메뉴 건너뛰기




Volumn 37, Issue 3, 2004, Pages 330-338

Modification of substrate inhibition of synaptosomal acetylcholinesterase by cardiotoxins

Author keywords

Acetylcholinesterase; Cardiotoxins; Peripheral site; Substrate inhibition; Synaptosome

Indexed keywords

ACETYLCHOLINESTERASE; ARGININE; CARDIOTOXIN; FASCICULIN;

EID: 3142670394     PISSN: 12258687     EISSN: None     Source Type: Journal    
DOI: 10.5483/bmbrep.2004.37.3.330     Document Type: Article
Times cited : (6)

References (37)
  • 3
    • 0027978350 scopus 로고
    • Cardiotoxin II from Taiwan cobra venom, Naja naja atra. Structure in solution and comparison among homologous cardiotoxins
    • Bhaskaran, R., Huang, C. C., Tsai, Y. C., Jayaraman, G., Chang, D. K. and Yu, C. (1994a) Cardiotoxin II from Taiwan cobra venom, Naja naja atra. Structure in solution and comparison among homologous cardiotoxins. J. Biol. Chem. 269, 23500-23508.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23500-23508
    • Bhaskaran, R.1    Huang, C.C.2    Tsai, Y.C.3    Jayaraman, G.4    Chang, D.K.5    Yu, C.6
  • 4
    • 0028271479 scopus 로고
    • Cardiotoxin III from Taiwan Cobra (Naja naja atra) Determination of Structure in Solution and Comparison with Short Neurotoxins
    • Bhaskaran, R., Huang, C. C., Chang, K. D. and Yu, C. (1994b) Cardiotoxin III from Taiwan Cobra (Naja naja atra) Determination of Structure in Solution and Comparison with Short Neurotoxins. J. Mol. Biol. 235, 1291-1301.
    • (1994) J. Mol. Biol. , vol.235 , pp. 1291-1301
    • Bhaskaran, R.1    Huang, C.C.2    Chang, K.D.3    Yu, C.4
  • 5
    • 0028818897 scopus 로고
    • Acetylcholinesterase inhibition by fasciculin: Crystal structure of the complex
    • Bourne, Y., Taylor, P. and Marchot, P. (1995) Acetylcholinesterase inhibition by fasciculin: crystal structure of the complex. Cell 83, 503-512.
    • (1995) Cell , vol.83 , pp. 503-512
    • Bourne, Y.1    Taylor, P.2    Marchot, P.3
  • 6
    • 0028948305 scopus 로고
    • Role of arginine residues for the activity of fasciculin
    • Cervenansky, C., Engstrom, A. and Karlsson, E. (1995) Role of arginine residues for the activity of fasciculin. Eur. J. Biochem. 229, 270-275.
    • (1995) Eur. J. Biochem. , vol.229 , pp. 270-275
    • Cervenansky, C.1    Engstrom, A.2    Karlsson, E.3
  • 7
    • 0031447137 scopus 로고    scopus 로고
    • A novel neurotoxin, cobrotoxin b, from Naja naja atra (Taiwan cobra) venom: Purification, characterization, and gene organization
    • Chang, L. S., Chou, Y. C., Lin, S. R., Wu, B. N., Lin, J., Hong, E., Sun, Y. J. and Hsiao, C. D. (1997) A novel neurotoxin, cobrotoxin b, from Naja naja atra (Taiwan cobra) venom: purification, characterization, and gene organization. J. Biochem. (Tokyo). 122, 1252-1259.
    • (1997) J. Biochem. (Tokyo) , vol.122 , pp. 1252-1259
    • Chang, L.S.1    Chou, Y.C.2    Lin, S.R.3    Wu, B.N.4    Lin, J.5    Hong, E.6    Sun, Y.J.7    Hsiao, C.D.8
  • 8
    • 0034256920 scopus 로고    scopus 로고
    • The multiplicity of cardiotoxins from Naja naja atra (Taiwan cobra) venom
    • Chang, L. S., Huang, H. B. and Lin, S. R. (2002) The multiplicity of cardiotoxins from Naja naja atra (Taiwan cobra) venom. Toxicon. 38, 1065-1076.
