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Volumn 91, Issue 11-12, 2009, Pages 1450-1456

High aryl acylamidase activity associated with cobra venom acetylcholinesterase: Biological significance

Author keywords

Acetylcholinesterase; Cobra venom; Serotonin

Indexed keywords

ACETYLCHOLINESTERASE; ARYL ACYLAMIDASE; CHOLINERGIC RECEPTOR BLOCKING AGENT; MONOMER; SEROTONIN ANTAGONIST; SNAKE VENOM;

EID: 72649104036     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2009.08.004     Document Type: Article
Times cited : (5)

References (52)
  • 1
    • 0033583819 scopus 로고    scopus 로고
    • The adhesion function on acetylcholinesterase is located at peripheral anionic site
    • Glynis J., and Samuel S.W. The adhesion function on acetylcholinesterase is located at peripheral anionic site. Biochem. Biophys. Res. Commun. 258 (1999) 758-762
    • (1999) Biochem. Biophys. Res. Commun. , vol.258 , pp. 758-762
    • Glynis, J.1    Samuel, S.W.2
  • 2
    • 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 1 (1999) 59-64
    • (1999) Environ. Health Perspect. , vol.107 , Issue.1 , pp. 59-64
    • Brimijoin, S.1    Koenigsberger, C.2
  • 3
    • 0031550623 scopus 로고    scopus 로고
    • Acetylcholinesterase promotes regeneration of neuritis in cultured adult neurons of Aplysia
    • Srivatsan M., and Peretz B. Acetylcholinesterase promotes regeneration of neuritis in cultured adult neurons of Aplysia. Neuroscience 77 (1997) 921-931
    • (1997) Neuroscience , vol.77 , pp. 921-931
    • Srivatsan, M.1    Peretz, B.2
  • 4
    • 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
  • 5
    • 0024352019 scopus 로고
    • Comparison of butyrylcholinesterase and acetylcholinesterase
    • Chatonnet A., and Lockridge O. Comparison of butyrylcholinesterase and acetylcholinesterase. Biochem. J. 260 (1989) 625-634
    • (1989) Biochem. J. , vol.260 , pp. 625-634
    • Chatonnet, A.1    Lockridge, O.2
  • 6
    • 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 3 (1995) 1-94
    • (1995) Prog. Histochem. Cytochem. , vol.29 , Issue.3 , pp. 1-94
    • Layer, P.G.1    Willbold, E.2
  • 8
    • 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
  • 10
    • 0013989108 scopus 로고
    • Enzymes of snake venoms as tools in biochemical research
    • Zeller E.A. Enzymes of snake venoms as tools in biochemical research. Mem. Inst. Butantan 33 (1966) 349-357
    • (1966) Mem. Inst. Butantan , vol.33 , pp. 349-357
    • Zeller, E.A.1
  • 11
    • 0015912230 scopus 로고
    • The acetylcholinesterase of Bungarus fasciatus venom
    • Kumar V., and Elliott W.B. The acetylcholinesterase of Bungarus fasciatus venom. Eur. J. Biochem. 34 (1973) 586-592
    • (1973) Eur. J. Biochem. , vol.34 , pp. 586-592
    • Kumar, V.1    Elliott, W.B.2
  • 15
    • 0020410149 scopus 로고
    • Cobra venom acetylcholinesterase: nature of charge isoforms
    • Raba R., and Aaviskaar A. Cobra venom acetylcholinesterase: nature of charge isoforms. Eur. J. Biochem. 127 (1982) 507-512
    • (1982) Eur. J. Biochem. , vol.127 , pp. 507-512
    • Raba, R.1    Aaviskaar, A.2
  • 16
    • 0025295164 scopus 로고
    • The active site and partial sequence of cobra venom acetylcholinesterase
    • Weise C., Kreienkamp H.J., Raba R., Aaviskaar A., and Hucho F. The active site and partial sequence of cobra venom acetylcholinesterase. J. Prot. Chem. 9 (1990) 53-57
    • (1990) J. Prot. Chem. , vol.9 , pp. 53-57
    • Weise, C.1    Kreienkamp, H.J.2    Raba, R.3    Aaviskaar, A.4    Hucho, F.5
  • 17
    • 0025871564 scopus 로고
