Distribution of isoforms of the microtubule‐associated protein tau in grey and white matter areas of human brain: A two‐dimensional gelelectrophoretic analysis

FEBS Letters

Klose, Joachim²  Arendt, Thomas¹  Janke, Carsten¹  Holzer, Max¹ 

[1] Paul Flechsig Institute of Brain Research, Department of Neurochemistry, University of Leipzig, Jahnallee 59, 04109 Leipzig, Germany;Institute of Human Genetics, Freie Universität Berlin, Germany

关键词: Microtubule-associated protein;    Tau protein;    Two-dimensional gel electrophoresis;    Isoform;    Alzheimer's disease;    Quantitative analysis;    Regional distribution;   

DOI  :  10.1016/0014-5793(95)01522-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown