Tau protein in the glial cytoplasmic inclusions of multiple system atrophy can be distinguished from abnormal tan in Alzheimer's disease

Neuroscience Letters

Volumn 230, Issue 1, 1997, Pages 49-52

  Cairns, Nigel J ^a   Atkinson, Penny F ^a   Hanger, Diane P ^a   Anderton, Brian H ^a   Daniel, Susan E ^b   L Lantos, Peter ^a  

^a KING'S COLLEGE LONDON   (United Kingdom)

^b UNIVERSITY COLLEGE LONDON   (United Kingdom)

Author keywords

Alzheimer's disease; Glial cytoplasmic inclusion; Multiple system atrophy; Neurofibrillary tangle; Tau protein

Indexed keywords

TAU PROTEIN;

ALZHEIMER DISEASE; ARTICLE; BRAIN REGION; CLINICAL ARTICLE; CONTROLLED STUDY; FEMALE; GLIA CELL; HUMAN; HUMAN TISSUE; IMMUNOHISTOCHEMISTRY; MALE; NEUROFIBRILLARY TANGLE; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; SHY DRAGER SYNDROME;

EID: 0031564828     PISSN: 03043940     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0304-3940(97)00474-6     Document Type: Article

References (33)

1. Abe H., Yagishita S., Amano N., Iwabuchi K., Hasegawa K., Kowa K. Argyrophilic glial intracytoplasmic inclusions in multiple system atrophy. Acta Neuropathol. 84:1992;273-277.
2. Anderton B.H., Breinburg D., Downes M.J., Green P.J., Tomlinson B.E., Ulrich J., Wood J.N., Kahn J. Monoclonal antibodies show that neurofibrillary tangles and neurofilaments share antigenic determinants. Nature. 298:1982;84-86.
3. Biernat J., Mandelkow E.-M., Schroter C., Lichtenberg-Kraag B., Steiner B., Berling B., Meyer H., Mercken M., Vandermeeren A., Goedert M., Mandelkow E. The switch of tau protein to an Alzheimer-like state includes the phosphorylation of two serine-proline motifs upstream of the microtubule binding region. EMBO J. 11:1992;1593-1597.
4. Binder L.I., Frankfurter A., Rebhun L.I. The distribution of tau in the mammalian central nervous system. J. Cell Biol. 101:1985;1371-1378.
5. Brion J.-P., Couck A.-M., Robertson J., Loviny T.L.F., Anderton B.H. Neurofilament monoclonal antibodies RT97 and 8D8 recognize different modified epitopes in paired helical filament-τ in Alzheimer's disease. J. Neurochem. 60:1993;1372-1382.
6. Costa C., Duyckaerts C., Cervara P., Hauw J.-J. Oligodendroglial inclusions, a marker of multisystemic atrophies. Rev. Neurol. Paris. 148:1992;274-280.
7. Davis D.R., Brion J.-P., Couck A.M., Gallo J.-M., Hanger D.P., Ladhani K., Lewis K., Miller C.C.J., Rupniak T., Smith C., Anderton B.H. The phosphorylation state of the microtubule-associated protein tau is affected by glutamate, colchicine and beta-amyloid in primary rat cortical neuronal cultures. Biochem. J. 309:1995;941-949.
8. Feany M.B., Ksiezak-Reding H., Liu W.-K., Vincent I., Yen S.-H.C., Dickson D.W. Epitope expression and hyperphosphorylation of tau protein in corticobasal degeneration: differentiation from progressive supranuclear palsy. Acta Neuropathol. 90:1995;37-43.
9. Feany M.B., Dickson D.W. Neurodegenerative disorders with extensive tau pathology: a comparative study and review. Ann. Neurol. 40:1996;139-148.
10. Goedert M., Spillantini M.G., Cairns N.J., Crowther R.A. Tau proteins of Alzheimer paired helical filaments: abnormal phosphorylation of all six isoforms. Neuron. 8:1992;159-168.
11. Goedert M., Jakes R., Crowther R.A., Cohen P., Vanmechelen E., Vandermeeren M., Cras P. Epitope mapping of monoclonal antibodies to the paired helical filaments of Alzheimer's disease: identification of phosphorylation sites in tau protein. Biochem. J. 301:1994;871-877.
12. Goedert M., Jakes R., Vanmechelen E. Monoclonal antibody AT8 recognises tau protein phosphorylated at both serine 202 and threonine 205. Neurosci. Lett. 189:1995;167-170.
13. Graham J.C., Oppenheimer D.R. Orthostatic hypotension in a case of multiple system atrophy. J. Neurol. Neurosurg. Psychiat. 32:1969;28-34.
14. Hanger D.P., Brion J.-P., Gallo J.-M., Cairns N.J., Luthert P.J., Anderton B.H. Tau in Alzheimer's disease and Down's syndrome is insoluble and abnormally phosphorylated. Biochem. J. 275:1991;99-104.