    • Investigation of ligand-binding sites of the acetylcholine receptor using photoactivatable derivatives of Neurotoxin II from Naja naja oxiana
    • Kreienkamp H.J., Weise C., Raba R., Aaviksaar A., and Hucho F. Investigation of ligand-binding sites of the acetylcholine receptor using photoactivatable derivatives of Neurotoxin II from Naja naja oxiana. Biochemistry 88 (1991) 6117-6121
    • (1991) Biochemistry , vol.88 , pp. 6117-6121
    • Kreienkamp, H.J.1    Weise, C.2    Raba, R.3    Aaviksaar, A.4    Hucho, F.5
  • 18
    • 0017149229 scopus 로고
    • Serotonin-sensitive aryl acylamidase activity of acetylcholinesterases
    • Fujimoto D. Serotonin-sensitive aryl acylamidase activity of acetylcholinesterases. FEBS Lett. 71 (1976) 121-123
    • (1976) FEBS Lett. , vol.71 , pp. 121-123
    • Fujimoto, D.1
  • 19
    • 0018749692 scopus 로고
    • The association of the serotonin-sensitive aryl acylamidase with acetylcholinesterase in the monkey brain
    • Oommen A., and Balasubramanian A.S. The association of the serotonin-sensitive aryl acylamidase with acetylcholinesterase in the monkey brain. Eur. J. Biochem. 94 (1979) 135-143
    • (1979) Eur. J. Biochem. , vol.94 , pp. 135-143
    • Oommen, A.1    Balasubramanian, A.S.2
  • 20
    • 0019949987 scopus 로고
    • Serotonin-sensitive aryl acylamidase activity of platelet acetylcholinesterase
    • Majumdar R., George S.T., and Balasubramanian A.S. Serotonin-sensitive aryl acylamidase activity of platelet acetylcholinesterase. Biochem. Pharmacol. 31 (1982) 2319-2325
    • (1982) Biochem. Pharmacol. , vol.31 , pp. 2319-2325
    • Majumdar, R.1    George, S.T.2    Balasubramanian, A.S.3
  • 21
    • 0020595327 scopus 로고
    • Carboxylesterases in rat and human sera and their relationship to serum aryl acylamidases and cholinesterases
    • Tsujita T., and Okuda H. Carboxylesterases in rat and human sera and their relationship to serum aryl acylamidases and cholinesterases. Eur. J. Biochem. 133 (1983) 215-220
    • (1983) Eur. J. Biochem. , vol.133 , pp. 215-220
    • Tsujita, T.1    Okuda, H.2
  • 22
    • 0024371283 scopus 로고
    • Human cerebrospinal fluid acetylcholinesterase and butyrylcholinesterase. Evidence for identity between the serum and cerebrospinal fluid butyrylcholinesterase
    • Rao R.V., Gnanamuthu C., and Balasubramanian A.S. Human cerebrospinal fluid acetylcholinesterase and butyrylcholinesterase. Evidence for identity between the serum and cerebrospinal fluid butyrylcholinesterase. Clin. Chim. Acta 183 (1989) 135-146
    • (1989) Clin. Chim. Acta , vol.183 , pp. 135-146
    • Rao, R.V.1    Gnanamuthu, C.2    Balasubramanian, A.S.3
  • 23
    • 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
  • 24
    • 0026528244 scopus 로고
    • Cholinesterases exhibiting aryl acylamidase activity in human amniotic fluid
    • Jayanthi L.D., Balasubramanian N., and Balasubramanian A.S. Cholinesterases exhibiting aryl acylamidase activity in human amniotic fluid. Clin. Chim. Acta 205 (1992) 157-166
    • (1992) Clin. Chim. Acta , vol.205 , pp. 157-166
    • Jayanthi, L.D.1    Balasubramanian, N.2    Balasubramanian, A.S.3
  • 25
    • 0041883337 scopus 로고    scopus 로고
    • Identification of serotonin sensitive aryl acylamidase activity with cobra venom acetylcholinesterase
    • Rajesh R.V., Balasubramanian A.S., and Boopathy R. Identification of serotonin sensitive aryl acylamidase activity with cobra venom acetylcholinesterase. Indian J. Biochem. Biophys. 40 (2003) 92-97
    • (2003) Indian J. Biochem. Biophys. , vol.40 , pp. 92-97
    • Rajesh, R.V.1    Balasubramanian, A.S.2    Boopathy, R.3
  • 26
    • 62649132782 scopus 로고    scopus 로고
