Abstract
The structural basis of the cellular disturbance in Alzheimer’s disease (AD) may involve the cytoskeleton. One of the major constituents of the cytoskeleton is the microtubule network. This is composed primarily of tubulin which has a molecular weight of 55 kd and assembles, under certain conditions, to form the microtubules (Cleveland et al., 1977). Other microtubular components include the microtubule associated proteins (MAPS), MAP I and MAP II, and Tau proteins, which co-purify with MAPs. “Tau” represents a class of several proteins which will be referred to collectively as Tau protein.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Andrews, P.W. Retinoic acid induces neuronal differentiation of a cloned human embryonal carcinoma cell line in vitro. Dev. Biol. 103, 285–293, (1984).
Argasinski, A., Sternberg, H., Fingado, B., Huynh, H., Timiras, P.S. Doxorubicin Effects Tau Protein Metabolism In Human Neuroblastoma Cells. Neurochemical Research, in press).
Argasinski, A., Fingado, B., Huynh, H., Sternberg, H., and Timiras, P.S. “Tau Protein in Alzheimer’s Disease: Doxorubicin Effects in Cultured Human Cells” (abstract) American Physiological Soc. 1988.
Baudier, J., and Cole, R.D., Phosphorylation of tau proteins to a state like that in Alzheimer brain is catalyzed by a calcium/calmodulin-dependent kinase and modulated by phospholipids, J. Biol. Chem. 1987, 262: 17584–17590.
Biedler, J.L., Helson, L., and Spengler, B.A. Morphology and growth, tumorigenicity, and cytogenetics of human neuroblastoma cells in continuous culture. Cancer Res., 33, 2643–2652 (1973).
Binder, L.I., Frankfurter, A., and Rebhun, L.I. Differential localization of MAP-2 and tau in mammalian neurons in situ “ Ann. N.Y. Acad. Sci. 1986 466: 145–66.
Butler, M., and Shelanski, M.L., Microheterogeneity of microtubuleassociated tau proteins in living cells“ J. Neurochem. 47, 1517–22 (1986).
Chapman, J., Sela, B.A., Wertman, E., Michaelson, D., “Antibodies to Ganglioside GM1 in Patients with Alzheimer’s Disease” Neurosci. Lett. 1988 Mar 31 86 (2): 235–240.
Cho, E.S., Spencer, P.S., and Jortner, B.S. Doxorubicin, in Experimental and Clinical Neurotoxicology. P.S. Spencer and H.H. Schaumberg, eds. Wilkins and Wilkins, Baltimore, pp. 430–439 (1980).
Cleveland, D.W., Hwo, S.Y., Kirschner, M.W. “Physical and Chemical Properties of Purified Tau Factor and the Role of Tau in Microtubule Assembly” J. Mol. Biol. 1977 116: 227–247.
Cole, G.M. An in vitro Model for Alzheimer’s Disease Pathology. Ph.D. Dissertation, University of California, Berkeley, (1986).
Cole, G.M. and Timiras, P.S. Aging-related pathology in human neuroblastoma and teratocarcinoma cell lines. In Model Systems of Development and Aging of the Nervous System, A. Vernadakis et al., eds., Martinus Nijhoff Publ., Boston, pp. 453–473 (1987a).
Cole, G.M. and Timiras, P.S. Ubiquitin-protein conjugates in Alzheimer’s lesions. Neurosci. Let. 79, 207–212, (1987b).
Cole, G.M., Wu, K., and Timiras, P.S. A culture model for age-related human neurofibrillary pathology. Int. J. Dev. Neurosci. 3, 23–32 (1985).
Cole, GM. Dobkins, K.R., Hansen, L.A., Terry, R.D. and Saitoh, T. (1988) Brain Res., in press.
Drubin, D.G., Kirschner, M.W. “Tau Protein Function in Living Cells” J. Cell. Biol. 1986 103 (No.6 Pt. 2) p. 2739–2746.
Drubin, D.G., Feinstein, S.C., Shooter, E.M., and Kirschner, M.W. Nerve Growth Factor Induced Neurite Outgrowth in PC12 Cells Involves the Coordinated Induction of Microtubule Assembly and Assembly Promoting Factors. J. Cell. Biol. 101, 1799–1807 (1985).
Geddes, J.W., Monaghan, D.T., Cotman, C.W., Cott, I.T., Kim, R.C., and Chui, H.C. Plasticity of hippocampal circuitry in Alzheimer’s disease. Science, 230 (4730) 1179–81 (1985).
Goedert, M., Wischik, C.M., Crowther, R.A., Walker, J.E., and Klug, A. Cloning and sequencing of the cDNA encoding a core protein of the paired helical filaments of Alzheimer’s disease: identification as the microtubule-associated protein Tau. Proc. Natl. Acad. Sci. USA, 85, 11, 4051–4055 (1988).
Grundke-Iqbal, I., Iqbal, K., Tung, Y.C., Quinlan, M., Wisniewski, H.M., and Binder, L.I. Abnormal phosphorylation of microtubule-associated protein (Tau) in Alzheimer cytoskeletal pathology. Proc. Natl. Acad. Sci. USA, 83, 4913–4917 (1986).
