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Science 8 February 1991:
Vol. 251. no. 4994, pp. 675 - 678
DOI: 10.1126/science.1899488
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Articles

Science, Vol 251, Issue 4994, 675-678
Copyright © 1991 by American Association for the Advancement of Science

articles

A68: a major subunit of paired helical filaments and derivatized forms of normal Tau

VM Lee, BJ Balin, L Otvos Jr, and JQ Trojanowski

Department of Pathology and Laboratory Medicine, University of Pennsylvania School of Medicine, Philadelphia 19104.

Putative Alzheimer disease (AD)-specific proteins (A68) were purified to homogeneity and shown to be major subunits of one form of paired helical filaments (PHFs). The amino acid sequence and immunological data indicate that the backbone of A68 is indistinguishable from that of the protein tau (tau), but A68 could be distinguished from normal human tau by the degree to which A68 was phosphorylated and by the specific residues in A68 that served as phosphate acceptors. The larger apparent relative molecular mass (Mr) of A68, compared to normal human tau, was attributed to abnormal phosphorylation of A68 because enzymatic dephosphorylation of A68 reduced its Mr to close to that of normal tau. Moreover, the LysSerProVal motif in normal human tau appeared to be an abnormal phosphorylation site in A68 because the Ser in this motif was a phosphate acceptor site in A68, but not in normal human tau. Thus, the major subunits of a class of PHFs are A68 proteins and the excessive or inappropriate phosphorylation of normal tau may change its apparent Mr, thus transforming tau into A68.


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J. Biol. Chem. 273, 9761-9768
   Abstract »    Full Text »    PDF »
Alzheimer-like Changes in Microtubule-associated Protein Tau Induced by Sulfated Glycosaminoglycans. INHIBITION OF MICROTUBULE BINDING, STIMULATION OF PHOSPHORYLATION, AND FILAMENT ASSEMBLY DEPEND ON THE DEGREE OF SULFATION.
M. Hasegawa, R. A. Crowther, R. Jakes, and M. Goedert (1997)
J. Biol. Chem. 272, 33118-33124
   Abstract »    Full Text »    PDF »
Phosphorylation by Neuronal cdc2-like Protein Kinase Promotes Dimerization of Tau Protein in Vitro.
H. K. Paudel (1997)
J. Biol. Chem. 272, 28328-28334
   Abstract »    Full Text »    PDF »
Life and Death of Neurons in the Aging Brain.
J. H. Morrison and P. R. Hof (1997)
Science 278, 412-419
   Abstract »    Full Text »
Lithium Reduces Tau Phosphorylation by Inhibition of Glycogen Synthase Kinase-3.
M. Hong, D. C. R. Chen, P. S. Klein, and V. M.-Y. Lee (1997)
J. Biol. Chem. 272, 25326-25332
   Abstract »    Full Text »    PDF »
Insulin and Insulin-like Growth Factor-1 Regulate Tau Phosphorylation in Cultured Human Neurons.
M. Hong and V. M.-Y. Lee (1997)
J. Biol. Chem. 272, 19547-19553
   Abstract »    Full Text »    PDF »
Selective Destruction of Stable Microtubules and Axons by Inhibitors of Protein Serine/Threonine Phosphatases in Cultured Human Neurons (NT2N Cells).
S. E. Merrick, J. Q. Trojanowski, and V. M.-Y. Lee (1997)
J. Neurosci. 17, 5726-5737
   Abstract »    Full Text »    PDF »
Familial multiple system tauopathy with presenile dementia: A disease with abundant neuronal and glial tau filaments.
M. G. Spillantini, M. Goedert, R. A. Crowther, J. R. Murrell, M. R. Farlow, and B. Ghetti (1997)
PNAS 94, 4113-4118
   Abstract »    Full Text »    PDF »
Conversion of Serine to Aspartate Imitates Phosphorylation-induced Changes in the Structure and Function of Microtubule-associated Protein Tau.
J. Leger, M. Kempf, G. Lee, and R. Brandt (1997)
J. Biol. Chem. 272, 8441-8446
   Abstract »    Full Text »    PDF »
The Neurofibrillary Pathology of Alzheimer's Disease.
M. Goedert (1997)
Neuroscientist 3, 131-141
   Abstract »    PDF »
Phosphorylation-dependent Monoclonal Tau Antibodies Do Not Reliably Report Phosphorylation by Extracellular Signal-regulated Kinase 2at Specific Sites.
HannoM. Roder, R.P. Fracasso, FrederickJ. Hoffman, J. A. Witowsky, G. Davis, and C. B. Pellegrino (1997)
J. Biol. Chem. 272, 4509-4515
   Abstract »    Full Text »    PDF »
`Oxidation Inhibits Substrate Proteolysis by Calpain I but Not Autolysis.
R. P. Guttmann, J. S. Elce, P. D. Bell, J. C. Isbell, and G. V.W. Johnson (1997)
J. Biol. Chem. 272, 2005-2012
   Abstract »    Full Text »    PDF »
The Structural Basis of Monoclonal Antibody Alz50's Selectivity for Alzheimer's Disease Pathology.
G. Carmel, E. M. Mager, L. I. Binder, and J. Kuret (1996)
J. Biol. Chem. 271, 32789-32795
   Abstract »    Full Text »    PDF »
The Microtubule-associated Protein Tau Is Extensively Modified with O-linked N-acetylglucosamine.
C. S. Arnold, G. V.W. Johnson, R. N. Cole, D. L.-Y. Dong, M. Lee, and G. W. Hart (1996)
J. Biol. Chem. 271, 28741-28744
   Abstract »    Full Text »    PDF »
A Spatial Gradient of Tau Protein Phosphorylation in Nascent Axons.
J. W. Mandell and G. A. Banker (1996)
J. Neurosci. 16, 5727-5740
   Abstract »    Full Text »    PDF »
Site-specific Dephosphorylation of Tau Protein at Ser[IMAGE]/Thr[IMAGE] in Response to Microtubule Depolymerization in Cultured Human Neurons Involves Protein Phosphatase 2A.
S. E. Merrick, D. C. Demoise, and V. M.-Y. Lee (1996)
J. Biol. Chem. 271, 5589-5594
   Abstract »    Full Text »    PDF »
Molecular Dissection of the Neurofibrillary Lesions of Alzheimer's Disease.
M. Goedert, M.G. Spillantini, M. Hasegawa, R. Jakes, R.A. Crowther, and A. Klug (1996)
Cold Spring Harb Symp Quant Biol 61, 565-573
   Abstract »    PDF »
Widespread Appearance of Alz-50 Immunoreactive Neurons in the Human Brain With Cerebral Infarction.
T. Uchihara, K. Tsuchiya, H. Kondo, T. Hayama, and K. Ikeda (1995)
Stroke 26, 2145-2148
   Abstract »    Full Text »
Polymerization of Microtubule-associated Protein Tau under Near-physiological Conditions.
D. M. Wilson and L. I. Binder (1995)
J. Biol. Chem. 270, 24306-24314
   Abstract »    Full Text »    PDF »
Amyloid beta-Protein Inhibits Ubiquitin-dependent Protein Degradation in Vitro.
L. Gregori, C. Fuchs, M. E. Figueiredo-Pereira, W. E. Van Nostrand, and D. Goldgaber (1995)
J. Biol. Chem. 270, 19702-19708
   Abstract »    Full Text »    PDF »


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