Microtubule-associated protein tau

Goedert, M., Spillantini, M.G., Jakes, R., Rutherford, D., 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. 

Several pathological self-polymerizing systems have been biophysi-cally characterized sufficiently to permit identification of protein or peptide species that could serve as molecular targets in a structure-activity relationship. These include transthyretin (TTR) [73-76], serum amyloid A protein (SAA) [77], microtubule-associated protein tau [78-80], amylin or islet amyloid polypeptide (IAPP) [81,82], IgG light chain amyloidosis (AL) [83-85], polyglutamine diseases [9,86], a-synuclein [47,48] and the Alzheimer s (3 peptide [87-96]. A variety of A(3 peptide assay systems have been established at Parke-Davis to search for inhibitors of fibril formation that could be therapeutically useful [97]. 

FriedhoffP, Schneider A, Mandelkow EM, Mandelkow E. Rapid assembly of Alzheimer-like paired helical filaments from microtubule-associated protein tau monitored by flourescence in solution. Biochemistry 1998 37 10223-10230. 

Schweers O, Mandelkow EM, Biemat J, Mandelkow E. Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments. Proc Natl Acad Sci USA 1995 92 8463-8467. 

Lewy bodies, neurofibrillary lesions and Pick bodies are intracellular filamentous inclusions. It is now well established that Lewy bodies are made of the protein a-synuclein and both neurofibrillary lesions and Pick bodies of the microtubule-associated protein tau. Mutations in the a-synuclein gene or an increase in its copy number cause autosomal-dominantly inherited forms of Parkinson s disease and dementia with Lewy bodies. Mutations in the tau gene cause a familial form of frontotemporal dementia. Here we review the evidence implicating a-synuclein and tau in these inherited and a number of sporadic neurodegenerative diseases. Collectively, a-synucleinopathies and tauopathies account for the vast majority of cases of late-onset neurodegenerative disease (Tables 45-1 and 45-2). 

Grundke-Iqbal, I. et al. Abnormal phosphorylation of the microtubule-associated protein tau in Alzheimer cytoskel-etal pathology. Proc. Natl. Acad. Sci. USA 83 4913-4917, 1986. 

Goedert, M. et al. Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans. Nature 338 550-553,1996. 

MAPT microtubule-associated protein tau NIPP nuclear inhibitor of protein phosphatase... 

There is also interest in the involvement of the cytoskeleton in such degenerative diseases as Alzheimer s disease (see Chapter 14) which is characterized by tangles (paired helical filaments). It seems likely that one of the microtubule-associated proteins (tau protein) is an important component of the tangles found in Alzheimer s disease. 

The microtubule-associated-protein tau is a component of the neurofibrillary tangles in Alzheimer s disease and a target of S100A1. PC 12 cells devoid of S100A1 were shown to be more resistant to A(3(25-35) peptide-mediated cell death and have lower levels of intracellular amyloid precursor protein (APP) (Zimmer et al., 2005). 

Deka, J., Kuhlmann, J., and Muller, O. (1998). A domain within the tumor suppressor protein APC shows very similar biochemical properties as the microtubule-associated protein tau. Eur.J. Biochem. 253, 591—597. 

Janke, C., Holzer, M., Klose, J, and Arendt, T. (1996) Distribution of isoforms of the microtubule-associated protein tau in grey and white matter areas of human brain a two-dimensional gelelectrophoretic analysis. FEBS Lett. 379, 222-226. 

Grundke-Iqbal, I., Iqbal, K., Quinlan, M., Tung, Y. C., Zaidi, M. S., et al. (1986) Microtubule-associated protein tau. A component of Alzheimer paired helical filaments. J Biol Chem 261, 6084-6089. 

Goedert, M., Wiscliik, C. M., Crowther, R. A., Walker, J. E. and Klug, A. (1988) Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease identification as the microtubule-associated protein tau. Proc Natl Acad Sci USA 85, 4051-4055. 

Kosik, K. S., Joacliim, C. L. and Selkoe, D. J. (1986) Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease. Proc Natl Acad Sci USA 83, 4044-4048. 

Wood JG, Mirra SS, Pollock NJ, Binder LI (1986) Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau (tau). Proc... 

Tau pathology corresponds to the intraneuronal aggregation of microtubule-associated tau proteins into abnormal filaments. Paired hehcal filaments (PHF) are the most characteristic cytoskeletal alterations affecting numerous neurons in AD. Using a combined immunocytochemical and biochemical approach (Iqbal et al., 1989) demonshated for the first time that the microtubule-associated protein tau, a normal brain cytoskeletal protein, is a component of the PHF. The authors also indicated for the first time that posttranslational modification of tau such as phosphorylation might occur which would allow it to assemble either alone or together... 

Arnold CS, Johnson GV, Cole RN, Dong DL, Lee M, Hart GW (1996) The microtubule-associated protein tau is extensively modified with 0-linked N-acetylglucosamine. J Biol Chem 271 28741-28744... 

Brandt R, Lee G (1993) Functional organization of microtubule-associated protein tau. Identification of regions which affect microtubule growth, nucleation, and bundle formation... 

Couchie D, Legay F, Guilleminot J, Lebeugy F, Brion JP, Nunez J (1990) Expression of Tau protein and Tau mRNA in the cerebellum during axontil outgrowth. Exp Brain Res 82 589-596 Crowther T, Goedert M, Wischik CM (1989) The repeat region of microtubule-associated protein tau forms part of the core of the paired helical fileunent of Alzheimer s disease. Ann Med 21 127-132... 

Ledesma MD, Bonay P, Colaco C, Avila J (1994) Analysis of microtubule-associated protein tau glycation in paired helical filaments. J Biol Chem 269 21614-21619 Lee G (1990) Tau protein an update on structure and function. Cell Motil Cytoskeleton 15 199-203... 

Schooneboom NHH, Scheltens P, Leon M (2006) Cerebrospinal fluid markers for the diagnosis of Alzheimer s disease. In Gauthier SSP, Cummings JL (eds) Alzheimer s Disese and related Disorders Annual, Vol 5. Taylor and Francis, Oxford, pp 17-33 Schweers O, Mandelkow EM, Biemat 1, Mandelkow E (1995) Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments. Proc Natl Acad Sci U S A 92 8463-8467... 

Van DeerUn VM, Forman MS, Farmer JM, Grossman M, Joyce S, Crowe A et al (2007) Biochemical and pathological characterization of frontotemporal dementia due to a Leu266Val mutation in microtubule-associated protein tau in an African American individual. Acta Neuropathol 113 471-479... 

Wang JZ, Liu F (2008) Microtubule-associated protein tau in development, degeneration and protection of neurons. Prog Neurobiol 85 148-175 Wenning GK, S YB-, Hughes A, Daniel SE, Lees A, Quinn, NP (2000) What chnical features are most useful to distinguish definite multiple system atrophy from Parkinson s disease J Neurol Neurosurg Psychiatry 68 434 40... 

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