Abstract
The level of mRNA for an amyloid precursor (APP770) containing a Kunitz-type trypsin inhibitor (PI) is elevated in the autopsied Alzheimer brain.1 However, the physiological significance of the augumented APP770 production has not been clarified thus far.
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
S. Tanaka, S. Nakamura, K. Ueda, M. Kameyama, S. Siojiri, Y.Takahashi, N. Kitaguchi, and H. Ito: Three types of amyloid protein precursor mRNA in human brain: Their differential expression in Alzheimer’s disease, Biochem.Biophys.Res.Commun. 157: 472 (1988).
P. Davies and A. J. F. Maloney: Selective loss of central cholinergic neurons in Alzheimer’s disease, Lancet 2: 1403 (1976).
K. Koshimura, T. Kato, I. Tohyama, S. Nakamura, and M. Kameyama: Qualitative abnormalities of choline acetyltransferase in Alzheimer type dementia, J.Neurol.Sci. 76: 143 (1986).
S. G. Younkin, B. Goodridge, J. Katz, G. Lockett, D. Nafziger, M. F. Usik, and L. H. Younkin: Molecular forms of acetylcholinesterase in Alzheimer’s disease, Fed.Proc. 45: 2982 (1986).
M. M. Mesulam and M. A. Moran: Cholinesterases within neurofibrillary tangles related to age and Alzheimer’s disease, Ann.Neurol. 22: 223 (1987).
N. Kitaguchi, Y. Takahashi, Y. Tokushima, S. Shiojiri, and H. Ito: Novel precursor of Alzheimer’s disease amyloid protein shows protease inhibitory activity, Nature 331: 530 (1988).
E. G. Gray and V. P. Whittaker: The isolation of nerve endings from brain. An electron microscopic study of all fragments derived by homogenisation and centrifugation, J.Anat. 96: 79 (1962).
J. M. Candy, J. Klinowski, R. H. Perry, E. K. Perry, A. Fairbairn, A. E. Oakley, T. A. Carpenter, J. R. Atack, G. Blessed, and J. A. Edwardson: Aluminosilicates and senile plaque formation in Alzheimer’s disease, Lancet 1: 354 (1986).
S. Nakamura, S. Kawashima, S. Nakano, T. Tsuji, and W. Araki: Sub-cellular distribution of acetylcholinesterase in Alzheimer’s disease: Abnormal localization and solubilization, J.Neural Trans., in press.
S. G. Younkin, C. Rosenstein, P. C. Collins, and T. I. Rasenberry: Cellular localization of the molecular forms of acetylcholinesterase in rat diaphragm, J.Biol.Chem. 257: 13630 (1982).
R. G. Martin and B. N. Ames: A method for determining the sedimentation behavior of enzymes — Application to protein mixtures, J.Biol.Chem. 236: 1372 (1961).
S. Nakano, T. Kato, S. Nakamura, and M. Kameyama: Acetylcholinesterase activity in cerebrospinal fluid of patients with Alzheimer’s disease and senile dementia, J.Neurol.Sci. 75: 213 (1986).
C. D. Johnson and R. L. Russell: A rapid, simple radiometric assay for cholinesterase, suitable for multiple determinations, Anal. Biochem. 64: 229 (1975).
O. H. Lowry, N. J. Rosebrough, A. L. Farr, and R. J. Randall: Protein measurement with the Folin phenol reagent, J.Biol.Chem. 193: 265 (1951).
D. H. Small and R. J. Simpson: Acetylcholinesterase undergoes autolysis to generate trypsin-like activity, Neurosci.Lett. 89: 223 (1988).
C. R. Abraham, D. J. Selkoe, and H. Potter: Immunochemical identification of the serine protease inhibitor a-l-antichymotrypsin in the brain amyloid deposits of Alzheimer’s disease, Cell 52: 487 (1988).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1990 Plenum Press, New York
About this chapter
Cite this chapter
Nakamura, S. et al. (1990). Protease Inhibitor and Cholinergic System in Alzheimer’s Disease. In: Nagatsu, T., Fisher, A., Yoshida, M. (eds) Basic, Clinical, and Therapeutic Aspects of Alzheimer’s and Parkinson’s Diseases. Advances in Behavioral Biology, vol 38A. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5844-2_8
Download citation
DOI: https://doi.org/10.1007/978-1-4684-5844-2_8
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-5846-6
Online ISBN: 978-1-4684-5844-2
eBook Packages: Springer Book Archive