    • Evidence for presence of Zn+2-binding site in acetylcholinesterase
    • Rajesh R.V., Balasubramanian A.S., and Boopathy R. Evidence for presence of Zn+2-binding site in acetylcholinesterase. Biochimie 91 (2009) 526-532
    • (2009) Biochimie , vol.91 , pp. 526-532
    • Rajesh, R.V.1    Balasubramanian, A.S.2    Boopathy, R.3
  • 27
    • 0015247334 scopus 로고
    • Nitroacetanilides as chromogenic substrates for assaying de-acetylating activity: the isolation and partial purification of aryl acylamidases from erepsin and tulip
    • Hoagland R.E., and Graf G. Nitroacetanilides as chromogenic substrates for assaying de-acetylating activity: the isolation and partial purification of aryl acylamidases from erepsin and tulip. Enzymologia 41 (1971) 313-319
    • (1971) Enzymologia , vol.41 , pp. 313-319
    • Hoagland, R.E.1    Graf, G.2
  • 30
    • 0343629838 scopus 로고
    • The specificity of cobra venom cholinesterase
    • Mounter L.A. The specificity of cobra venom cholinesterase. Biochem. J. 50 (1951) 122-128
    • (1951) Biochem. J. , vol.50 , pp. 122-128
    • Mounter, L.A.1
  • 31
    • 0016541701 scopus 로고
    • Acetylcholinesterase from Bungarus fasciatus venom-I. Substrate specificity
    • Kumar V., and Elliot W.B. Acetylcholinesterase from Bungarus fasciatus venom-I. Substrate specificity. Comp. Biochem. Physiol. C 51 (1975) 249-253
    • (1975) Comp. Biochem. Physiol. C , vol.51 , pp. 249-253
    • Kumar, V.1    Elliot, W.B.2
  • 32
    • 72649097730 scopus 로고
    • Comparison between the acetylcholinesterase of helix blood and cobra venom-I. The hydrolysis of acetylcholine and its inhibition by various compounds
    • Augustinsson K.B. Comparison between the acetylcholinesterase of helix blood and cobra venom-I. The hydrolysis of acetylcholine and its inhibition by various compounds. Acta Chem. Scand. 5 (1951) 699-711
    • (1951) Acta Chem. Scand. , vol.5 , pp. 699-711
    • Augustinsson, K.B.1
  • 33
    • 72649102156 scopus 로고
    • Comparison between the acetylcho1inesterase of helix blood and cobra venom-II. The hydrolysis of certain choline and noncholine esters
    • Augustinsson K.B. Comparison between the acetylcho1inesterase of helix blood and cobra venom-II. The hydrolysis of certain choline and noncholine esters. Acta Chem. Scand. 5 (1951) 112-123
    • (1951) Acta Chem. Scand. , vol.5 , pp. 112-123
    • Augustinsson, K.B.1
  • 34
    • 0015523050 scopus 로고
    • Acetylcholinesterase:kinetic studies on the mechanism of atropine inhibition
    • Kato G., Tan E., and Yung J. Acetylcholinesterase:kinetic studies on the mechanism of atropine inhibition. J. Biol. Chem. 247 (1971) 3186-3189
    • (1971) J. Biol. Chem. , vol.247 , pp. 3186-3189
    • Kato, G.1    Tan, E.2    Yung, J.3
  • 35
    • 0013945471 scopus 로고
    • Responses of acetylcholinesterase from Torpedo marmorata to salts and curarizing drugs
    • Changeux J.P. Responses of acetylcholinesterase from Torpedo marmorata to salts and curarizing drugs. Mol. Pharmacol. 2 (1966) 369-392
    • (1966) Mol. Pharmacol. , vol.2 , pp. 369-392
    • Changeux, J.P.1
  • 37
    • 0021249729 scopus 로고
    • A comparison of eel electroplax and snake venom acetylcholinesterase
    • Agbaji A.S., Gerassimidis K., and Hider R.C. A comparison of eel electroplax and snake venom acetylcholinesterase. Comp. Biochem. Physiol. C 17 (1984) 211-216
    • (1984) Comp. Biochem. Physiol. C , vol.17 , pp. 211-216
    • Agbaji, A.S.1    Gerassimidis, K.2    Hider, R.C.3
  • 38
    • 0017333568 scopus 로고
    • Snake venom action: are enzymes involved in it?
