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Volumn 380, Issue 1-2, 2007, Pages 151-156

Human serum cholinesterase from liver pathological samples exhibit highly elevated aryl acylamidase activity

Author keywords

Aryl acylamidase; Butyrylcholinesterase; Gamma glutamyltransferase; Glutamate oxaloacetate transferase

Indexed keywords

ARYL ACYLAMIDASE; ASPARTATE AMINOTRANSFERASE; BOVINE SERUM ALBUMIN; CHOLINESTERASE; GAMMA GLUTAMYLTRANSFERASE; MONOCLONAL ANTIBODY;

EID: 33947684265     PISSN: 00098981     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cca.2007.02.001     Document Type: Article
Times cited : (17)

References (35)
  • 1
    • 0032941771 scopus 로고    scopus 로고
    • Cholinesterases in neural development: new findings and toxicologic implications
    • Brimijoin S., and Koenigsberger C. Cholinesterases in neural development: new findings and toxicologic implications. Environ Health Perspect 107 Suppl 1 (1999) 59-64
    • (1999) Environ Health Perspect , vol.107 , Issue.SUPPL. 1 , pp. 59-64
    • Brimijoin, S.1    Koenigsberger, C.2
  • 2
    • 15244351268 scopus 로고    scopus 로고
    • Four new mutations in the BCHE gene of human butyrylcholinesterase in a Brazilian blood donor sample
    • Souza R.L., Mikami L.R., Maegawa R.O., and Chautard-Freire-Maia E.A. Four new mutations in the BCHE gene of human butyrylcholinesterase in a Brazilian blood donor sample. Mol Genet Metab 84 (2005) 349-353
    • (2005) Mol Genet Metab , vol.84 , pp. 349-353
    • Souza, R.L.1    Mikami, L.R.2    Maegawa, R.O.3    Chautard-Freire-Maia, E.A.4
  • 3
    • 0025294717 scopus 로고
    • Genetic variants of human serum cholinesterase influence metabolism of the muscle relaxant succinylcholine
    • Lockridge O. Genetic variants of human serum cholinesterase influence metabolism of the muscle relaxant succinylcholine. Pharmacol Ther 47 (1990) 35-60
    • (1990) Pharmacol Ther , vol.47 , pp. 35-60
    • Lockridge, O.1
  • 4
    • 0029163984 scopus 로고
    • Novel functions of cholinesterases in development, physiology and disease
    • Layer P.G., and Willbold E. Novel functions of cholinesterases in development, physiology and disease. Prog Histochem Cytochem 29 (1995) 1-93
    • (1995) Prog Histochem Cytochem , vol.29 , pp. 1-93
    • Layer, P.G.1    Willbold, E.2
  • 6
    • 0016420686 scopus 로고
    • Cholinesterase in embryonic development
    • Drews U. Cholinesterase in embryonic development. Prog Histochem Cytochem 7 (1975) 1-52
    • (1975) Prog Histochem Cytochem , vol.7 , pp. 1-52
    • Drews, U.1
  • 7
    • 0026316185 scopus 로고
    • A role for cholinesterases in tumorigenesis?
    • Soreq H., Lapidot-Lifson Y., and Zakut H. A role for cholinesterases in tumorigenesis?. Cancer Cells 3 (1991) 511-516
    • (1991) Cancer Cells , vol.3 , pp. 511-516
    • Soreq, H.1    Lapidot-Lifson, Y.2    Zakut, H.3
  • 8
    • 0033568704 scopus 로고    scopus 로고
    • Structural roles of acetylcholinesterase variants in biology and pathology
    • Grisaru D., Sternfeld M., Eldor A., Glick D., and Soreq H. Structural roles of acetylcholinesterase variants in biology and pathology. Eur J Biochem 264 (1999) 672-686
    • (1999) Eur J Biochem , vol.264 , pp. 672-686
    • Grisaru, D.1    Sternfeld, M.2    Eldor, A.3    Glick, D.4    Soreq, H.5
  • 9
    • 0027198071 scopus 로고
    • Cholinesterases regulate neurite growth in chick nerve cells invitro by means of a nonenzymatic mechanism
    • Layer P.G., Weikert T., and Alber R. Cholinesterases regulate neurite growth in chick nerve cells invitro by means of a nonenzymatic mechanism. Cell Tissue Res 273 (1993) 219-226
    • (1993) Cell Tissue Res , vol.273 , pp. 219-226
