메뉴 건너뛰기




Volumn 147, Issue 1, 2000, Pages 33-39

Kinetic analysis of the toxicological effect of tacrine (Cognex®) on human retinal acetylcholinesterase activity

Author keywords

Acetylcholinesterase; Alzheimer's disease; Inhibition; Kinetics; Retina; Tacrine

Indexed keywords

ACETYLCHOLINESTERASE; CHOLINESTERASE INHIBITOR; TACRINE;

EID: 0034685887     PISSN: 0300483X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-483X(00)00177-3     Document Type: Article
Times cited : (34)

References (28)
  • 1
    • 0025074669 scopus 로고
    • Multiple effects of tetrahyroaminoacridine on the cholinergic system: Biochemical and behavioral aspects
    • Adem A., Mohammed A.K., Winblad B. Multiple effects of tetrahyroaminoacridine on the cholinergic system: biochemical and behavioral aspects. J. Neural. Transm. Park. Dis. Dement. Sect. 2:1990;113-128.
    • (1990) J. Neural. Transm. Park. Dis. Dement. Sect. , vol.2 , pp. 113-128
    • Adem, A.1    Mohammed, A.K.2    Winblad, B.3
  • 2
    • 0029902311 scopus 로고    scopus 로고
    • The nature of the inhibition of camel retina acetylcholinesterase (EC 3.1.1.7) activity by tetrahydroaminoacridine
    • Al-Jafari A.A. The nature of the inhibition of camel retina acetylcholinesterase (EC 3.1.1.7) activity by tetrahydroaminoacridine. J. Ocul. Pharmacol. Ther. 12:1996;503-514.
    • (1996) J. Ocul. Pharmacol. Ther. , vol.12 , pp. 503-514
    • Al-Jafari, A.A.1
  • 3
    • 0031637354 scopus 로고    scopus 로고
    • Sensitivity of bovine retinal acetylcholinesterase (EC 3.1.1.7) towards tacrine: Kinetic characterization
    • Al-Jafari A.A., Kamal M.A., Alhomida A.S. Sensitivity of bovine retinal acetylcholinesterase (EC 3.1.1.7) towards tacrine: kinetic characterization. J. Biochem. Mol. Toxicol. 12:1998;245-251.
    • (1998) J. Biochem. Mol. Toxicol. , vol.12 , pp. 245-251
    • Al-Jafari, A.A.1    Kamal, M.A.2    Alhomida, A.S.3
  • 4
    • 0030734590 scopus 로고    scopus 로고
    • Potential role of muscarinic agonists in Alzheimer's disease
    • Avery E.E., Baker L.D., Asthana S. Potential role of muscarinic agonists in Alzheimer's disease. Drugs Aging. 11:1997;450-459.
    • (1997) Drugs Aging , vol.11 , pp. 450-459
    • Avery, E.E.1    Baker, L.D.2    Asthana, S.3
  • 5
    • 0000443666 scopus 로고    scopus 로고
    • The second generation of cholinesterase inhibitors: Clinical and pharmacological effects
    • R. Becker, & E. Giacobini. Boston: Brirkhauser
    • Becker R., Moriearty P., Unni L. The second generation of cholinesterase inhibitors: clinical and pharmacological effects. Becker R., Giacobini E. Cholinergic Basis of Alzheimer's disease. 1997;263-296 Brirkhauser, Boston.
    • (1997) Cholinergic Basis of Alzheimer's Disease , pp. 263-296
    • Becker, R.1    Moriearty, P.2    Unni, L.3
  • 6
    • 0026504115 scopus 로고
    • Interaction of tetrahydroaminoacridine with acetylcholin-esterase and butyrylcholinesterase
    • Berman H.A., Leonard K. Interaction of tetrahydroaminoacridine with acetylcholin-esterase and butyrylcholinesterase. Mol. Pharmacol. 41:1992;412-418.
    • (1992) Mol. Pharmacol. , vol.41 , pp. 412-418
    • Berman, H.A.1    Leonard, K.2
