From Split to Sibenik: The tortuous pathway in the cholinesterase field

Chemico-Biological Interactions

Volumn 187, Issue 1-3, 2010, Pages 3-9

  Taylor, Palmer ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Acetylcholinesterase; Butyrylcholinesterase; Neuroligin; Oxime reactivation; Thyroglobulin; , Hydrolase fold proteins

Indexed keywords

ALPHA HYDROLASE; BETA HYDROLASE; CHAPERONE; CHOLINESTERASE; HYDROLASE; NEUREXIN; NEUROLIGIN; ORGANOPHOSPHATASE; PHOSPHATASE; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; CATALYSIS; ENZYME ACTIVITY; ENZYME SUBSTRATE; ENZYME SUBUNIT; GENE EXPRESSION REGULATION; GENE FUNCTION; GENE IDENTIFICATION; GENE STRUCTURE; HUMAN; HYDROLYSIS; MOLECULAR CLONING; NONHUMAN; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN SYNTHESIS; PROTEIN TRANSPORT; STRUCTURE ANALYSIS; TRANSGENE;

EID: 77955516804     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2010.05.005     Document Type: Article

References (46)

1. Proceedings of the International meeting on Cholinesterases and Cholinergic Receptors, Cholinesterases and Cholinergic Receptors 1975, E. Reiner (Ed.).
2. Ellman G.L., Courtney K.D., Andres V., Featherstone R.M. A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem. Pharmacol. 1961, 7:88-95.
3. Karnovsky M.J., Roots L. A " Direct-Coloring" thiocholine method for cholinesterases. J. Histochem. Cytochem. 1964, 12:219-221.
4. Koelle G.B., Gromadzki C.G. Comparison of the gold-thiocholine and gold-thiolacetic acid methods for the histochemical localization of acetylcholinesterase and cholinesterases. J. Histochem. Cytochem. 1966, 14(6):443-454.
5. Schumacher M., Camp S., Maulet Y., Newton M., MacPhee-Quigley K., Taylor S.S., Friedmann T., Taylor P. Primary structure of Torpedo californica acetylcholinesterase deduced from its cDNA sequence. Nature 1986, 319(6052):407-409.
6. Sussman J.L., Harel M., Frolow F., Oefner C., Goldman A., Toker L., Silman I. Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science 1991, 253(5022):872-879.
7. Taylor P. Anticholinesterase agents. The Pharmacological Basis of Therapeutics 2006, Goodman & Gilman's, (Chapter 8). 11th ed. L.L. Brunton (Ed.).
8. Ollis D.L., Cheah E., Cygler M., Dijkstra B., Frolow F., Franken S.M., Harel M., Remington S.J., Silman I., Schrag J., et al. The alpha/beta hydrolase fold. Protein Eng. 1992, 5(3):197-211.
9. Doctor B.P., Chapman T.C., Christner C.E., Deal C.D., De La Hoz D.M., Gentry M.K., Ogert R.A., Rush R.S., Smyth K.K., Wolfe A.D. Complete amino acid sequence of fetal bovine serum acetylcholinesterase and its comparison in various regions with other cholinesterases. FEBS Lett. 1990, 266(1-2):123-127.
10. Lockridge O., Bartels C.F., Vaughan T.A., Wong C.K., Norton S.E., Johnson L.L. Complete amino acid sequence of human serum cholinesterase. J. Biol. Chem. 1987, 262(2):549-557.
11. McTiernan C., Adkins S., Chatonnet A., Vaughan T.A., Bartels C.F., Kott M., Rosenberry T.L., La Du B.N., Lockridge O. Brain cDNA clone for human cholinesterase. Proc. Natl. Acad. Sci. U.S.A. 1987, 84(19):6682-6686.
12. Prody C.A., Zevin-Sonkin D., Gnatt A., Goldberg O., Soreq H. Isolation and characterization of full-length cDNA clones coding for cholinesterase from fetal human tissues. Proc. Natl. Acad. Sci. U.S.A. 1987, 84(11):3555-3559.
13. Rachinsky T.L., Camp S., Li Y., Ekstrom T.J., Newton M., Taylor P. Molecular cloning of mouse acetylcholinesterase: tissue distribution of alternatively spliced mRNA species. Neuron 1990, 5(3):317-327.
