Alzheimer disease hyperphosphorylated tau aggregates hydrophobically

Synapse

Volumn 27, Issue 3, 1997, Pages 208-229

  Ruben, George C ^a   Ciardelli, Thomas L ^b   Grundke Iqbal, Inge ^c   Iqbal, Khalid ^c  

^a Dartmouth College   (United States)

^b DARTMOUTH MEDICAL SCHOOL   (United States)

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

Author keywords

Circular dichroism; Freeze dried vertically Pt C replicated tau on silver filters; Inverse temperature transition; MAP tau; Neurofibrillary tangles; Transmission electron microscopy

Indexed keywords

ALKALINE PHOSPHATASE; ELASTIN; HYDROFLUORIC ACID; TAU PROTEIN;

ALZHEIMER DISEASE; AMINO TERMINAL SEQUENCE; ARTICLE; CIRCULAR DICHROISM; DEPHOSPHORYLATION; HUMAN; HUMAN TISSUE; HYDROPHOBICITY; NEUROFIBRILLARY TANGLE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ISOLATION; PROTEIN PHOSPHORYLATION; PROTEIN SECONDARY STRUCTURE; SYNAPTIC TRANSMISSION; TRANSMISSION ELECTRON MICROSCOPY;

ALKALINE PHOSPHATASE; ALZHEIMER DISEASE; ANIMALS; CATTLE; CHEMISTRY, PHYSICAL; CIRCULAR DICHROISM; FEMALE; FETUS; HUMANS; HYDROFLUORIC ACID; MICROSCOPY, ELECTRON; PHOSPHORYLATION; PREGNANCY; RATS; RECOMBINANT PROTEINS; SILVER STAINING; TAU PROTEINS; TEMPERATURE;

EID: 0030931864     PISSN: 08874476     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1098-2396(199711)27:3<208::AID-SYN7>3.0.CO;2-H     Document Type: Article

References (44)