  • 7
    • 0026079024 scopus 로고
    • General occurrence of binding to acetylcholinesterase-substrate complex in noncompetitive inhibition and in inhibition by substrate
    • Cohen S.G., Chishti S.B., Bell D.A., Howard S.I., Salih E., Cohen J.B. General occurrence of binding to acetylcholinesterase-substrate complex in noncompetitive inhibition and in inhibition by substrate. Biochim. Biophys. Acta. 1076:1991;112-122.
    • (1991) Biochim. Biophys. Acta , vol.1076 , pp. 112-122
    • Cohen, S.G.1    Chishti, S.B.2    Bell, D.A.3    Howard, S.I.4    Salih, E.5    Cohen, J.B.6
  • 8
    • 0342331354 scopus 로고
    • The cholinergic synapse and the site of memory
    • Deutsch J. The cholinergic synapse and the site of memory. Science. 313:1985;7-11.
    • (1985) Science , vol.313 , pp. 7-11
    • Deutsch, J.1
  • 9
    • 77049143386 scopus 로고
    • The determination of enzyme inhibitor constant
    • Dixon M. The determination of enzyme inhibitor constant. J. Biochem. 55:1953;170-171.
    • (1953) J. Biochem. , vol.55 , pp. 170-171
    • Dixon, M.1
  • 10
    • 0026513979 scopus 로고
    • Tacrine in Alzheimer's disease. Time course of changes in cognitive function and practice effects
    • Eagger S., Morant N., Levy R., Sahakian B. Tacrine in Alzheimer's disease. Time course of changes in cognitive function and practice effects. Br. J. Psychol. 160:1992;36-40.
    • (1992) Br. J. Psychol. , vol.160 , pp. 36-40
    • Eagger, S.1    Morant, N.2    Levy, R.3    Sahakian, B.4
  • 12
    • 0020694099 scopus 로고
    • Starburst amicrine cells and cholinergic neurons mirror symmetric ON and OFF amicrine cells of rabbit retina
    • Famiglietti Jr E.V. Starburst amicrine cells and cholinergic neurons mirror symmetric ON and OFF amicrine cells of rabbit retina. Brain Res. 261:1983;138-144.
    • (1983) Brain Res. , vol.261 , pp. 138-144
    • Famiglietti E.V., Jr.1
  • 13
    • 0000134682 scopus 로고    scopus 로고
    • Cholinesterase inhibitors do more than inhibit cholinesterase
    • R. Becker, & E. Giacobini. Boston: Birkhuser
    • Giacobini E. Cholinesterase inhibitors do more than inhibit cholinesterase. Becker R., Giacobini E. Alzheimer's Disease: From Molecular Biology to Therapy. 1997;187-204 Birkhuser, Boston.
    • (1997) Alzheimer's Disease: From Molecular Biology to Therapy , pp. 187-204
    • Giacobini, E.1
  • 15
    • 0027092277 scopus 로고
    • Ambenonium is a rapidly reversible non-covalent inhibitor of acetylcholinesterase, with one of the highest known affinities
    • Hodge A.S., Humphrey D.R., Rosenberry T.L. Ambenonium is a rapidly reversible non-covalent inhibitor of acetylcholinesterase, with one of the highest known affinities. Mol. Pharmacol. 41:1992;937-942.
    • (1992) Mol. Pharmacol. , vol.41 , pp. 937-942
    • Hodge, A.S.1    Humphrey, D.R.2    Rosenberry, T.L.3
  • 16
    • 0023376851 scopus 로고
    • Acetylcholine as a neurotransmitter in the vertebrate retina
    • Hutchins J.B. Acetylcholine as a neurotransmitter in the vertebrate retina. Exp. Eye Res. 45:1987;1-38.
    • (1987) Exp. Eye Res. , vol.45 , pp. 1-38
    • Hutchins, J.B.1
  • 17
