Interactions of oxime reactivators with diethylphosphoryl adducts of human acetylcholinesterase and its mutant derivatives

Molecular Pharmacology

Volumn 50, Issue 3, 1996, Pages 639-649

  Grosfeld, Haim ^a   Barak, Dov ^a   Ordentlich, Arie ^a   Velan, Baruch ^a   Shafferman, Avigdor ^a  

^a ISRAEL INSTITUTE FOR BIOLOGICAL RESEARCH   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

1 (4 CARBAMOYLPYRIDINIO) 1' (2 HYDROXYIMINOMETHYLPYRIDINIO)DIMETHYL ETHER; ACETYLCHOLINESTERASE; OXIME DERIVATIVE; PARAOXON; PRALIDOXIME; TRIMEDOXIME;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME KINETICS; ENZYME REACTIVATION; ENZYME SUBSTRATE COMPLEX; HUMAN; MOLECULAR INTERACTION; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION;

ACETYLCHOLINESTERASE; AMINO ACID SEQUENCE; BINDING SITES; CHOLINESTERASE INHIBITORS; CHOLINESTERASE REACTIVATORS; HUMANS; KINETICS; MUTAGENESIS, SITE-DIRECTED; ORGANOPHOSPHORUS COMPOUNDS; OXIMES; PARAOXON; PHENYLALANINE; POINT MUTATION; RECOMBINANT PROTEINS; TRIMEDOXIME; TRYPTOPHAN; TYROSINE;

EID: 0029786271     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (41)

