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Tau Protein: Its Presence and Metabolism in Human Neuroblastoma Cells

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Molecular Aspects of Development and Aging of the Nervous System

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 265))

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.

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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).

    Google Scholar 

  • Argasinski, A., Sternberg, H., Fingado, B., Huynh, H., Timiras, P.S. Doxorubicin Effects Tau Protein Metabolism In Human Neuroblastoma Cells. Neurochemical Research, in press).

    Google Scholar 

  • 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.

    Google Scholar 

  • 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.

    Google Scholar 

  • 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).

    Google Scholar 

  • 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.

    Article  Google Scholar 

  • Butler, M., and Shelanski, M.L., Microheterogeneity of microtubuleassociated tau proteins in living cells“ J. Neurochem. 47, 1517–22 (1986).

    Article  Google Scholar 

  • 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.

    Google Scholar 

  • 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).

    Google Scholar 

  • 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.

    Article  Google Scholar 

  • Cole, G.M. An in vitro Model for Alzheimer’s Disease Pathology. Ph.D. Dissertation, University of California, Berkeley, (1986).

    Google Scholar 

  • 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).

    Google Scholar 

  • Cole, G.M. and Timiras, P.S. Ubiquitin-protein conjugates in Alzheimer’s lesions. Neurosci. Let. 79, 207–212, (1987b).

    Article  Google Scholar 

  • 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).

    Article  Google Scholar 

  • Cole, GM. Dobkins, K.R., Hansen, L.A., Terry, R.D. and Saitoh, T. (1988) Brain Res., in press.

    Google Scholar 

  • Drubin, D.G., Kirschner, M.W. “Tau Protein Function in Living Cells” J. Cell. Biol. 1986 103 (No.6 Pt. 2) p. 2739–2746.

    Article  Google Scholar 

  • 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).

    Article  Google Scholar 

  • 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).

    Article  Google Scholar 

  • 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).

    Article  Google Scholar 

  • 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).

    Article  Google Scholar 

  • 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).

    Google Scholar 

  • 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.

    Article  Google Scholar 

  • 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.

    Google Scholar 

  • 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).

    Google Scholar 

  • 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.

    Article  Google Scholar 

  • 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.

    Article  Google Scholar 

  • Lee, G., Cowan, N., and Kirschner, M.W. “The Primary Structure and Heterogeneity Tau Protein from Mouse Brain” Science 239: 285–89, 1988.

    Article  Google Scholar 

  • 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).

    Google Scholar 

  • 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.

    Article  Google Scholar 

  • Mesco, E.R., Sternberg, H., Timiras, P.S. Immunological Identification of Tau Protein in Neuroblastoma Cells. American Aging Association, San Francisco, CA (1988).

    Google Scholar 

  • 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.

    Google Scholar 

  • 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.

    Google Scholar 

  • 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).

    Google Scholar 

  • Selden, S.C. and Pollard, T.D. Phosphorylation of microtubule associated protein regulates their interation with filaments. J. Biol. Chem. 258, 7064–7071 (1983).

    Google Scholar 

  • 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).

    Google Scholar 

  • 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 ).

    Google Scholar 

  • 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).

    Google Scholar 

  • 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).

    Article  Google Scholar 

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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

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  • 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

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