15. Hanger D.P., Hughes K., Woodgett J.R., Brion J.-P., Anderton B.H. Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: generation of paired helical filament epitopes and neuronal localisation of the kinase. Neurosci. Lett. 147:1992;58-62.
16. Horoupian D.S., Dickson D.W. Striatonigral degeneration, olivopontocerbelar atrophy and atypical Pick disease. Acta Neuropathol. 81:1991;287-295.
17. Irving E.A., Nicoll J., Graham D.I., Dewar D. Increased tau immunoreactivity in oligodendrocytes following human stroke and head injury. Neurosci. Lett. 213:1996;189-192.
18. Kato S., Nakamura H. Cytoplasmic argyrophilic inclusions in neurons of pontine nuclei in patients with olivopontocerebellar atrophy: immunohistochemical and ultrastructural studies. Acta Neuropathol. 79:1990;584-594.
19. Kobayashi K., Miyazu K., Katsukawa K., Fukutani Y., Mukai M., Nakamura I., Yamaguchi N., Matsubara R., Isaki K. Cytoskeletal protein abnormalities in patients with olivopontocerebellar atrophy: an immunocytochemical and Gallyas silver impregnation study. Neuropathol. Appl. Neurobiol. 18:1992;237-249.
20. Lantos P.L., Papp M.I. Cellular pathology of multiple system atrophy: a review. J. Neurol. Neurosurg. Psychiatry. 57:1994;129-133.
21. Lichtenberg-Kraag B., Mandelkow E.-M., Biernat J., Steiner B., Schroter C., Gustke N., Meyer H.E., Mandelkow E. Phosphorylation-dependent epitopes of neurofilament antibodies on tau protein and relationship with Alzheimer tau. Proc. Natl. Acad. Sci. USA. 89:1992;5384-5388.
22. Mercken M., Vandermeeren M., Lubke U., Six J., Boons J., Van-de-Voorede A., Martin J.-J., Gheuens J. Monoclonal antibodies with selective specificity for Alzheimer tau and directed against phosphatase-sensitive epitopes. Acta Neuropathol. 84:1992;265-272.
23. Miller C.C., Brion J.-P., Calvert R., Chin T.K., Eagles P.A., Downes M.J., Flament-Durand J., Haugh M., Kahn J., Probst A., Ulrich J., Anderton B.H. Alzheimer's paired helical filaments share epitopes with neurofilament side arms. EMBO J. 5:1986;269-276.
24. Mirra S.S., Heyman A., McKeel D., Sumi S.M., Crain B.J., Brownlee L.M., Vogel F.S., Hughes J.P., van Belle G., Berg L., et al. The consortium to establish a registry for Alzheimer's disease (CERAD), II: standardization of the neuropathological assessment of Alzheimer's disease. Neurology. 41:1991;479-486.
25. Mulot S.F.C., Hughes K., Woodgett J.R., Anderton B.H., Hanger D.P. PHF-tau from Alzheimer's brain comprises four species on SDS-PAGE which can be mimicked by in vitro phosphorylation of human brain tau by glycogen synthase kinase-3β FEBS Lett. 349:1994;359-364.
26. Murayama S., Arima K., Nakazato Y., Satoh J., Oda M., Inose T. Immunocytochemical and ultrastructural studies of neuronal and oligodendroglial cytoplasmic inclusions in multiple system atrophy. Acta Neuropathol. 84:1992;32-38.
27. Papp M.I., Kahn J.E., Lantos P.L. Glial cytoplasmic inclusions in the CNS of patients with multiple system atrophy (striatonigral degeneration, olivopontocerebellar atrophy and Shy-Drager syndrome). J. Neurol. Sci. 94:1989;79-100.
28. Papp M.I., Lantos P.L. Accumulation of tubular structures in oligodendroglial and neuronal cells as the basic alteration in multiple system atrophy. J. Neurol. Sci. 107:1992;172-182.
29. Probst A., Tolnay M., Langui D., Goedert M., Spillantini M.G. Pick's disease: hyperphosphorylated tau protein segregates to the somatoaxonal compartment. Acta Neuropathol. 92:1996;588-596.
30. Spillantini M.G., Crowther R.A., Goedert M. Comparison of the neurofibrillary pathology in Alzheimer's disease and familial presenile dementia with tangles. Acta Neuropathol. 92:1996;42-48.
31. Sternberger L.A., Sternberger N.H. Monoclonal antibodies distinguish phosphorylated and nonphosphorylated forms of neurofilaments in situ. Proc. Natl. Acad. Sci. USA. 80:1983;6126-6130.
32. Tamaoka A., Mizusawa H., Mori H., Shoji S. Ubiquitinated αB-crystallin in glial cytoplasmic inclusions from the brain of a patient with multiple system atrophy. J. Neurol. Sci. 129:1995;192-198.
33. Trojanowski J.Q., Lee V.M.-Y. Phosphorylation of paired helical filament tau in Alzheimer's disease neurofibrillary lesions: focusing on phosphatases. Fed. Am. Soc. Exp. Biol. J. 9:1995;1570-1576.