1. Chambers, H. W. Organophosphorus compounds: an overview, in Organophosphates: Chemistry, Fate, and Metabolism (J. E. Chambers and P. E. Levi, eds.). Academic Press, San Diego, 3-17 (1992).
2. Aldridge, W. N., and E. Reiner. Enzyme Inhibitors as Substrates. North-Holland Publishing, Amsterdam (1972).
3. Gray, A. P. Design and structure-activity relationships of antidotes of organophosphorus anticholinesterase agents. Drug Metab. Rev. 15:557-589 (1984).
4. Wilson, B. W., M. J. Hooper, M. E. Hensen, and P. S. Neiberg. Reactivation of organophosphorus inhibited AChE with oximes, in Organophosphates: Chemistry, Fate, and Metabolism (J. E. Chambers and P. E. Levi, eds.). Academic Press, San Diego, 108-137 (1992).
5. Ellin, R. I. Anomalies in theories and therapy of intoxication by potent organophosphorus anticholinesterase compounds. Gen. Pharmacol. 13: 457-466 (1982).
6. Taylor, P. Anticholinesterase agents, in Goodman and Gilman's The Pharmacological Basis of Therapeutics (A. G. Gilman, T. W. Rall, A. S. Nies, and P. Taylor, eds.). Pergamon Press, Chapter 7 (1990).
7. Rousseaux, C. G., and A. K. Dua. Pharmacology of HI-6, an H-series oxime. Can. J. Physiol. Pharmacol. 67:1183-1189 (1989).
8. Eyer, P., I. Hagedorn, R. Klimmek, P. Lippstreu, M. Löffeler, H. Oldiges, U. Spöhrer, I. Steidl. L. Szinicz, and F. Worek. HLö 7 dimethanesulfonate: a potent bispyridinium-dioxime against anticholinesterases. Arch. Toxicol. 66:603-621 (1992).
9. Clement, J. G., S. Rosario, E. Bessette, and N. Erhardt. Soman and sarin inhibition of molecular forms of acetylcholinesterase in mice. Biochem. Pharmacol. 42:329-335 (1991).
10. Sussman, J. L., M. Harel, F. Frolow, C. Oefner, A. Goldman, and I. Silman. Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine binding protein. Science (Washington D. C.) 253:872-879 (1991).
11. Gibney, G., S. Camp, M. Dionne, K. MacPhee-Quigley, and P. Taylor. Mutagenesis of essential functional residues in acetylcholinesterase. Proc. Natl. Acad. Sci. USA 87:7546-7550 (1990).
12. Shafferman, A., C. Kronman, Y. Flashner, M. Leitner, H. Grosfeld, A. Ordentlich, Y. Gozes, S. Cohen, N. Ariel, D. Barak, M. Harel, I. Silman, J. L. Sussman, and B. Velan. Mutagenesis of acetylcholinesterase: identification of residues involved in catalytic activity and in polypeptide folding. J. Biol. Chem. 267:17649-17648 (1992).
13. Harel, M., J. L. Sussman, E. Krejci, S. Bon, P. Chanal, J. Massoulie, and I. Silman. Conversion of acetylcholinesterase to butyrylcholinesterase: modeling and mutagenesis. Proc. Natl. Acad. Sci. USA 89:10827-10831 (1992).
14. Shafferman, A., B. Velan, A. Ordentlich, C. Kronman, H. Grosfeld, M. Leitner, Y. Flashner, S. Cohen, D. Barak, and N. Ariel. Substrate inhibition of acetylcholinesterase: residues involved in signal transduction from the surface to the active center. EMBO J. 11:3561-3568 (1992).
15. Vellom, D. C., Z. Radic, Y. Li, N. A. Pickering, S. Camp, and P. Taylor. Amino acid residues controlling acetylcholinesterase and butyrylcholinesterase specificity. Biochemistry 32:12-17 (1993).
16. Ordentlich, A., D. Barak, C. Kronman, Y. Flashner, M. Leitner, Y. Segall, N. Ariel, S. Cohen, B. Velan, and A. Shafferman. Dissection of the human acetylcholinesterase active center, determinants of substrate specificity. J. Biol. Chem. 268:17083-17095 (1993).
17. Taylor, P., and Z. Radic. The cholinesterases: from genes to proteins. Annu. Rev. Pharmacol. Toxicol. 34:281-320 (1994).
18. Barak, D., C. Kronman, A. Ordentlich, N. Ariel, A. Bromberg, D. Marcus, A. Lazar, B. Velan, and A. Shafferman. Acetylcholinesterase peripheral anionic site degeneracy conferred by amino acid arrays sharing a common core. J. Biol. Chem. 269:6296-6305 (1994).
19. Gnatt, A., Y. Loewenstein, A. Yaron, M. Schwartz, and H. Soreq. Sitedirected mutagenesis of active site residues reveals plasticity of human butyrylcholinesterase in substrate and inhibitor interactions. J. Neurochem. 62:749-755 (1994).
20. Ordentlich, A., D. Barak, C. Kronman, N. Ariel, Y. Segall, B. Velan, and A. Shafferman. 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. 270:2082-2091 (1995).
21. Radie, Z., R. Duran, D. C. Vellom, Y. Li, C. Cervenanski, and P. Taylor. Site of fasciculin interaction with acetylcholine. J. Biol. Chem. 269:11233-11239 (1994).