    • Layer, P.G.1    Weikert, T.2    Alber, R.3
  • 10
    • 0033836376 scopus 로고    scopus 로고
    • Abundant tissue butyrylcholinesterase and its possible function in the acetylcholinesterase knockout mouse
    • Li B., Stribley J.A., Ticu A., et al. Abundant tissue butyrylcholinesterase and its possible function in the acetylcholinesterase knockout mouse. J Neurochem 75 (2000) 1320-1331
    • (2000) J Neurochem , vol.75 , pp. 1320-1331
    • Li, B.1    Stribley, J.A.2    Ticu, A.3
  • 11
    • 0034119973 scopus 로고    scopus 로고
    • Postnatal developmental delay and supersensitivity to organophosphate in gene-targeted mice lacking acetylcholinesterase
    • Xie W., Stribley J.A., Chatonnet A., et al. Postnatal developmental delay and supersensitivity to organophosphate in gene-targeted mice lacking acetylcholinesterase. J Pharmacol Exp Ther 293 (2000) 896-902
    • (2000) J Pharmacol Exp Ther , vol.293 , pp. 896-902
    • Xie, W.1    Stribley, J.A.2    Chatonnet, A.3
  • 12
    • 0036070598 scopus 로고    scopus 로고
    • Wild-type and A328W mutant human butyrylcholinesterase tetramers expressed in Chinese hamster ovary cells 16-hour half-life in the circulation and protect mice from cocaine toxicity
    • Duysen E.G., Bartels C.F., and Lockridge O. Wild-type and A328W mutant human butyrylcholinesterase tetramers expressed in Chinese hamster ovary cells 16-hour half-life in the circulation and protect mice from cocaine toxicity. J Pharmacol Exp Ther 302 (2002) 751-758
    • (2002) J Pharmacol Exp Ther , vol.302 , pp. 751-758
    • Duysen, E.G.1    Bartels, C.F.2    Lockridge, O.3
  • 13
    • 0036073873 scopus 로고    scopus 로고
    • Cocaine metabolism accelerated by a re-engineered human butyrylcholinesterase
    • Sun H., Shen M.L., Pang Y.P., Lockridge O., and Brimijoin S. Cocaine metabolism accelerated by a re-engineered human butyrylcholinesterase. J Pharmacol 302 (2002) 710-716
    • (2002) J Pharmacol , vol.302 , pp. 710-716
    • Sun, H.1    Shen, M.L.2    Pang, Y.P.3    Lockridge, O.4    Brimijoin, S.5
  • 14
    • 0027435432 scopus 로고
    • Noncholinergic functions of cholinesterases
    • Balasubramanian A.S., and Bhanumathy C.D. Noncholinergic functions of cholinesterases. FASEB J 7 (1993) 1354-1358
    • (1993) FASEB J , vol.7 , pp. 1354-1358
    • Balasubramanian, A.S.1    Bhanumathy, C.D.2
  • 15
    • 0028079652 scopus 로고
    • Cholinesterases display genuine arylacylamidase activity but are totally devoid of intrinsic peptidase activities
    • Checler F., Grassi J., and Vincent J.P. Cholinesterases display genuine arylacylamidase activity but are totally devoid of intrinsic peptidase activities. J Neurochem 62 (1994) 756-763
    • (1994) J Neurochem , vol.62 , pp. 756-763
    • Checler, F.1    Grassi, J.2    Vincent, J.P.3
  • 16
    • 0032476123 scopus 로고    scopus 로고
    • Aryl acylamidase activity exhibited by butyrylcholinesterase is higher in chick than in horse, but much lower than in fetal calf serum
    • Weitnauer E., Robitzki A., and Layer P.G. Aryl acylamidase activity exhibited by butyrylcholinesterase is higher in chick than in horse, but much lower than in fetal calf serum. Neurosci Lett 254 (1998) 153-156
    • (1998) Neurosci Lett , vol.254 , pp. 153-156
    • Weitnauer, E.1    Robitzki, A.2    Layer, P.G.3
  • 17
    • 16544387273 scopus 로고    scopus 로고
    • Aryl acylamidase activity on acetylcholinesterase is high during early chicken brain development
    • Boopathy R., and Layer P.G. Aryl acylamidase activity on acetylcholinesterase is high during early chicken brain development. Protein J 23 (2004) 325-333
    • (2004) Protein J , vol.23 , pp. 325-333
    • Boopathy, R.1    Layer, P.G.2
  • 18
