‐dimensional gelelectrophoretic analysis
Author(s) -
Janke Carsten,
Holzer Max,
Klose Joachim,
Arendt Thomas
Publication year - 1996
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(95)01522-1
Subject(s) - gene isoform , grey matter , microtubule , alternative splicing , microtubule associated protein , tubulin , tau protein , biology , white matter , human brain , recombinant dna , microbiology and biotechnology , biochemistry , gene , alzheimer's disease , neuroscience , pathology , medicine , disease , radiology , magnetic resonance imaging
The microtubule‐associated protein tau in human brain consists of six molecular isoforms derived from a single gene by alternative mRNA‐splicing and further modified by posttranslational processing. In the present study, the distribution of tau isoforms in grey and white matter of human temporal cortex was investigated by two‐dimensional gelelectrophoresis. More than 80 isoforms were detected. The pattern of isoforms obtained after treatment with alkaline phosphatase was still more complex than those of recombinant tau, indicating that posttranslational modifications other than phosphorylation contribute to the molecular heterogeneity of tau. The tau isoform D according to Goedert [1] containing fout tubulin‐binding regions shown to promote tubulin polymerisation most efficiently was present in higher amounts in white as compared to grey matter. The pattern of isoform distribution was not significantly altered in Alzheimer's disease. It is concluded that molecular isoforms that differ in their tubulin‐binding characteristics are differentially distributed in subcellular neuronal compartments and/or neuronal types.