    • (2002) Toxicon , vol.38 , pp. 1065-1076
    • Chang, L.S.1    Huang, H.B.2    Lin, S.R.3
  • 9
    • 0028797804 scopus 로고
    • Sequence comparison and computer modeling of cardiotoxins and cobrotoxin isolated from Taiwan cobra
    • Chiou, S. H., Hung, C. C., Huang, H. C., Chen, S. T., Wang, K. T. and Yang, C. C. (1995a) Sequence comparison and computer modeling of cardiotoxins and cobrotoxin isolated from Taiwan cobra. Biochem. Biophys. Res. Commun. 206, 22-32.
    • (1995) Biochem. Biophys. Res. Commun. , vol.206 , pp. 22-32
    • Chiou, S.H.1    Hung, C.C.2    Huang, H.C.3    Chen, S.T.4    Wang, K.T.5    Yang, C.C.6
  • 10
    • 0029555459 scopus 로고
    • Inhibition of protein kinase C by snake venom toxins: Comparison of enzyme inhibition, lethality and hemolysis among different cardiotoxin isoforms
    • Chiou, S. H., Chuang, M. H., Hung, C. C., Huang, H. C., Chen, S. T., Wang, K. T. and Ho, C. L. (1995b) Inhibition of protein kinase C by snake venom toxins: comparison of enzyme inhibition, lethality and hemolysis among different cardiotoxin isoforms. Biochem. Mol. Biol. Int. 35, 1103-1112.
    • (1995) Biochem. Mol. Biol. Int. , vol.35 , pp. 1103-1112
    • Chiou, S.H.1    Chuang, M.H.2    Hung, C.C.3    Huang, H.C.4    Chen, S.T.5    Wang, K.T.6    Ho, C.L.7
  • 11
    • 0035968202 scopus 로고    scopus 로고
    • Thioflavin T is a fluorescent probe of the acetylcholinesterase peripheral site that reveals conformational interactions between the peripheral and acylation sites
    • De Ferrari, G. V., Mallender, W. D., Inestrosa, N. C. and Rosenberry, T. L. (2001) Thioflavin T is a fluorescent probe of the acetylcholinesterase peripheral site that reveals conformational interactions between the peripheral and acylation sites. J. Biol. Chem. 276, 23282-23287.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23282-23287
    • De Ferrari, G.V.1    Mallender, W.D.2    Inestrosa, N.C.3    Rosenberry, T.L.4
  • 12
    • 0019791636 scopus 로고
    • A rapid method for preparing synaptosomes: Comparison, with alternative procedures
    • Dodd, P. R., Hardy, J. A., Oakley, A. E., Edwardson, J. A., Perry, E. K. and Delaunoy, J. P. (1981) A rapid method for preparing synaptosomes: comparison, with alternative procedures. Brain Res. 226, 107-118.
    • (1981) Brain Res. , vol.226 , pp. 107-118
    • Dodd, P.R.1    Hardy, J.A.2    Oakley, A.E.3    Edwardson, J.A.4    Perry, E.K.5    Delaunoy, J.P.6
  • 15
    • 0028147995 scopus 로고
    • Structure of cobra cardiotoxin CTX I as derived from nuclear magnetic resonance spectroscopy and distance geometry calculations
    • Jahnke, W., Mierke, D. F., Beress, L. and Kessler, H. (1994) Structure of cobra cardiotoxin CTX I as derived from nuclear magnetic resonance spectroscopy and distance geometry calculations. J. Mol. Biol. 240, 445-458.