    • Zeller E.A. Snake venom action: are enzymes involved in it?. Cell. Mol. Life Sci. 33 (1977) 143-150
    • (1977) Cell. Mol. Life Sci. , vol.33 , pp. 143-150
    • Zeller, E.A.1
  • 39
    • 0028175404 scopus 로고
    • Characterization of OhS1, an arginine/lysine amidase from the venom of king cobra
    • Zhang Y., Lee W.H., Xiong Y.L., Wang W.Y., and Zhu S.W. Characterization of OhS1, an arginine/lysine amidase from the venom of king cobra. Toxicon 32 (1994) 615-623
    • (1994) Toxicon , vol.32 , pp. 615-623
    • Zhang, Y.1    Lee, W.H.2    Xiong, Y.L.3    Wang, W.Y.4    Zhu, S.W.5
  • 41
    • 0017612986 scopus 로고
    • Serotonin containing neurons: their possible role in pain and analgesia
    • Messing R.B., and Lytle L.D. Serotonin containing neurons: their possible role in pain and analgesia. Pain 4 (1977) 1-21
    • (1977) Pain , vol.4 , pp. 1-21
    • Messing, R.B.1    Lytle, L.D.2
  • 42
    • 0029863697 scopus 로고    scopus 로고
    • Acetylcholinesterase accelerates assembly of amyloid beta-peptides into Alzheimer's fibrils: possible role of the peripheral site of the enzyme
    • Linker C., Casanueva O.I., Soto C., and Garrido J. Acetylcholinesterase accelerates assembly of amyloid beta-peptides into Alzheimer's fibrils: possible role of the peripheral site of the enzyme. Neuron 16 (1996) 881-891
    • (1996) Neuron , vol.16 , pp. 881-891
    • Linker, C.1    Casanueva, O.I.2    Soto, C.3    Garrido, J.4
  • 43
    • 0026031094 scopus 로고
    • Anomalous molecular form of acetylcholinesterase in cerebrospinal fluid in histologically diagnosed Alzheimer's disease
    • Navaratnam D.S., Priddle J.D., McDonald B., Esiri M.M., Robinson J.R., and Smith A.D. Anomalous molecular form of acetylcholinesterase in cerebrospinal fluid in histologically diagnosed Alzheimer's disease. Lancet 337 (1991) 447-449
    • (1991) Lancet , vol.337 , pp. 447-449
    • Navaratnam, D.S.1    Priddle, J.D.2    McDonald, B.3    Esiri, M.M.4    Robinson, J.R.5    Smith, A.D.6
  • 44
    • 0026674465 scopus 로고
    • Differential inhibition of acetylcholinesterase molecular forms in normal and Alzheimer disease brain
    • Ogane N., Giacobiniand E., and Struble R. Differential inhibition of acetylcholinesterase molecular forms in normal and Alzheimer disease brain. Brain Res. 589 (1992) 307-312
    • (1992) Brain Res. , vol.589 , pp. 307-312
    • Ogane, N.1    Giacobiniand, E.2    Struble, R.3
  • 45
    • 0002654491 scopus 로고
    • The second generation of cholinesterase inhibitors: pharmacological aspects
    • Becker R., and Giacobini E. (Eds), Birkhauser, Boston
    • Giacobini E. The second generation of cholinesterase inhibitors: pharmacological aspects. In: Becker R., and Giacobini E. (Eds). Cholinergic Basis for Alzheimer Therapy (1991), Birkhauser, Boston 247-262
    • (1991) Cholinergic Basis for Alzheimer Therapy , pp. 247-262
    • Giacobini, E.1
  • 46
    • 0032080309 scopus 로고    scopus 로고
    • Stable complexes involving acetylcholinesterase and amyloid-β peptide change the biochemical properties of the enzyme and increase the neurotoxicity of Alzheimer's fibrils