14. Bourne Y., Taylor P., Radic Z., Marchot P. Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site. EMBO J. 2003, 22(1):1-12.
15. Li Y., Camp S., Rachinsky T.L., Getman D., Taylor P. Gene structure of mammalian acetylcholinesterase. Alternative exons dictate tissue-specific expression. J. Biol. Chem. 1991, 266(34):23083-23090.
16. Getman D.K., Eubanks J.H., Camp S., Evans G.A., Taylor P. The human gene encoding acetylcholinesterase is located on the long arm of chromosome 7. Am. J. Hum. Genet. 1992, 51(1):170-177.
17. Dvir H., Harel M., Bon S., Liu W.Q., Vidal M., Garbay C., Sussman J.L., Massoulie J., Silman I. The synaptic acetylcholinesterase tetramer assembles around a polyproline II helix. EMBO J. 2004, 23(22):4394-4405.
18. Perrier A.L., Massoulie J., Krejci E. PRiMA: the membrane anchor of acetylcholinesterase in the brain. Neuron 2002, 33(2):275-285.
19. Krejci E., Coussen F., Duval N., Chatel J.M., Legay C., Puype M., Vandekerckhove J., Cartaud J., Bon S., Massoulie J. Primary structure of a collagenic tail peptide of Torpedo acetylcholinesterase: co-expression with catalytic subunit induces the production of collagen-tailed forms in transfected cells. EMBO J. 1991, 10(5):1285-1293.
20. Xie W., Stribley J.A., Chatonnet A., Wilder P.J., Rizzino A., McComb R.D., Taylor P., Hinrichs S.H., Lockridge O. Postnatal developmental delay and supersensitivity to organophosphate in gene-targeted mice lacking acetylcholinesterase. J. Pharmacol. Exp. Ther. 2000, 293(3):896-902.
21. Camp S., De Jaco A., Zhang L., Marquez M., De la Torre B., Taylor P. Acetylcholinesterase expression in muscle is specifically controlled by a promoter-selective enhancesome in the first intron. J. Neurosci. 2008, 28(10):2459-2470.
22. Camp S., Zhang L., Marquez M., de la Torre B., Long J.M., Bucht G., Taylor P. Acetylcholinesterase (AChE) gene modification in transgenic animals: functional consequences of selected exon and regulatory region deletion. Chem. Biol. Interact. 2005, 157-158:79-86.
23. Feng G., Krejci E., Molgo J., Cunningham J.M., Massoulie J., Sanes J.R. Genetic analysis of collagen Q: roles in acetylcholinesterase and butyrylcholinesterase assembly and in synaptic structure and function. J. Cell Biol. 1999, 144(6):1349-1360.
24. Dobbertin A., Hrabovska A., Dembele K., Camp S., Taylor P., Krejci E., Bernard V. Targeting of acetylcholinesterase in neurons in vivo: a dual processing function for the proline-rich membrane anchor subunit and the attachment domain on the catalytic subunit. J. Neurosci. 2009, 29(14):4519-4530.
25. Adler M., Manley H.A., Purcell A.L., Deshpande S.S., Hamilton T.A., Kan R.K., Oyler G., Lockridge O., Duysen E.G., Sheridan R.E. Reduced acetylcholine receptor density, morphological remodeling, and butyrylcholinesterase activity can sustain muscle function in acetylcholinesterase knockout mice. Muscle Nerve 2004, 30(3):317-327.
26. Massoulie J. The origin of the molecular diversity and functional anchoring of cholinesterases. Neurosignals 2002, 11(3):130-143.
27. Cheng Y., Suen J.K., Zhang D., Bond S.D., Zhang Y., Song Y., Baker N.A., Bajaj C.L., Holst M.J., McCammon J.A. Finite element analysis of the time-dependent Smoluchowski equation for acetylcholinesterase reaction rate calculations. Biophys. J. 2007, 92(10):3397-3406.
28. Wilson I.B. Acetylcholinesterase. XIII. Reactivation of alkyl phosphate-inhibited enzyme. J. Biol. Chem. 1952, 199(1):113-120.
29. Saxena A., Maxwell D.M., Quinn D.M., Radic Z., Taylor P., Doctor B.P. Mutant acetylcholinesterases as potential detoxification agents for organophosphate poisoning. Biochem. Pharmacol. 1997, 54(2):269-274.