    • (1994) J. Mol. Biol. , vol.240 , pp. 445-458
    • Jahnke, W.1    Mierke, D.F.2    Beress, L.3    Kessler, H.4
  • 16
    • 0030784592 scopus 로고    scopus 로고
    • Comparison of the hemolytic activity and solution structures of two snake venom cardiotoxin analogues which only differ in their N-terminal amino acid
    • Jang, J. Y., Krishnaswamy, T., Kumar, S., Jayaraman, G., Yang, P. W. and Yu, C. (1997) Comparison of the hemolytic activity and solution structures of two snake venom cardiotoxin analogues which only differ in their N-terminal amino acid. Biochemistry 36, 14635-14641.
    • (1997) Biochemistry , vol.36 , pp. 14635-14641
    • Jang, J.Y.1    Krishnaswamy, T.2    Kumar, S.3    Jayaraman, G.4    Yang, P.W.5    Yu, C.6
  • 17
    • 0034092709 scopus 로고    scopus 로고
    • Elucidation of the Solution Structure of Cardiotoxin Analogue V from the Taiwan Cobra (Naja naja atra) Venom
    • Jayaraman, G., Kumar, T. K. S., Tsai, C. C., Chou, S. H., Ho, C. L. and Yu, C. (2000) Elucidation of the Solution Structure of Cardiotoxin Analogue V from the Taiwan Cobra (Naja naja atra) Venom. Protein Sci. 9, 637-646.
    • (2000) Protein Sci. , vol.9 , pp. 637-646
    • Jayaraman, G.1    Kumar, T.K.S.2    Tsai, C.C.3    Chou, S.H.4    Ho, C.L.5    Yu, C.6
  • 18
    • 0038219567 scopus 로고    scopus 로고
    • Unmasking tandem site interaction in human acetylcholinesterase. Substrate activation with a cationic acetanilide substrate
    • Johnson, J. L., Cusack, B., Davies, M. P., Fauq, A. and Rosenberry, T. L. (2003) Unmasking tandem site interaction in human acetylcholinesterase. Substrate activation with a cationic acetanilide substrate. Biochemistry 42, 5438-5452.
    • (2003) Biochemistry , vol.42 , pp. 5438-5452
    • Johnson, J.L.1    Cusack, B.2    Davies, M.P.3    Fauq, A.4    Rosenberry, T.L.5
  • 20
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J. and Doolittle, R. F. (1982) A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 22
    • 0017342055 scopus 로고
    • Mechanism of anticholinesterase activities of cardiotoxin, protamine and polylysine
    • Lin, S. Y., Liao, C. and Lee, C. Y. (1977) Mechanism of anticholinesterase activities of cardiotoxin, protamine and polylysine. Biochem. J. 161, 229-232.
    • (1977) Biochem. J. , vol.161 , pp. 229-232
    • Lin, S.Y.1    Liao, C.2    Lee, C.Y.3
  • 23
    • 0033605661 scopus 로고    scopus 로고
    • Organophosphorylation of acetylcholinesterase in the Presence of Peripheral Site Ligands: Distinct effects of propodium and fasciculin
    • Mallender, W. D., Szegletes, T. and Rosenberry, T. L. (1999) Organophosphorylation of acetylcholinesterase in the Presence of Peripheral Site Ligands: distinct effects of propodium and fasciculin. J. Biol. Chem. 274, 8491-8499.
    • (1999) J. Biol. Chem. , vol.274 , pp. 8491-8499
    • Mallender, W.D.1    Szegletes, T.2    Rosenberry, T.L.3
  • 24
    • 0035283141 scopus 로고    scopus 로고
    • Prediction of protein surface accessibility with information theory
    • Naderi-Manesh, H., Sadeghi, M., Arab, S. and Moosavi Movahedi, A. A. (2001) Prediction of protein surface accessibility with information theory. Proteins 42, 452-459.
