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
C JankeT Arendt

Abstract

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 containing four 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.

References

May 1, 1991·Trends in Neurosciences·M GoedertC C Garner
Aug 1, 1990·Proceedings of the National Academy of Sciences of the United States of America·S G Greenberg, P Davies
Sep 1, 1989·Journal of the Neurological Sciences·S FlamentA Défossez
Nov 1, 1985·Archives of Neurology·Z S Khachaturian
Oct 1, 1985·The Journal of Cell Biology·L I BinderL I Rebhun
Sep 1, 1982·The American Journal of Psychiatry·B ReisbergT Crook
Nov 1, 1993·Trends in Neurosciences·M Goedert
Jan 13, 1995·The Journal of Biological Chemistry·M Morishima-KawashimaY Ihara
Aug 16, 1994·Biochemistry·N GustkeE Mandelkow

❮ Previous
Next ❯

Citations

Mar 29, 2001·Electrophoresis·J T RegulaR Frank
Feb 2, 2002·Experimental Hematology·Ellen A PaniskoTimothy D Veenstra
Nov 30, 2002·Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences·Thomas C HunterPaul A Haynes
Jan 30, 2016·Journal of Diabetes Research·Magdalena MajJohannes Attems
Jul 15, 2016·Biomarkers in Medicine·John A Bilello
Oct 26, 2016·Brain Research Bulletin·Thomas ArendtMax Holzer
Mar 26, 2002·Nature Genetics·Joachim KloseHans Lehrach
Nov 22, 2013·Electrophoresis·Stanislav N NaryzhnyAlexander I Archakov
May 27, 1999·Electrophoresis·J Klose
Sep 22, 2001·Electrophoresis·K Sperling
May 10, 2008·Expert Review of Proteomics·Nicolas SergeantLuc Buée
May 16, 2015·Biomedit︠s︡inskai︠a︡ khimii︠a︡·S N NaryzhnyA I Archakov
Dec 26, 2018·Journal of Alzheimer's Disease : JAD·Rudy J Castellani, George Perry
Sep 15, 2000·Journal of Neurochemistry·A Heicklen-Klein, I Ginzburg
Apr 7, 1999·Neurobiology of Aging·U GärtnerT Arendt
Aug 11, 2000·Brain Research·A Heicklen-KleinI Ginzburg
Jun 6, 2006·Protein Expression and Purification·Daniela Volke, Ralf Hoffmann

❮ Previous
Next ❯

Related Concepts

Related Feeds

Alzheimer's Disease: Tau & TDP-43

Alzheimer's disease is a neurodegenerative disease. This feed focuses on the underlying role of tau proteins and TAR DNA-binding protein 43, as well as other genetic factors, in Alzheimer's disease.