    • 0030767243 scopus 로고    scopus 로고
    • The cholinergic system in Alzheimer's disease
    • Kasa P., Rakonczay Z., Gulya K. The cholinergic system in Alzheimer's disease. Prog. Neurobiol. 52:1997;511-535.
    • (1997) Prog. Neurobiol. , vol.52 , pp. 511-535
    • Kasa, P.1    Rakonczay, Z.2    Gulya, K.3
  • 20
    • 0018573317 scopus 로고
    • Autoradiographic identification of acetylcholine in the rabbit retina
    • Masland R.H., Mills J.W. Autoradiographic identification of acetylcholine in the rabbit retina. J. Cell. Biol. 83:1979;159-178.
    • (1979) J. Cell. Biol. , vol.83 , pp. 159-178
    • Masland, R.H.1    Mills, J.W.2
  • 21
    • 0026017299 scopus 로고
    • Effect of tetrahydroaminoacridine on cognition, function and behavior in Alzheimer's disease
    • Molly D.W., Guyatt G.H., Wilson D.B., Duke R., Rees L., Singer J. Effect of tetrahydroaminoacridine on cognition, function and behavior in Alzheimer's disease. Can. Med. Assoc. J. 144:1991;29-34.
    • (1991) Can. Med. Assoc. J. , vol.144 , pp. 29-34
    • Molly, D.W.1    Guyatt, G.H.2    Wilson, D.B.3    Duke, R.4    Rees, L.5    Singer, J.6
  • 22
    • 0030751425 scopus 로고    scopus 로고
    • Nicotinic system involvement in Alzheimer's and Parkinson's diseases. Implications for therapeutics
    • Newhouse P.A., Potter A., Levin E.D. Nicotinic system involvement in Alzheimer's and Parkinson's diseases. Implications for therapeutics. Drugs Aging. 11:1997;206-208.
    • (1997) Drugs Aging , vol.11 , pp. 206-208
    • Newhouse, P.A.1    Potter, A.2    Levin, E.D.3
  • 23
    • 0023038429 scopus 로고
    • Acetylcholinesterase localization in cat retina: A comparison with choline acetyltransferase
    • Pourcho R.G., Osman K. Acetylcholinesterase localization in cat retina: a comparison with choline acetyltransferase. Exp. Eye Res. 43:1986;585-594.
    • (1986) Exp. Eye Res. , vol.43 , pp. 585-594
    • Pourcho, R.G.1    Osman, K.2
  • 24
    • 0343636004 scopus 로고
    • Laminar distribution of choline acetyltransferase and acetylcholinesterase activities in the inner plexiform layer of rat retina
    • Ross C.D., Dunning D.D., Juengel L.I., Godfrey D.A. Laminar distribution of choline acetyltransferase and acetylcholinesterase activities in the inner plexiform layer of rat retina. Exp. Eye Res. 465:1985;1091-1099.
    • (1985) Exp. Eye Res. , vol.465 , pp. 1091-1099
    • Ross, C.D.1    Dunning, D.D.2    Juengel, L.I.3    Godfrey, D.A.4
  • 25
    • 0001131495 scopus 로고
    • Behavior and analysis of rapid equilibrium and steady-state enzyme systems
    • New York, John Wiley and Sons
    • Segel, I.H., 1975. Behavior and analysis of rapid equilibrium and steady-state enzyme systems. Enzyme Kinetics, New York, John Wiley and Sons, pp. 170-176.
    • (1975) Enzyme Kinetics , pp. 170-176
    • Segel, I.H.1
  • 26
    • 0024515082 scopus 로고
    • Acetylcholinesterase: Zymogens of neuropeptide processing enzymes?
    • Small, D.H., 1989. Acetylcholinesterase: Zymogens of neuropeptide processing enzymes? Neuroscience. 291-299.
    • (1989) Neuroscience , pp. 291-299
    • Small, D.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.