    • (2001) Proteins , vol.42 , pp. 452-459
    • Naderi-Manesh, H.1    Sadeghi, M.2    Arab, S.3    Moosavi Movahedi, A.A.4
  • 25
    • 0028955778 scopus 로고
    • Contribution of aromatic moieties of tyrosine 133 and of the anionic subsite tryptophan 86 to catalytic efficiency and allosteric modulation of acetylcholinesterase
    • Ordentlich, A., Barak, D., Kronman, C., Ariel, N., Segall, Y., Velan, B. and Shafferman, A. (1995) Contribution of aromatic moieties of tyrosine 133 and of the anionic subsite tryptophan 86 to catalytic efficiency and allosteric modulation of acetylcholinesterase. J. Biol. Chem. 270, 2080-2091.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2080-2091
    • Ordentlich, A.1    Barak, D.2    Kronman, C.3    Ariel, N.4    Segall, Y.5    Velan, B.6    Shafferman, A.7
  • 26
    • 0026031111 scopus 로고
    • Role of the peripheral anionic site on acetylcholinesterase: Inhibition by substrates and coumarin derivatives
    • Radic, Z., Reiner, E. and Taylor, P. (1991) Role of the peripheral anionic site on acetylcholinesterase: inhibition by substrates and coumarin derivatives. Mol. Pharmacol. 39, 98-104.
    • (1991) Mol. Pharmacol. , vol.39 , pp. 98-104
    • Radic, Z.1    Reiner, E.2    Taylor, P.3
  • 27
    • 0029133139 scopus 로고
    • Allosteric control of acetylcholinesterase catalysis by fasciculin
    • Radic, Z., Quinn, D. M., Vellom, D. C., Camp, S. and Taylor, P. (1995) Allosteric control of acetylcholinesterase catalysis by fasciculin. J. Biol. Chem. 270, 20391-20399.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20391-20399
    • Radic, Z.1    Quinn, D.M.2    Vellom, D.C.3    Camp, S.4    Taylor, P.5
  • 28
    • 0035895884 scopus 로고    scopus 로고
    • Interaction kinetics of reversible inhibitors and substrates with acetylcholinesterase and its fasciculin 2 complex
    • Radic, Z. and Taylor, P. (2001) Interaction kinetics of reversible inhibitors and substrates with acetylcholinesterase and its fasciculin 2 complex. J. Biol. Chem. 276, 4622-4633.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4622-4633
    • Radic, Z.1    Taylor, P.2
  • 29
    • 0030050490 scopus 로고    scopus 로고
    • Binding of the neurotoxin fasciculin 2 to the acetylcholinesterase peripheral site drastically reduces the association and dissociation rate constants for N-methylacridinium binding to the active site
    • Rosenberry, T. L., Rabl, C. R. and Neumann, E. (1996) Binding of the neurotoxin fasciculin 2 to the acetylcholinesterase peripheral site drastically reduces the association and dissociation rate constants for N-methylacridinium binding to the active site. Biochemistry 35, 685-690.
    • (1996) Biochemistry , vol.35 , pp. 685-690
    • Rosenberry, T.L.1    Rabl, C.R.2    Neumann, E.3
  • 30
    • 0032998176 scopus 로고    scopus 로고
    • A steric blockade model for inhibition of acetylcholinesterase by peripheral site ligands and substrate
    • Rosenberry, T. L., Mallender, W. D., Thomas, P. J. and Szegletes, T. (1999) A steric blockade model for inhibition of acetylcholinesterase by peripheral site ligands and substrate. Chem. Biol. Interact. 119, 85-89.