    • 33644811612 scopus 로고
    • A new and rapid colorimetric determination of acetylcholinesterase activity
    • Ellman G.L., Courtney K.D., Andres Jr. V., and Feather-Stone R.M. A new and rapid colorimetric determination of acetylcholinesterase activity. Biochemistry 7 (1961) 88-95
    • (1961) Biochemistry , vol.7 , pp. 88-95
    • Ellman, G.L.1    Courtney, K.D.2    Andres Jr., V.3    Feather-Stone, R.M.4
  • 19
    • 0342333428 scopus 로고
    • Nonspecific cholinesterase and acetylcholinesterase in rat tissues: molecular forms, structural and catalytic properties, and significance of the two enzyme systems
    • Marc V., Victor G., and Massoulie J. Nonspecific cholinesterase and acetylcholinesterase in rat tissues: molecular forms, structural and catalytic properties, and significance of the two enzyme systems. Proc Natl Acad Sci 75 (1978) 2588-2592
    • (1978) Proc Natl Acad Sci , vol.75 , pp. 2588-2592
    • Marc, V.1    Victor, G.2    Massoulie, J.3
  • 20
    • 0019218509 scopus 로고
    • The identity of the serotonin-sensitive aryl acylamidase with acetylcholinesterase from in human erythrocytes, and sheep basal ganglion and electric eel
    • George S.T., and Balasubramanian A.S. The identity of the serotonin-sensitive aryl acylamidase with acetylcholinesterase from in human erythrocytes, and sheep basal ganglion and electric eel. Eur J Biochem 111 (1980) 511-524
    • (1980) Eur J Biochem , vol.111 , pp. 511-524
    • George, S.T.1    Balasubramanian, A.S.2
  • 21
    • 0024453698 scopus 로고
    • CSF choline and acetylcholinesterase in early-onset vs. late-onset Alzheimer's disease patients
    • Kumar V., Giacobini E., and Markwell S. CSF choline and acetylcholinesterase in early-onset vs. late-onset Alzheimer's disease patients. Acta Anaesthesiol Scand 80 (1989) 461-466
    • (1989) Acta Anaesthesiol Scand , vol.80 , pp. 461-466
    • Kumar, V.1    Giacobini, E.2    Markwell, S.3
  • 22
    • 71849104860 scopus 로고
    • Protein measurement with folin phenol reagent
    • Lowry O.H., Rosebrough N.J., and Randall R.J. Protein measurement with folin phenol reagent. J Biol Chem 193 (1951) 265-269
    • (1951) J Biol Chem , vol.193 , pp. 265-269
    • Lowry, O.H.1    Rosebrough, N.J.2    Randall, R.J.3
  • 23
    • 0027457620 scopus 로고
    • Receiver-Operating Characteristic (ROC) plots: a fundamental evaluation tool in clinical medicine
    • Zweigand M.H., and Campbell G. Receiver-Operating Characteristic (ROC) plots: a fundamental evaluation tool in clinical medicine. Clin Chem 39 (1993) 561-577
    • (1993) Clin Chem , vol.39 , pp. 561-577
    • Zweigand, M.H.1    Campbell, G.2
  • 24
    • 0019768441 scopus 로고
    • The aryl acylamidase and their relationship to cholinesterase in human serum, erythrocyte and liver
    • George S.T., and Balasubramanian A.S. The aryl acylamidase and their relationship to cholinesterase in human serum, erythrocyte and liver. Eur J Biochem 121 (1981) 177-186
    • (1981) Eur J Biochem , vol.121 , pp. 177-186
    • George, S.T.1    Balasubramanian, A.S.2
  • 25
    • 0023907878 scopus 로고
    • Monoclonal antibodies specific for the different subunits of asymmetric acetylcholinesterase from chick muscle
    • Tsim K.W., Randall W.R., and Barnard E.A. Monoclonal antibodies specific for the different subunits of asymmetric acetylcholinesterase from chick muscle. J Neurochem 51 (1988) 95-104
    • (1988) J Neurochem , vol.51 , pp. 95-104
    • Tsim, K.W.1    Randall, W.R.2    Barnard, E.A.3
  • 26
    • 33646101461 scopus 로고    scopus 로고
    • Serum cholinesterase activity helps to distinguish between liver disease and non-liver disease aberration in liver functional tests