1. Alonso, A. del C., Zaidi, T., Grundke-Iqbal, I., and Iqbal, K. (1994) Role of abnormally phosphorylated tau in the breakdown of microtubules in alzheimers disease. Proc. Natl. Acad. Sci. U.S.A., 91:5562-5566.
2. Alonso, A. del C., Grundke-Iqbal, I., and Iqbal, K. (1996) Alzheimer's disease hyperphosphorylated tau sequesters normal tau into tangles of filament and disassembles microtubules. Nature Medicine, 2:1-5.
3. Bancher, C., Brunner, C., Lassmann, H., Budka, H., Jellinger, K., Wiche, G., Seitelberger, F., Grundke-Iqbal, I., Iqbal, K., and Wisniewski, H.M. (1989) Accumulation of abnormally phosphorylated tau precedes the formation of neurofibrillary tangles in Alzheimer's disease. Brain Res., 477:90-99.
4. Barcikowska, M., Wisniewski, H.M., Bancher, C., and Grundke-Iqbal, I. (1989) About the presence of paired helical filaments in dystrophic neurites participating in the plaque formation. Acta Neuropathol. (Berl.), 78:225-231.
5. Bensadoun, A., and Weinstein, D. (1976) Assay of proteins in the presence of interfering materials. Anal. Biochem., 70:241-250.
6. Biernat, J., Gustke, N., Drewes, G., Mandelkow, E.-M., and Mandelkow, E. (1993) Phosphorylation of Ser-262 strongly reduces binding of tau to microtubules: Distinction between PHF-like immunoreactivity and microtubule binding. Neuron, 11:153-163.
7. Brion, J.P., Hager. D.P., Bruce, M.T., Couck, A.M., Flament-Durant, J., and Anderton, B.T. (1991) Tau in Alzheimers nerofibriliary tangles. Biochem. J., 273:127-133.
8. Ciardelli, T.L., Landgraf, B., Gadski, R., Strand, J., Cohen, F.E., and Smith, K.A. (1988) A design approach to the structural analysis of interleukin-2. J. Mol. Recognit., 1:42-47.
9. Dickson, D.W., Farlo, J., Davies, P., Crystal, H., Fuld, P., and Yen, S.C. (1988) Alzheimer's disease. Am. J. Pathol., 132:86-101.
10. Francis, P.T., Chessell, I.P., Webster, M.-T., Clarke, N.A., Procter, A.W., Alder, J.T., Chen, C., Qume, M., Zeman, S., Dijk, S., and Bowen, D. (1995) Is improvement of cholinergic transmission the correct strategy for Alzheimer's disease? In: Research Advances in Alzheimer's Disease and Related Disorders. K. Iqbal, J.A. Mortimer, B. Winblad, and H.M. Wisniewski, eds. J. Wiley & Sons, New York, pp. 273-281.
11. Goedert, M., Spillantini, M.G., Jakes, R., Rutherford, D., and Crowther, R.A. (1989) Multiple isoforms of human microtubule-associated protein tau: Sequences and localization in neurofibrillary tangles of Alzheimer's disease. Neuron, 3:519-526.
12. Goedert, M., Spillantini, M.G., Cairns, N.J., and Crowther, R.A. (1992) Tau proteins of Alzheimer paired helical filaments: Abnormal phosphorylation of all six brain isoforms. Neuron, 8:159-168.
13. PHF proteins display the same biochemical properties as normal τ*. J. Biol. Chem., 267:564-569.
14. Grundke-Iqbal, I., Iqbal, K., Quinlan, M., Tung, Y.-C., Zaidi, M.S., and Wisniewski, H.M. (1986a) Microtubule-associated protein tau: A component of Alzheimer paired helical filaments. J. Biol. Chem., 261:6084-6089.
15. Grundke-Iqbal, I., Iqbal, K., Tung, Y-C., Quinlan, M., Wisniewski, H.M., and Binder, L. I. (1986b) Abnormal phosphorylation of the microtubule associated protein tau in Alzheimer cytoskeletal pathology. Proc. Natl. Acad. Sci. U. S. A. 83:4913-4917.
16. Hasegawa, M., Morishima-Kawashima, M., Takio, K., Suzuki, M., Titani, K., and Ihara, Y. (1992) Protein sequence and mass spectrmetric analyses of tau in Alzheimer disease brain. J. Biol. Chem., 267:17047-17054.
17. Iqbal, K., and Grundke-Iqbal, I. (1995) Alzheimer abnormally phosphorylated tau is more hyperphosphorylated than the fetal tau and causes the disruption of microtubules. Neurobiol. Aging, 16:375-379.
18. Iqbal, K., Grundke-Iqbal, I., Zaidi, T, Merz, P.A., Wen, G.Y., Shaikh, S.S., Wisniewski, H.M., Alafuzoff, I., and Winblad, B. (1986) Defective brain microtubule assembly in Alzheimer's disease. Lancet, 2:421-426.
19. Iqbal, K., Grundke-Iqbal, I., Smith, A.J., George, L., Tung, Y-C. and Zaidi, T. (1989) Identification and localization of a tau peptide to paired helical filaments of Alzheimer disease. Proc. Natl. Acad. Sci. U. S. A., 86:5646-5650.
20. Iqbal, K., Zaidi, T., Bancher, C., and Grundke-Iqbal, I. (1994) Alzheimer paired helical filaments: Restoration of the biological activity by dephosphorylation. FEBS Lett., 349:104-108.
21. Jakes, R., Novak, M., Davison, M., and Wischik, C.M. (1991) Identification of 3-and 4-repeat tau isoforms within the PHF in Alzheimer's disease. EMBO J., 10:2725-2729.
22. Katzman, R., Terry, R.D., Deteresa, R., Brown, R., Davies, P., Fuld, P., Renling, X., and Peck, A. (1988) Clinical, pathologic and neurochemical changes in dementia: A subgroup with preserved mental status and numerous neocortical plaques. Ann. Neurol., 23:138-144.