Haas, A.L., and Bright, P. M. The immunochemical detection and quantitation of intracellular ubiquitin-protein conjugates. J. Cell Biol., 260, 23, 12464–12473 (1985).
Hoshi, M., Nishida, E., Miyata, Y., Sakai, H., Miyoshi, T., Ogawara, H., and Ayikama, T. “Protein kinase C phosphorylates Tau and induces its functional alterations” FEBS Letters 1987, June 15, 217 (2): 237–41.
Iqbal, K., Grundke-Iqbal, I., Zaidi, T., Merz, P.A., Wen, G.Y., Shaikh, S.S., Wisniewski, H.M. “Defective brain microtubule assembly in Alzheimer’s Disease” Lancet, 1986 Aug. 23, 2 (8504): 421–426.
Kosik, K.S. Joachim, C.L. and Selkoe, D. J. Microtubule-associated protein tau is a major antigenic component of paired helical filaments in Alzheimer disease. Proc. Natl. Acad. Sci. USA, 83, 4044–4048 (1986).
Kowall, N.W., Kosik, K.S. “The Cytoskeletal Pathology of Alzheimer’s Disease is Characterized by Aberrant Tau Distribution” Ann. Neurol. 22: 639–43, 1987.
Lamour, Y., Scarna, H., Roudier, M., Safer, S., and Davous, P. Serum Neuron-specific enolase in senile dementia of the Alzheimer’s type, Neurology 1987 37: 768–772.
Lee, G., Cowan, N., and Kirschner, M.W. “The Primary Structure and Heterogeneity Tau Protein from Mouse Brain” Science 239: 285–89, 1988.
Lindwall, G., and Cole, D. The purification of Tau protein and the occurrence of two phosphorylation states of Tau in brain. J. Biol. Chem, 259, 19, 12241–12245 (1984).
Love, S., Saitoh, T., Quiada, S., Cole, G.M., and Terry, R.D. “Alz-50, ubiquitin, and Tau immunoreactivity of neurofibrillary tangles, Pick’s bodies, and Lewy bodies” J. Neuropath. Exp. Neurol. 1988 Jul. 47 (4): 393–405.
Mesco, E.R., Sternberg, H., Timiras, P.S. Immunological Identification of Tau Protein in Neuroblastoma Cells. American Aging Association, San Francisco, CA (1988).
Miyata, Y., Hoshi, M., Mishida, E., Minami, Y., and Sakai, H. “Binding of MAP-2 and Tau to the intermediate filament reassembled from the neurofilament 70kDa subunit protein; Its regulation by Calmodulin” J. Biol. Chem. 1986, 261 (28): 13026–13030.
Murti, K.G., Smith, H.,T., and Fried, V.A. “Ubiquitin is a Component of the Microtubule Network” Proc. Nat. Acad. Sci. U.S.A. 85(9):1301923, 1988.
Probst, A., Basler, V., Bron, B.,-and Ulrich, J. Neuritic plaques in senile dementia of Alzheimer’s type: a golgi analysis in the hippocampal region. Brain Res. 268 (2), 249–254 (1983).
Selden, S.C. and Pollard, T.D. Phosphorylation of microtubule associated protein regulates their interation with filaments. J. Biol. Chem. 258, 7064–7071 (1983).
Sternberg, H., Mesco, G., Argasinski, A.B., Sanchez, I., and Timiras, P.S. Tau protein in LAN-5 cells. American Society for Neurochemistry (abstracts ), New Orleans, LA, (1988a).
Sternberg, H., Baudier, J., Akizuki, K., Cole, G., Martin, W.H., Creutz, C.E., and Timiras, P.S., Similarities and differences between Tau protein and chromobindin A. Neurochem. Inter., (accepted Jan. 1988b ).
Sternberg, H., Mesco, G., Fingado, B.H., Petrie, R., Dao, Q., Cole, G.M., and Timiras, P. S. Differentiation of a human neuroblastoma cell line influences Tau protein. Int. Soc. Develop. Neurosci. (abstracts), Jerusalem, Israel, (1988c).
Wolozin, B.L., Pruchnicki, A., Dickson, D.W., and Davies, P. A neuronal antigen in the brains of Alzheimer patients. Science, 232, 4750, 648–50 (1986).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1990 Springer Science+Business Media New York
About this chapter
Cite this chapter
Sternberg, H., Mesco, G., Cole, G., Timiras, P.S. (1990). Tau Protein: Its Presence and Metabolism in Human Neuroblastoma Cells. In: Lauder, J.M., Privat, A., Giacobini, E., Timiras, P.S., Vernadakis, A. (eds) Molecular Aspects of Development and Aging of the Nervous System. Advances in Experimental Medicine and Biology, vol 265. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-5876-4_27
Download citation
DOI: https://doi.org/10.1007/978-1-4757-5876-4_27
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4757-5878-8
Online ISBN: 978-1-4757-5876-4
eBook Packages: Springer Book Archive