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Ubiquitin is a component of polypeptides purified from corpora amylacea of aged human brain

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Abstract

Corpora amylacea (CA) are one of the conspicuous features of brain tissue in normal aging and neurodegenerative diseases. Quantitative protein determination of purified CA revealed a protein content of about 4% of total weight. Qualitative protein analysis revealed a broad range of polypeptides, with four being more abundant. High performance liquid chromatography (HPLC), fractionation of this protein material showed four peaks which are related to the four major polypeptides with molecular weights of 24 KD, 42 KD, 94 KD, and 133 KD. Amino acid content analysis of the 24 KD, 42 KD and 94 KD polypeptides indicated that distinct protein species are involved. N-terminal amino acid sequence analysis of the 24 KD and 42 KD polypeptides revealed in both cases homology with the N-terminal sequence of human ubiquitin.

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References

  1. Anzil, A. P., Herrlinger, H., Blinzinger, K., and Kronski, D. 1974. Intraneuritic Corpora amylacea. Virchows Arch. A. Path. Anat. Histol. 364:297–304.

    Google Scholar 

  2. Ramsey, H. J. (1965). Ultrastructure of Corpora amylacea. J. Neuropathol. Exp. Neurol. 24:25–39.

    PubMed  Google Scholar 

  3. Palmucci, L., Anzil, A. P., and Luh, S. (1982). Intra-astrocytic glycogen granules and Corpora amylacea stain positively for polyglucosans: A cytochemical contribution on the fine structural polymorphism of particulate polysaccharide. Acta Neuropathol. (Berl), 57:99–102.

    Google Scholar 

  4. Alder, N. (1953). On the nature, origin and distribution of the Corpora amylacea of the brain with observation on some new staining reactions. Br. J. Psychiat., 99:689–697.

    Google Scholar 

  5. Averback, P. (1981). Parasynaptic Corpora amylacea in the striatum. Arch. Pathol. Lab. Med., 105:334–335.

    PubMed  Google Scholar 

  6. Ellis, R. T. (1920). Norms for some structural changes in the human cerebellum from birth to old age. The J. Comp. Neurol., 32:1–33.

    Google Scholar 

  7. Fleming, P. D., Cordoza, M. E., Woods, S. G., Griesbach, E. J. and Worcester, M. A. (1987). Corpora amylacea increased in Alzheimer's disease. Neurology (suppl. 1), 37:157.

    Google Scholar 

  8. Robitaille, Y., Carpenter, S., Karpati, G. and DiMauro, S. (1980). A distinct form of adult polyglucosan disease with massive involvement of central and peripheral neuronal processes and astrocytes. Brain, 103:315–336.

    PubMed  Google Scholar 

  9. Fleming, P. D. and Rogers, J. (1986) Neuropathology of olfactory system in Alzheimer's disease and normal aging. Soc. Neurosci. Abstr., 12:1314.

    Google Scholar 

  10. Roukema, P. A., and Oderkerk, C. H. (1970). Isolation and preliminary characterization of Corpora amylacea from human brains. Psychiat. Neurol. Neurochir. 73:87–89.

    PubMed  Google Scholar 

  11. Stam, F. C. and Roukema, P. A. (1973) Histochemical and biochemical aspects of Corpora amylacea. Acta Neuropathol. (Berl), 25:95–102.

    Google Scholar 

  12. Sakai, M., Austin, J., Witmer, F. and Trueb, L. (1969a). Studies of Corpora amylacea. I: Isolation and preliminary characterization by chemical and histochemical techniques. Arch. Neurol., 21:526–544.

    PubMed  Google Scholar 

  13. Sakai, M., Austin, J., Witmer, F. and Trueb, L. (1969b) Corpora amylacea: Isolation, characterization and significance. Trans. Am. Neurol. Assoc., 94:336–338.

    PubMed  Google Scholar 

  14. Steyaert, A., Cissé, S., Merhi, Y., Kalbakji, A., Reid, N., Gauvreau, D. and Lacoste-Royal, G. (1990). Purification and polypeptide composition of corpora amylacea from aged human brain. J. Neurosci. Meth., 31:59–64.

    Google Scholar 

  15. Selkoe, D. J. (1986). Altered structural proteins in plaques and tangles: What do they tell us about the biology of Alzheimer's disease? Neurobiol. Aging 7:425–432.

    PubMed  Google Scholar 

  16. Selkoe, D. J. (1989). Biochemistry of altered brain proteins in Alzheimer's disease. Ann. Rev. Neurosci., 12:463–490.

    PubMed  Google Scholar 

  17. Lew, E. O., Rozdilsky, B., Munoz, D. G. and Perry, G. (1989). A new type of neuronal cytoplasmic inclusion: histological, ultrastructural, and immunochemical studies. Acta Neuropathol., 77:599–604.

    PubMed  Google Scholar 

  18. Perry, G. (1987). Alterations of the neuronal cytoskeleton in Alzheimer disease. (G. Perry, ed.) p. 229, Plenum Press, New York.

    Google Scholar 

  19. Zhang, H., Sternberger, N. H., Rubinstein, L. J., Herman, M. M., Binder, L. I., and Sternberger, L. A. 1989. Abnormal processing of multiple proteins in Alzheimer disease. Proc. Natl. Acad. Sci. USA 86:8045–8049.

    PubMed  Google Scholar 

  20. Weidmann, A., König, G., Bunke, D., Fischer, P., Salbaum, J. M., Masters, C. L., and Beyreuther, K. (1989). Identification, biogenics, and localization of precursors of Alzheimer's disease A4 amyloid protein. Cell, 57:115–126.