23. Kidd, M. (1964) Alzheimer's disease. An electron microscopical study. Brain, 87:307-320.
24. Kirschner, D.A., Abraham, C., and Selkoe, D.J. (1986) X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-β conformation. Proc. Natl. Acad. Sci. U. S. A., 83:503-507.
25. Köpke, E., Tung, Y.-C., Shaikh, S., Alanso, A. del C., Iqbal, K., and Grundke-Iqbal, I. (1993) Microtubule-associated protein tau: Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer's disease. J. Biol. Chem., 268:24374-24384.
26. Lindwall, G., and Cole, R.D. (1984a) Phosphorylation affects the ability of the tau protein to promote microtubule assembly. J. Biol. Chem., 259:5301-5305.
27. Lindwall, G., and Cole, R.D. (1984b) Purification of tau protein and the occurrence of two phosphorylation states of tau in brain. J. Biol. Chem., 258:12241-12245.
28. Morishima-Kawashima, M., Hasegawa, M., Takio, K., Zuzuki, M., Yoshida, H., Watanabe, A., Titani, K., and Ihara, Y. (1995a) Hyperphosphorylation of tau in PHF. Neurobiol. Aging, 16:365-380.
29. Morishima-Kawashima, M., Hasegawa, M., Takio, K., Suzuki, M., Yoshida, H., Watanabe, A., Titani, K., and Ihara, Y. (1995b) Proline-directed and non-proline-directed phosphorylation of PHF-tau. J. Biol. Chem., 270:823-829.
30. Perczel, A., Hollosi, M., Tusnady, G., and Fasman, G.D. (1991) Convex constraint analysis: A natural deconvolution of circular dichroism spectra. Protein Eng., 4:669-679.
31. Ruben, G.C., Harris, Jr., E.D., and Nagase, H. (1988) Electron microscope studies of free and proteinase-bound duck ovostatins (ovomacroglobins): model of ovostatin structure and its transformation upon proteolysis, J. Biol. Chem., 263:2861-2869.
32. Ruben, G.C. (1989) Ultrathin (1nm) vertically shadowed Pt-C replicas for imaging individual molecules in freeze-etched biological DNA and material science metal and plastic specimens. J. Electr. Microsc. Tech., 13:335-354.
33. Ruben, G.C., Iqbal, K., Grundke-Iqbal, I., Wisniewski, H.M., Ciardelli, T.L., and Johnson, J.E., Jr. (1991) The microtubule associated protein tau forms a triple-stranded left-hand helical polymer. J. Biol. Chem., 266:22019-22027.
34. Ruben, G.C., Iqbal, K., Wisniewski, H.M., Johnson, J.E., Jr., and Grundke-Iqbal, I. (1992) Alzheimer neurofibrillary tangles contain 2.1 nm filaments structurally identical to the microtubule associated protein tau: Ahigh resolution transmission electron microscopy study of tangles and senile plaque core amyloid. Brain Res., 590:164-179.
35. Ruben, G.C., Iqbal, K., Grundke-Iqbal, I., and Johnson, J.E., Jr. (1993) The organization of the microtubule associated protein tau in Alzheimer paired helical filaments. Brain Res., 602:1-13.
36. Ruben, G.C., Novak, M., Edwards, P.C., and Iqbal, K. (1995) Alzheimer paired helical filaments, untreated and pronase digested, studied by vertical platinum-carbon replication and high resolution transmission electron microscopy. Brain Res., 675:1-12.
37. Ruben, G.C., Alonso, A. del C., Grundke-Iqbal, I., and Iqbal, K. (1996) Taxol stabilized rat brain microtubules with microtubule-associated proteins (MAPs) freeze-dried and vertically platinum-carbon (Pt-C) replicated: New ultra-high resolution images for evaluating the relationship of MAPs to microtubules. Neuroscience-Net, 1:article 10002.
38. Schweers, O., Schonbrunn-Hanebeck, E., Marx, A., and Mandelkow, E. (1994) Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for b-structure. J. Biol. Chem., 269:24290-24297.
39. Singh, T.J., Haque, N., Grundke-Iqbal, I., and Iqbal, K. (1995) Rapid Alzheimer-like phosphorylation of tau by the synergistic actions of non-proline-dependent protein kinase and GSK-3. FEBS Lett., 358:267-272.
40. Urry, D.W. (1990) Protein folding and assembly: An hydration-mediated free energy driving force. In: Protein Folding: Deciphering the Second Half of the Genetic Code. L.M. Gierasch and J. King, eds. American Association for the Advancement of Science, Washington, DC, pp. 63-71.
41. Urry, D.W. (1993) Molecular machines: How motion and other functions of living organisms can result from reversible chemical changes. Angew. Chem. Int. Ed. Engl. 32:819-841.
42. Wang, J.-Z., Gong, C.-X., Zaidi, T., Grundke-Iqbal, I., and Iqbal, K. (1995) Dephosphorylation of Alzheimer paired helical filaments by protein phosphatase-2A and -2B. J. Biol. Chem., 270:4854-4860.
43. Watanabe, A., Hasegawa, M., Suzuki, M., Takio, K., Morishima-Kawashima, M., Titani, A., Arai, T., Kosik, K.A., and Ihara, Y. (1993) In vivo phosphorylation sites in fetal and adult rat tau. J. Biol. Chem., 268:25712-25717.
44. Yoshida, H., and Ihara, Y. (1993) Tau in paired helical filaments is functionally distinct from fetal tau: Assembly incompetence of paired helical filament tau. J. Neurochem., 61:1183-1186.