Glycosylation of microtubule-associated protein tau: An abnormal posttranslational modification in Alzheimer's disease

Nature Medicine

Volumn 2, Issue 8, 1996, Pages 871-875

  Wang, Jian Zhi ^a   Grundke Iqbal, Inge ^a   Iqbal, Khalid ^a  

^a NEW YORK STATE INSTITUTE FOR BASIC RESEARCH IN DEVELOPMENTAL DISABILITIES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GLYCAN; MICROTUBULE ASSOCIATED PROTEIN; TAU PROTEIN;

ALZHEIMER DISEASE; ARTICLE; DEGENERATIVE DISEASE; DEGLYCOSYLATION; DEPHOSPHORYLATION; HUMAN; HUMAN TISSUE; NEUROFIBRILLARY TANGLE; NEUROLOGIC DISEASE; PRIORITY JOURNAL; PROTEIN GLYCOSYLATION;

ALZHEIMER DISEASE; ANIMALS; BRAIN; CATTLE; GLYCOSYLATION; HUMANS; NEUROFIBRILLARY TANGLES; POLYSACCHARIDES; PROTEIN PROCESSING, POST-TRANSLATIONAL; TAU PROTEINS;

EID: 0029815467     PISSN: 10788956     EISSN: None     Source Type: Journal    
DOI: 10.1038/nm0896-871     Document Type: Article

References (33)