22. Ordentlich, A., D. Barak, C. Kronman, N. Ariel, Y. Segall, B. Velan, and A. Shafferman. The architecture of human acetylcholinesterase active center probed by interactions with selected organophosphate inhibitors. J. Biol. Chem. 271:11953-11962 (1996).
23. Ordentlich, A., C. Kronman, D. Barak, D. Stein, N. Ariel, D. Marcus, B. Velan, and A. Shafferman. Engineering resistance to 'aging' of phosphylated human acetylcholinesterase. FEBS Lett. 334:215-220 (1993).
24. Ashani, Y., Z. Radic, I. Tsigelny, D. C. Vellom, N. A. Pickering, D. M. Quinn, B. P. Doctor, and P. Taylor. Amino acid residues controlling reactivation of organophosphonyl conjugates of acetylcholinesterase by monoand bisquaternary oximes. J. Biol. Chem. 270:6370-6380 (1995).
25. Velan, B., H. Grosfeld, C. Kronman, M. Leitner, Y. Gozes, A. Lazar, Y. Flashner, D. Markus, S. Cohen, and A. Shafferman. The effect of elimination of intersubunit disulfide bonds on the activity, assembly, and secretion of recombinant human acetylcholinesterase. J. Biol. Chem. 266: 23977-23984 (1991).
26. Kronman, C., B. Velan, Y. Gozes, M. Leitner, Y. Flashner, A. Lazar, D. Marcus, T. Sery, A. Papier, H. Grosfeld, S. Cohen, and A. Shafferman. Production and secretion of high levels of recombinant human acetylcholinesterase. Gene 121:295-304 (1992).
27. Lazar, A., S. Reuveny, C. Kronman, B. Velan, and A. Shafferman. Evaluation of anchorage-dependent cell propagation systems for production of human acetylcholinesterase by recombinant 293 cells. Cytotechnology 13: 115-123 (1993).
28. Barak, D., A. Ordentlich, A. Bromberg, C. Kronman, D. Marcus, A. Lazar, N. Ariel, B. Velan, and A. Shafferman. Allosteric modulation of acetylcholinesterase activity by peripheral ligands involves a conformational transition of the anionic subsite. Biochemistry 34:15444-15452 (1995).
29. Ellman, G. L., K. D. Courtney, V. Andres, and R. M. Featherstone. A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem. Pharmacol. 7:88-95 (1961).
30. Green, A. L., and H. J. Smith. The reactivation of cholinesterase inhibited organophosphorus compounds. Biochem. J. 68:28-31 (1958).
31. Main, A. R. Affinity and phosphorylation constants for the inhibition of esterases by organophosphates. Science (Washington D. C.) 144:992-993 (1964).
32. Harvey, B., R. P. Scott, D. J. Sellers, and P. Watts. In vitro studies on the reactivation by oximes of phosphylated acetylcholinesterase-II. Biochem. Pharmacol. 35:745-751 (1986).
33. Whiteley, C. G., and D. S. Ngwenya. Protein ligand interactions: alkylated pyridinium salts as inhibitors of acetylcholinesterase from Electrophorus electricus. Biochem. Biophys. Res. Commun. 211:1083-1090 (1995).
34. Berman, H. A., W. Becktel, and P. Taylor. Spectroscopic studies on acetylcholinesterase: influence peripheral-site occupation on active-center conformation. Biochemistry 20:4803-4810 (1981).
35. Hucho, F., J. Jarv, and C. Weise. Substrate-binding sites in acetylcholinesterase. Trends Pharmacol. Sci. 12:422-427 (1991).
36. Radic, Z., E. Reiner, and P. Taylor. Role of the peripheral binding site on acetylcholinesterase: inhibition by substrates and coumarin derivatives. Mol. Pharmacol. 39:98-104 (1991).
37. Harel, M., I. Schalk, L. Ehret-Sabatier, F. Bouet, M. Goeldner, C. Hirth, P. H. Axelsen, I. Silman, and J. L. Sussman. Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase. Proc. Natl. Acad. Sci. USA 90:9031-9035 (1993).
38. Berman, H. A., and M. M. Decker. Kinetic, equilibrium and spectroscopic studies on cation association at the active center of acetylcholinesterase: topographic distinction between trimethyl and trimethylammonium sites. Biochim. Biophys. Acta 872:125-133 (1986).
39. Gentry, M. K., and Doctor, B. P. Amino acid alignment of cholinesterases, esterases, lipases and related proteins, in Enzymes of the Cholinesterase Family (D. M. Quinn, A. S. Balasubarmanian, B. P. Doctor, and P. Taylor, eds.). Plenum Publishing, New York, 493-505 (1995).
40. 2-) to nitrogen nucleophiles from pyridino-N- phosphonates. J. Am. Chem. Soc. 106:7591-7596 (1984).
41. Massoulie, J., J. L. Sussman, B. P. Doctor, H. Soreq, B. Velan, M. Cygler, R. Rotundo, A. Shafferman, I. Silman, and P. Taylor. Recommendations for nomenclature in cholinesterases, in Multidisciplinary Approaches to Cholinesterase Functions (A. Shafferman and B. Velan, eds.). Plenum Publishing, New York, 285-288 (1992).