    • (1999) Chem. Biol. Interact. , vol.119 , pp. 85-89
    • Rosenberry, T.L.1    Mallender, W.D.2    Thomas, P.J.3    Szegletes, T.4
  • 31
    • 0028057518 scopus 로고
    • Trp279 is involved in the binding of quaternary ammonium at the peripheral site of Torpedo marmorata acetylcholinesterase
    • Schalk, I., Ehret-Sabatier, L., Bouet, F., Goeldner, M. and Hirth, C. (1994) Trp279 is involved in the binding of quaternary ammonium at the peripheral site of Torpedo marmorata acetylcholinesterase. Eur. J. Biochem. 219, 155-159.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 155-159
    • Schalk, I.1    Ehret-Sabatier, L.2    Bouet, F.3    Goeldner, M.4    Hirth, C.5
  • 32
    • 0344026149 scopus 로고    scopus 로고
    • Electron paramagnetic resonance reveals altered topography of the active center gorge of acetylcholinesterase after binding of fasciculin to the peripheral site
    • Sentjurc, M., Pecar, S., Stojan, J., Marchot, P., Radic, Z. and Grubic, Z. (1999) Electron paramagnetic resonance reveals altered topography of the active center gorge of acetylcholinesterase after binding of fasciculin to the peripheral site. Biochim. Biophys. Acta 1430, 349-358.
    • (1999) Biochim. Biophys. Acta , vol.1430 , pp. 349-358
    • Sentjurc, M.1    Pecar, S.2    Stojan, J.3    Marchot, P.4    Radic, Z.5    Grubic, Z.6
  • 33
  • 34
    • 0041731891 scopus 로고    scopus 로고
    • Nanosecond dynamics of the mouse acetylcholinesterase Cys69-Cys96 Omega loop
    • Shi, J., Tai, K., McCammon, A. J., Taylor, P. and Johnson, D.A. (2003) Nanosecond dynamics of the mouse acetylcholinesterase Cys69-Cys96 Omega loop. J. Biol Chem. 278, 30905-30911.
    • (2003) J. Biol. Chem. , vol.278 , pp. 30905-30911
    • Shi, J.1    Tai, K.2    McCammon, A.J.3    Taylor, P.4    Johnson, D.A.5
  • 35
    • 0000140355 scopus 로고    scopus 로고
    • Nonequilibrium analysis alters the mechanistic interpretation of inhibition of acetylcholinesterase by peripheral site ligands
    • Szegletes, T., Mallender, W. D. and Rosenberry, T. L. (1998) Nonequilibrium analysis alters the mechanistic interpretation of inhibition of acetylcholinesterase by peripheral site ligands. Biochemistry 37, 4206-4216.
    • (1998) Biochemistry , vol.37 , pp. 4206-4216
    • Szegletes, T.1    Mallender, W.D.2    Rosenberry, T.L.3
  • 36
    • 0033524414 scopus 로고    scopus 로고
    • Substrate binding to the peripheral site of acetylcholinesterase initiates enzymatic catalysis. Substrate inhibition arises as a secondary effect
    • Szegletes, T., Mallender, W. D., Thomas, P. J. and Rosenberry, T. L. (1999) Substrate binding to the peripheral site of acetylcholinesterase initiates enzymatic catalysis. Substrate inhibition arises as a secondary effect. Biochemistry 38, 122-133.
    • (1999) Biochemistry , vol.38 , pp. 122-133
    • Szegletes, T.1    Mallender, W.D.2    Thomas, P.J.3    Rosenberry, T.L.4
  • 37
    • 0037140753 scopus 로고    scopus 로고
    • Mechanism of acetylcholinesterase inhibition by fasciculin: A 5-ns molecular dynamics simulation
    • Tai, K., Shen, T., Henchman, R. H., Bourne, Y. Marchot, P. and McCammon, J. A. (2002) Mechanism of acetylcholinesterase inhibition by fasciculin: a 5-ns molecular dynamics simulation. J. Am. Chem. Soc. 29, 6153-6161.
    • (2002) J. Am. Chem. Soc. , vol.29 , pp. 6153-6161
    • Tai, K.1    Shen, T.2    Henchman, R.H.3    Bourne, Y.4    Marchot, P.5    McCammon, J.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.