    • Alvarez A., Alarcon R., Opazo C., Campos E.O., Munoz F.J., Calderon F.H., Dajas F., Gentry M.K., Doctor B.P., De Mello F.G., and Inestrosa N.C. Stable complexes involving acetylcholinesterase and amyloid-β peptide change the biochemical properties of the enzyme and increase the neurotoxicity of Alzheimer's fibrils. J. Neurosci. 18 (1998) 3113-3223
    • (1998) J. Neurosci. , vol.18 , pp. 3113-3223
    • Alvarez, A.1    Alarcon, R.2    Opazo, C.3    Campos, E.O.4    Munoz, F.J.5    Calderon, F.H.6    Dajas, F.7    Gentry, M.K.8    Doctor, B.P.9    De Mello, F.G.10    Inestrosa, N.C.11
  • 47
    • 0027475810 scopus 로고
    • Protease inhibitors and indoleamines selectively inhibit cholineaterases in the histopathologic structures of Alzheimer disease
    • Wright C.I., Geula C., and Mesulam M.M. Protease inhibitors and indoleamines selectively inhibit cholineaterases in the histopathologic structures of Alzheimer disease. Proc. Natl. Acad. Sci. 90 (1993) 683-686
    • (1993) Proc. Natl. Acad. Sci. , vol.90 , pp. 683-686
    • Wright, C.I.1    Geula, C.2    Mesulam, M.M.3
  • 48
    • 0022475304 scopus 로고
    • Molecular forms of acetylcholinesterase and butyrylcholinesterase in the aged human central nervous system
    • Atack J.R., Perry E.K., Bonnam J.R., Candy J.M., and Perry R.H. Molecular forms of acetylcholinesterase and butyrylcholinesterase in the aged human central nervous system. J. Neurochem. 47 (1986) 263-277
    • (1986) J. Neurochem. , vol.47 , pp. 263-277
    • Atack, J.R.1    Perry, E.K.2    Bonnam, J.R.3    Candy, J.M.4    Perry, R.H.5
  • 49
    • 0026794041 scopus 로고
    • Changes in acetylcholinesterase and butyrylcholinesterase in Alzheimer's disease resemble embryonic development - a study of molecular forms
    • Arendt T., Bruckner M.K., Lange M., and Bigl V. Changes in acetylcholinesterase and butyrylcholinesterase in Alzheimer's disease resemble embryonic development - a study of molecular forms. Neurochem. Int. 21 (1992) 381-396
    • (1992) Neurochem. Int. , vol.21 , pp. 381-396
    • Arendt, T.1    Bruckner, M.K.2    Lange, M.3    Bigl, V.4
  • 51
    • 0034098365 scopus 로고    scopus 로고
    • Huperzine A, a potential therapeutic agent for treatment of Alzheimer's disease
    • Bai D.L., Tang X.C., and He X.C. Huperzine A, a potential therapeutic agent for treatment of Alzheimer's disease. Curr. Med. Chem. 7 (2000) 355-374
    • (2000) Curr. Med. Chem. , vol.7 , pp. 355-374
    • Bai, D.L.1    Tang, X.C.2    He, X.C.3
  • 52
    • 0035876056 scopus 로고    scopus 로고
    • Huperzine A attenuates cognitive dysfunction and neuronal degeneration caused by β-amyloid protein-(1-40) in rat
    • Wang R., Zhang H.Y., and Tang X.C. Huperzine A attenuates cognitive dysfunction and neuronal degeneration caused by β-amyloid protein-(1-40) in rat. Eur. J. Pharmacol. 421 (2001) 149-156
    • (2001) Eur. J. Pharmacol. , vol.421 , pp. 149-156
    • Wang, R.1    Zhang, H.Y.2    Tang, X.C.3


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