30. Taylor P., Kovarik Z., Reiner E., Radic Z. Acetylcholinesterase: converting a vulnerable target to a template for antidotes and detection of inhibitor exposure. Toxicology 2007, 233(1-3):70-78.
31. Hotelier T., Renault L., Cousin X., Negre V., Marchot P., Chatonnet A. ESTHER, the database of the alpha/beta-hydrolase fold superfamily of proteins. Nucleic Acids Res. 2004, 32(Database issue):D145-D147.
32. McCutchen B.F., Uematsu T., Szekacs A., Huang T.L., Shiotsuki T., Lucas A., Hammock B.D. Development of surrogate substrates for juvenile hormone esterase. Arch. Biochem. Biophys. 1993, 307(2):231-241.
33. Ichtchenko K., Hata Y., Nguyen T., Ullrich B., Missler M., Moomaw C., Sudhof T.C. Neuroligin 1: a splice site-specific ligand for beta-neurexins. Cell 1995, 81(3):435-443.
34. Sudhof T.C. Neuroligins and neurexins link synaptic function to cognitive disease. Nature 2008, 455(7215):903-911.
35. Comoletti D., Grishaev A., Whitten A.E., Tsigelny I., Taylor P., Trewhella J. Synaptic arrangement of the neuroligin/beta-neurexin complex revealed by X-ray and neutron scattering. Structure 2007, 15(6):693-705.
36. Cline H. Synaptogenesis: a balancing act between excitation and inhibition. Curr. Biol. 2005, 15(6):R203-R205.
37. Craig A.M., Kang Y. Neurexin-neuroligin signaling in synapse development. Curr. Opin. Neurobiol. 2007, 17(1):43-52.
38. Comoletti D., Flynn R.E., Boucard A.A., Demeler B., Schirf V., Shi J., Jennings L.L., Newlin H.R., Sudhof T.C., Taylor P. Gene selection, alternative splicing, and post-translational processing regulate neuroligin selectivity for beta-neurexins. Biochemistry 2006, 45(42):12816-12827.
39. Fabrichny I.P., Leone P., Sulzenbacher G., Comoletti D., Miller M.T., Taylor P., Bourne Y., Marchot P. Structural analysis of the synaptic protein neuroligin and its beta-neurexin complex: determinants for folding and cell adhesion. Neuron 2007, 56(6):979-991.
40. Park Y.N., Arvan P. The acetylcholinesterase homology region is essential for normal conformational maturation and secretion of thyroglobulin. J. Biol. Chem. 2004, 279(17):17085-17089.
41. Kim P.S., Lee J., Jongsamak P., Menon S., Li B., Hossain S.A., Bae J.H., Panijpan B., Arvan P. Defective protein folding and intracellular retention of thyroglobulin-R19K mutant as a cause of human congenital goiter. Mol. Endocrinol. 2008, 22(2):477-484.
42. Di Jeso B., Ulianich L., Pacifico F., Leonardi A., Vito P., Consiglio E., Formisano S., Arvan P. Folding of thyroglobulin in the calnexin/calreticulin pathway and its alteration by loss of Ca2+ from the endoplasmic reticulum. Biochem. J. 2003, 370(Pt 2):449-458.
43. Menon S., Lee J., Abplanalp W.A., Yoo S.E., Agui T., Furudate S., Kim P.S., Arvan P. Oxidoreductase interactions include a role for ERp72 engagement with mutant thyroglobulin from the rdw/rdw rat dwarf. J. Biol. Chem. 2007, 282(9):6183-6191.
44. X. Wang, J. Lee, B. Di Jeso, A.S. Treglia, D. Comoletti, N. Dubi, P. Taylor, P. Arvan, Cis and trans actions of the cholinesterase-like domain within the thyroglobulin, dimer, J. Biol. Chem. (2010), in press.
45. De Jaco A., Comoletti D., Kovarik Z., Gaietta G., Radic Z., Lockridge O., Ellisman M.H., Taylor P. A mutation linked with autism reveals a common mechanism of endoplasmic reticulum retention for the alpha, beta-hydrolase fold protein family. J. Biol. Chem. 2006, 281(14):9667-9676.
46. Vono-Toniolo J., Kopp P. Thyroglobulin gene mutations and other genetic defects associated with congenital hypothyroidism. Arq. Bras. Endocrinol. Metab. 2004, 48(1):70-82.