    PubMed  Google Scholar 

  21. Lowe, J., Blanchard, A., Morrell K., Lennox, G., Reynolds, L., Billett, M., Landon, M. and Mayer, R. J. (1988). Ubiquitin is a common factor in intermediate filament inclusion bodies of diverse type in man, including those of Parkinson's disease, Pick's disease and Alzheimer's disease, as well as Rosenthal fibers in cerebellar astrocytics, cytoplasmic bodies in muscle and Mallory bodies in alcoholic liver disease. J. Pathol., 155:9–15.

    PubMed  Google Scholar 

  22. Manetto, V., Perry, G., Tabaton, M., Mulvihill, P., Fried, V. Smith, H., Gambetti, P., and Autilio-Gambetti, L. (1988) Ubiquitin is associated with abnormal cytoplasmic filaments characteristic of neurodegenerative diseases. Proc. Natl., Acad. Sci, USA, 84:4501–4505.

    Google Scholar 

  23. Manetto, V., Abdul-Karim, F. W., Perry, G., Tabaton, M., Autilio-Gambetti, L., and Gambetti, P. (1989). Selective presence of ubiquitin intracellular inclusions. Ann. J. Pathol. 134,3:505–513.

    Google Scholar 

  24. Power, D. M., Hue, D., Brion, J. P., Kahn, J., and Anderton, B. H. (1988). Neuronal inclusion in Alzheimer's, Parkinson's and Pick's diseases. Neurosci. Lett., 22:S55.

    Google Scholar 

  25. Cole, G. M., and Timiras, P. S. (1987) Ubiquitin-protein conjugates in Alzhimer's lesions. Neurosci. Lett. 79:207–212.

    PubMed  Google Scholar 

  26. Perry, G., Mulvihill, P., Pried, V. A., Smith, H. T., GrundkeIqbal, I., and Iqbal, K. 1989. Immunochemical properties of ubiquitin conjugates in the paired helical filaments of Alzheimer's disease. J. Neurochem, 52:1523–1528.

    PubMed  Google Scholar 

  27. Goldstein, G., Sheid, M., Hammerling, V., Boyse, E. A., Schlesinger, D. M., and Nail, H. D. 1975. Isolation of polypeptide that has lymphocyte differentiating properties and is probably represented universally in living cells. Proc. Natl. Acad. Sci. USA, 72:11–15.

    PubMed  Google Scholar 

  28. Finley, D., and Varshavsky, A. (1985). The ubiquitin system: Fonctions and mechanisms. Trends Biochem. Sci., 10:343–346.

    Google Scholar 

  29. Hershko, A., and Ciechanover, A. (1986). The ubiquitin pathway for the degradation of intracellular proteins. Prog. Nucleic Acid Res. Mol. Biol., 33:19–56.

    PubMed  Google Scholar 

  30. Hershko, A., Ciechanover, A., Heller, H., and Haasarose, I.A. (1980). Proposed role of ATP in protein breakdown: Conjugation of proteins with multiple chains of polypeptide ATP-dependant proteolysis. Proc. Natl. Acad. Sci. USA, 77:1783–1786.

    PubMed  Google Scholar 

  31. Dice, J.F. (1987). Molecular determinants of protein half-lives in eukaryotic cells. FASEB, J., 1:349–357.

    Google Scholar 

  32. Busch, M., and Goldnopf, I. L. (1982). Ubiquitin-protein conjugates. Mol. Cell. Biochem., 40:173–187.

    Google Scholar 

  33. St-John, T., Gallatin, W. M., Siegelman, M., Smith, H. T., Fried, V. A., and Weissman, I. L. (1986). Expression, cloning of a lymphocyte homing receptor cDNA: Ubiquitin is the reactive species. Science, 231:845–850.

    PubMed  Google Scholar 

  34. Siegelman, M., Bond, M. W., Gallatin, MW, St-John, T., Smith, H. T., Fried, V. A., and Weissman, I. L. (1986). Cell surface molecule associated with lymphocyte homing is ubiquitin branchedchain glycoprotein. Science, 231:823–829.

    PubMed  Google Scholar 

  35. Murti, K. G., Smith, H. T., and Fried, V. A. 1988. Ubiquitin is a component of the microtule network. Proc. Natl. acad. Sci. USA, 85:3019–3023.

    PubMed  Google Scholar 

  36. Ball, E., Karlik, C. C., Beall, C. J., Saville, D. L., Saparrow, J. C., Bullard, B., and Fryberg E. A. (1987). Arthrin, a myofibrillar protein of insect flight muscle, is actin-ubiquitin conjugate. Cell, 51:221–228.

    PubMed  Google Scholar 

  37. Yarden, Y., Escobedo, J. A., Kuang, W. J., Yang-Feng, T. L., Daniel, T. D., Tremble, P. M., Chen, E. Y., Ando, M. E., Harkins, R. N., Francke, U., Fried, V. A., Ullrich, A., and Williams, L. T. (1986). Structure of receptor for platelet-derived growth factor helps define a family of related growth factor receptor. Nature, 323:226–232.

    PubMed  Google Scholar 

  38. Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227:680–685.

    PubMed  Google Scholar 

  39. Schlesinger, D. H., and Goldstein, G. (1975). Ubiquitin: Human, complete sequence with experimental details. Nature, 255:423–424.

    PubMed  Google Scholar 

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Cissé, S., Lacoste-Royal, G., Laperrière, J. et al. Ubiquitin is a component of polypeptides purified from corpora amylacea of aged human brain. Neurochem Res 16, 429–433 (1991). https://doi.org/10.1007/BF00965562

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