1. Braak, H., Braak, E., Grundke-Iqbal, I. & Iqbal, K. Occurrence of neuropil threads in the senile human brain and in Alzheimer's disease: A third location of paired helical filaments outside of neurofibrillary tangles and neuritic plaques. Nenrosci. Lett. 65, 351-355 (1986).
2. Tomlinson, B.E., Blessed, G. & Roth, M. Observations on the brains of demented old people. J. Neurol. Sci. 11, 205-242 (1970).
3. Alafuzoff, I., Iqbal, K., Friden, H., Adolfsson, R. & Winblad, B. Histopathological criteria for progressive dementia disorders: Clinical-pathological correlation and classification by multivariate data analysis. Acta Neuropathol. (Berl.) 74, 209-225 (1987).
4. Grundke-Iqbal, I. et al. Microtubule-associated protein tau: A component of Alzheimer paired helical filaments. J. Biol. Chem. 261, 6084-6089 (1986).
5. Grundke-Iqbal, I. et al. Abnormal phosphorylation of the microtubule-associated protein τ(tau) in Alzheimer cytoskeletal pathology. Proc. Natl. Acad. Sci. USA 83, 4913-4917 (1986).
6. Iqbal, K. et al. Defective brain microtubule assembly in Alzheimer's disease. Lancet 2, 421-426 (1986).
7. Köpke, E. et al. Microbutule associated protein tau: Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease. J. Biol. Chem. 268, 24374-24384 (1993).
8. Drubin, D.G. & Kirschner, M.W. Tau protein function in living cells. J. Cell Biol. 103, 2739-46 (1986).
9. Ruben, G.C. et al. The microtubule associated protein tau forms a triplestranded left-hand helical polymer. J. Biol. Chem. 266, 22019-22027 (1991).
10. Goux, W.J., Rodriguez, S. & Sparkman, D.R. Analysis of the core components of Alzheimer paired helical filaments: A gas chromatography/mass spectrometry characterization of fatty acids, carbohydrates and long-chain bases. FEBS Lett. 366, 81-85 (1995).
11. Ruben, G.C., Iqbal, K., Wisniewski, H.M., Johnson, J.E. Jr. & Grundke-Iqbal, I. Alzheimer neurofibrillary tangles contain 2.1 nm filaments structurally identical to the microtubule associated protein tau: A high resolution transmission electron microscope study of tangles and senile plaque core amyloid. Brain Res. 590, 164-179 (1992).
12. Alonso, A. del C., Grundke-Iqbal, I. & Iqbal, K. Alzheimer disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules. Nature Med. 2, 783-787 (1996).
13. Wang, J.-Z., Gong, C.-X., Zaidi, T., Grundke-Iqbal, I. & Iqbal, K. Dephosphorylation of Alzheimer paired helical filaments by protein phosphatase-2A and -2B. J. Biol. Chem. 270, 4854-4860 (1995).
14. Smith, M.A. et al. Advanced Maillard reaction end products are associated with Alzheimer disease pathology. Proc. Natl. Acad. Sci. USA 91, 5710 (1994).
15. Ledesma, M.D., Bonay, P., Colaco, C. & Avila, J. Analysis of microtubule-associated protein tau glycation in paired helical filaments. J. Biol. Chem. 269, 21614-21619 (1994).
16. Yan, S.D. et al. Glycated tau protein in Alzheimer disease: A mechanism for induction of oxidant stress. Proc. Natl. Acad. Sci. USA 91, 7787 (1994).
17. Ledesma, M.D., Bonay, P. & Avila, J. τ Protein from Alzheimer's disease patients is glycated at its tubulin-binding domain. J. Neurochem. 65, 1658 (1995).
18. Tanaka, S., Avigad, G., Brodsky, B. & Eikenberry, E.F. Glycation induces expansion of molecular packing of collagen. J. Mol. Biol. 203, 495-505 (1988).
19. Bancher, C. et al. Accumulation of abnormally phosphorylated tau precedes the formation of neurofibrillary tangles in Alzheimer's disease. Brain Res. 477, 90-99 (1989).
20. Van, S.D. et al. Non-enzymatically glycated tau in Alzheimer's disease induces neuronal oxidant stress resulting in cytokine gene expression and release of amyloid β-peptide. Nature Med. 1, 693-699 (1995).
21. Papasozomenos, S.Ch. Tau protein immunoreactivity in dementia of the Alzheimer type. II. Electron microscopy and pathogenetic implications: Effects of fixation on the morphology of the Alzheimer's abnormal filaments. Lab. Invest. 60, 375-389 (1989).
22. Brandt, R., Léger, J. & Lee, G. Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain. J. Cell Biol. 131, 1327-1340 (1995).
23. Mason, R.P., Trumbore, M.W. & Pettegrew, J.W. Membrane interactions of a phosphomonoester elevated early in Alzheimer's disease. Neurobiol. Aging 16, 531-539 (1995).
24. Zubenko, G.S. et al. Platelet membrane fluidity in Alzheimer's disease. Alzheimer Dis. Assoc. Disord. 2, 179 (1988).
25. Sherrington, R. et al. Cloning of a gene bearing missense mutations in earlyonset familial Alzheimer's disease. Nature 375, 754-760 (1995).
26. Rogaev, E.I. et al. Familial Alzheimer's disease in kindreds with missense mutations in a gene on chromosome I related to the Alzheimer's disease type 3 gene. Nature 376, 775-778 (1995).
27. Kang, J. et al. The precursor of Alzheimer's disease amyloid A4 protein resembles a cell surface receptor. Nature 325, 733-736 (1987).
28. Goate, A. et al. Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease. Nature 349, 704-706 (1991).
29. Iqbal, K., Zaidi, T., Thompson, C.H., Merz, P.A. & Wisniewski, H.M. Alzheimer paired helical filaments: Bulk isolation, solubility and protein composition. Acta. Neuropathol. (Berl.) 62, 167-177 (1984).
30. Bensadoun, A. & Weinstein, D. Assay of proteins in the presence of interfering materials. Anal. Biochem. 70, 241-250 (1976).
31. Wisniewski, H.M., Merz, P.A. & Iqbal, K. Ultrastructure of paired helical filaments of Alzheimer's neurofibrillary' tangle. J. Neuropathol. Exp. Neturol. 43, 643-656 (1984).
32. Cohen, P. et al. Protein phosphatase-1 and protein phosphatase-2A from rabbit skeletal muscle. Methods Enzymol. 159, 390-408 (1988).
33. Khatoon, S., Grundke-Iqbal, I. & Iqbal, K. Brain levels of microtubule-associated protein tau are elevated in Alzheimer's disease: A radioimmuno-slot-blot assay for nanograms of the protein. J. Neurochem. 59, 750-753 (1992).