Summary
AChE activity was detected mainly in membrane-bound fractions in the frontal cortex of autopsied control or Alzheimer brain as well as rat cerebral cortex. However, the distribution of AChE among various membrane fractions was different between control and Alzheimer brains. The highest specific activity was detected in the fraction enriched with senile plaque, which was obtained from the Alzheimer brain by sonication, solubilization with detergent and centrifugation on a sucrose density gradient. The senile plaque enriched fraction was incubated with purified collagenase or protease and centrifuged at 100,000 g for 60 min. More than 50% of AChE activity was detected in the supernatant fraction. AChE in the supernatant solution showed a property of G4 isozyme. AChE might probably be anchored to the senile plaque through its collagen tail and be solubilized with collagenase or protease, producing a G4 isozyme.
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References
Abraham CR, Selkoe DJ, Potter H (1988) Immunochemical identification of the serine protease inhibitor α1-antichymotrypsin in the brain amyloid deposits of Alzheimer’s disease. Cell 52:487–501
Allsop D, Landon M, Kidd M (1983) The isolation and amino acid composition of senile plaque core protein. Brain Res 259:348–352
Atack JR, Perry EK, Perry RH, Wilson ID, Bober MJ, Blessed G, Tomlinson BE (1985) Blood acetyl- and butyrylcholinesterase in senile dementia of Alzheimer type. J Neurol Sci 70:1–12
Brzin M, Sketelj J, Klinar B (1983) Cholinesterases. In: Lajtha A (ed) Handbook of neurochemistry, vol 4. Plenum Press, New York, pp 251–292
Candy JM, Klinowski J, Perry RH, Perry EK, Fairbairn A, Oakley AE, Carpenter TA, Atack JR, Blessed G, Edwardson JA (1986) Aluminosilicates and senile plaque formation in Alzheimer’s disease. Lancet i:354 –357
Davies P, Maloney AJF (1976) Selective loss of central cholinergic neurons in Alzheimer’s disease. Lancet ii:1403
Ellman GL, Courtney KD, Andrews V Jr, Featherstone RM (1961) A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem Pharmacol 7:88–95
Friede RL (1965) Enzyme histochemical studies of senile plaques. Neuropathol Exp Neurol 24:477–491
Geula C, Mesulam M (1988) Enzymatic properties of cholinesterases in normal human brain and Alzheimer’s disease. Soc Neurosci Abstr 14:155
Gray EG, Whittaker VP (1962) The isolation of nerve endings from brain. An electronmicroscopic study of all fragments derived by homogenisation and centrifugation. J Anat 96:79–88
Hammond P, Brimijoin S (1988) Acetylcholinesterase in Huntington’s and Alzheimer’s diseases: simultaneous enzyme assay and immunoassay of multiple brain regions. J Neurochem 50:1111–1116
Kitaguchi N, Takahashi Y, Tokushima Y, Shiojiri S, Ito H (1988) Novel precursor of Alzheimer’s disease amyloid protein shows protease inhibitory activity. Nature 331:530–532
Koshimura K, Kato T, Tohyama I, Nakamura S, Kameyama M (1986) Qualitative abnormalities of choline acetyltransferase in Alzheimer type dementia. J Neurol Sci 76:143–150
Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193:265–275
Martin RG, Ames BN (1961) A method for determining the sedimentation behavior of enzymes — Application to protein mixtures. J Biol Chem 236:1372–1379
Massoulie J, Bon S (1982) The molecular forms of cholinesterase and acetylcholinesterase in vertebrates. Ann Rev Neurosci 5:57–106
McIntosh CHS, Plummer DT (1976) The subcellular localization of acetylcholinesterase and its molecular forms in pig cerebral cortex. J Neurochem 27:449–457
Mesulam MM, Geula C, Moran MA (1987) Anatomy of cholinesterase inhibition in Alzheimer’s disease: effect of physostigmine and tetrahydroaminoacridine on plaques and tangles. Ann Neurol 22:683–691
Mesulam MM, Moran MA (1987) Cholinesterases within neurofibrillary tangles related to age and Alzheimer’s disease. Ann Neurol 22:223–228
Nagata H, Mimori Y, Nakamura S, Kameyama M (1984) Regional and subcellular distribution in mammalian brain of the enzymes producing adenosine. J Neurochem 42:1001–1007
Nakamura S (1976) Effect of sodium deoxycholate on 5’-nucleotidase. Biochim Biophys Acta 426:339–347
Nakamura S, Yamao S, Ito J, Kameyama M (1979) Purification and properties of 2’-nucleotidase from mammalian brain. Biochim Biophys Acta 568:30–38
Nakano S, Kato T, Nakamura S, Kameyama M (1986) Acetylcholinesterase activity in cerebrospinal fluid of patients with Alzheimer’s disease and senile dementia. J Neurol Sci 75:213–223
Perry EK (1980) The cholinergic system in old age and Alzheimer’s disease. Age Ageing 9:1–8
Perry EK, Gibson PH, Blessed G, Perry RH, Tomlinson BE (1977) Neurotransmitter enzyme abnormalities in senile dementia. Choline acetyltransferase and glutamic acid decarboxylase activities in necropsy tissue. J Neurol Sci 34:247–265
Reisberg B (1986) Dementia: a systematic approach to identifying reversible causes. Geriatrics 41 (4):30–46
Small DH, Simpson RJ (1988) Acetylcholinesterase undergoes autolysis to generate trypsin-like activity. Neurosci Lett 89:223–228
Sottocasa GL, Kuylenstierna B, Ernster L, Bergstrand A (1967) An electron-transport system associated with the outer membrane of liver mitochondria. J Cell Biol 32:415–438
Tanaka S, Nakamura S, Ueda K, Kameyama M, Shiojiri S, Takahashi Y, Kitaguchi N, Ito H (1988) Three types of amyloid precursor mRNA in human brain: their differential expression in Alzheimer’s disease. Biochem Biophys Res Commun 157:472–479
Whittaker VP, Michaelsson IA, Kirkland JA (1964) The separation of synaptic vesicles from nerve-ending particles (synaptosomes). Biochem J 90:293–303
Younkin SG, Goodridge B, Katz J, Lockett G, Nafziger D, Usik MF, Younkin LH (1986) Molecular forms of acetylcholinesterase in Alzheimer’s disease. Fed Proc 45:2982–2988
Younkin SG, Rosenstein C, Collins PL, Rosenbérry TL (1982) Cellular localization of the molecular forms of acetylcholinesterase in rat diaphragm. J Biol Chem 257:13630–13637
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© 1990 Springer-Verlag
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Nakamura, S., Kawashima, S., Nakano, S., Tsuji, T., Araki, W. (1990). Subcellular distribution of acetylcholinesterase in Alzheimer’s disease: abnormal localization and solubilization. In: Gottfries, C.G., Nakamura, S. (eds) Neurotransmitter and Dementia. Journal of Neural Transmission, vol 30. Springer, Vienna. https://doi.org/10.1007/978-3-7091-3345-3_2
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DOI: https://doi.org/10.1007/978-3-7091-3345-3_2
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