    • Ogunkeye O.O., and Roluga A.I. Serum cholinesterase activity helps to distinguish between liver disease and non-liver disease aberration in liver functional tests. Pathophysiology 13 (2006) 91-93
    • (2006) Pathophysiology , vol.13 , pp. 91-93
    • Ogunkeye, O.O.1    Roluga, A.I.2
  • 27
    • 0032559867 scopus 로고    scopus 로고
    • Developmental expression of acetyl-and butyrylcholinesterase in the rat: enzyme and mRNA levels in embryonic dorsal root ganglia
    • Koenigsberger C., Hammond P., and Brimijoin S. Developmental expression of acetyl-and butyrylcholinesterase in the rat: enzyme and mRNA levels in embryonic dorsal root ganglia. Brain Res 787 (1998) 248-258
    • (1998) Brain Res , vol.787 , pp. 248-258
    • Koenigsberger, C.1    Hammond, P.2    Brimijoin, S.3
  • 28
    • 0030807997 scopus 로고    scopus 로고
    • Transfection of reaggregating embryonic chicken retinal cells with an antisense-5′DNA butyryl-cholinesterase expression vector inhibits proliferation and alters morphogenesis
    • Robitzki A., Mack A., Chatonnet A., and und Layer P.G. Transfection of reaggregating embryonic chicken retinal cells with an antisense-5′DNA butyryl-cholinesterase expression vector inhibits proliferation and alters morphogenesis. J Neurochem 69 (1997) 823-833
    • (1997) J Neurochem , vol.69 , pp. 823-833
    • Robitzki, A.1    Mack, A.2    Chatonnet, A.3    und Layer, P.G.4
  • 29
    • 0033828730 scopus 로고    scopus 로고
    • Regulation of the rat oligodendroglia cell line OLN-93 by antisense transfection of butyrylcholinesterase
    • Robitzki A., Doll F., Richter-Landsberg C., and Layer P.G. Regulation of the rat oligodendroglia cell line OLN-93 by antisense transfection of butyrylcholinesterase. Glia 31 (2000) 195-205
    • (2000) Glia , vol.31 , pp. 195-205
    • Robitzki, A.1    Doll, F.2    Richter-Landsberg, C.3    Layer, P.G.4
  • 30
    • 0027337833 scopus 로고
    • Neurological cholinesterases in the normal brain and in Alzheimer's disease: relationship to plaques, tangles, and patterns of selective vulnerability
    • Wright C.I., Geula C., and Mesulam M.M. Neurological cholinesterases in the normal brain and in Alzheimer's disease: relationship to plaques, tangles, and patterns of selective vulnerability. Ann Neurol 34 (1993) 373-384
    • (1993) Ann Neurol , vol.34 , pp. 373-384
    • Wright, C.I.1    Geula, C.2    Mesulam, M.M.3
  • 31
    • 0034018129 scopus 로고    scopus 로고
    • Association of butyrylcholinesterase K variant with cholinesterase-positive neuritic plaques in the temporal cortex in late-onset Alzheimer's disease
    • Lehmann D.J., Nagy Z., Litchfield S., Borja M.C., and Smith A.D. Association of butyrylcholinesterase K variant with cholinesterase-positive neuritic plaques in the temporal cortex in late-onset Alzheimer's disease. Hum Genet 106 (2000) 447-452
    • (2000) Hum Genet , vol.106 , pp. 447-452
    • Lehmann, D.J.1    Nagy, Z.2    Litchfield, S.3    Borja, M.C.4    Smith, A.D.5
  • 32
  • 34
    • 0025490658 scopus 로고
    • Cholinesterases preceding major tracts in vertebrate neurogenesis
    • Layer P.G. Cholinesterases preceding major tracts in vertebrate neurogenesis. Bioessays 12 (1990) 415-420
    • (1990) Bioessays , vol.12 , pp. 415-420
    • Layer, P.G.1
  • 35
    • 0035377458 scopus 로고    scopus 로고
    • Post-translational modification of proteins: acetylcholinesterase as a model system
    • Nalivaeva N.N., and Turner A.J. Post-translational modification of proteins: acetylcholinesterase as a model system. Proteomics 1 (2001) 735-747
    • (2001) Proteomics , vol.1 , pp. 735-747
    • Nalivaeva, N.N.1    Turner, A.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.