Acetylcholinesterase at high catalytic efficiency and substrate specificity in the optic lobe of Eledone moschata (Cephalopoda: Octopoda): Biochemical characterization and histochemical localization

Neurochemistry International

Volumn 33, Issue 2, 1998, Pages 131-141

  Talesa, Vincenzo ^a   Romani, Rita ^a   Calvitti, Mario ^a   Rosi, Gabriella ^a   Giovannini, Elvio ^a  

^a UNIVERSITY OF PERUGIA   (Italy)

Author keywords

Cholinergic synapses; Cholinesterase; Localization; Octopods; Optic lobe

Indexed keywords

ACETYLCHOLINESTERASE; CONCANAVALIN A; PHOSPHATIDYLINOSITOL; PROCAINAMIDE; SEPHAROSE; TRITON X 100;

AFFINITY CHROMATOGRAPHY; ANIMAL TISSUE; ARTICLE; BIOCHEMISTRY; CELL MEMBRANE; CEPHALOPOD; CHOLINERGIC SYNAPSE; CONTROLLED STUDY; DENSITY GRADIENT CENTRIFUGATION; ELECTRICITY; ENZYME ACTIVE SITE; ENZYME LOCALIZATION; ENZYME SPECIFICITY; ENZYME SUBSTRATE; GEL FILTRATION CHROMATOGRAPHY; HISTOCHEMISTRY; MOLECULAR SIZE; NERVOUS SYSTEM; NONHUMAN; OPTIC LOBE; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; VERTEBRATE;

ACETYLCHOLINESTERASE; ANIMALS; CATALYSIS; CENTRIFUGATION, DENSITY GRADIENT; DISULFIDES; HISTOCYTOCHEMISTRY; ISOENZYMES; KINETICS; MOLECULAR STRUCTURE; MOLECULAR WEIGHT; MOLLUSCA; OPTIC LOBE; PHOSPHOLIPASE C; SUBSTRATE SPECIFICITY;

EID: 0032142768     PISSN: 01970186     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0197-0186(98)00017-5     Document Type: Article

References (35)

1. Arpagaus, M., Richier, P., Bergé, J.-B., Toutant, J.-P., 1992. Acetylcholinesterases of the nematode Steinernema carpocapsae. Characterization of two types of amphiphilic forms differing in their mode of membrane association. Eur. J. Biochem. 207, 1101-1108.
2. Barlow, J.J., 1977. Comparative biochemistry of the central nervous system. Symp. Zool. Soc. Lond. 38, 325-346.
3. Bon, S., Toutant, J.-P., Méflah, K., Massoulié, J., 1988. Amphiphilic and nonamphiphilic forms of Torpedo cholinesterases: I. Solubility and aggregation properties. J. Neurochem. 51, 776-785.
4. Bradford, M.M., 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analyt. Biochem. 72, 248-254.
5. Ellman, G.L., Courtney, D.K., Andres, V., Featherstone, R.M., 1961. A new and rapid colorimetric determination of acetylcholinesterase activity. Biochem. Pharmacol. 7, 88-95.
6. Ferguson, M.A.J., Williams, A.F., 1988. Cell-surface anchoring of proteins via glycosyl-phosphatidylinositol structures. Ann. rev. Biochem. 57, 285-320.
7. Fournier, D., Bride, J.M., Karch, F., Bergé, J.B., 1988. Acetylcholinesterase from Drosophila melanogaster: identification of two subunits encoded by the same gene. FEBS Lett. 238, 333-337.
8. Gnagey, A.L., Forte, M., Rosenberry, T.L., 1987. Isolation and characterization of acetylcholinesterase from Drosophila. J. biol. Chem. 262, 13290-13298.
9. Hickman, C.P., 1967. Biology of the Invertebrates. C.V. Mosby, St Louis, MO, pp. 534-547.
10. Hickman, C.P., Roberts, L.S., Hickman, F.M., 1988. Integrated principles of Zoology. C.V. Mosby, St Louis, MO, pp. 284-293.
11. Karnovsky, M.J., Roots, L., 1964. A 'direct-coloring' thiocholine method for cholinesterases. J. Histochem. Cytochem. 12, 219-222.
12. Krupka, R.M., Laidler, K.J., 1961. Molecular mechanisms for hydrolytic enzyme action. I, II, III, IV. Structure of the active center and the reaction mechanism. J. Am. Chem. Soc. 83, 1445-1460.
13. 4. Nature 227, 680-685.
14. Laurent, T. C., Killander, J., 1964. A theory of gel filtration and its experimental verification. J. Chromatogr. 14, 317-330.
15. Massoulié, J., Toutant, J.-P., 1988. Vertebrate cholinesterase: structure and types of interaction. Handb. expt. Pharmac. 86, 167-224.
16. Massoulié, J., Bon, S., Krejci, E., Coussen, F., Duval, N., Chatel, J.M., Anselmet, A., Legay, C., Vallette, F. M., Grassi, J., 1991. The structure and significance of multiple cholinesterase forms. In: Massoulié, J., Bacou, F., Barnard, E.A., Chatonnet, A., Doctor, B.P. and Quinn, D. M. (Ed.). Cholinesterases: Structure, Function, Mechanism, Genetics and Cell Biology. Am. Chem. Soc., Washington, D.C., pp. 2-6.
17. Massoulié, J., Pezzementi, L., Bon, S., Krejci, E., Vallette, F. M., 1993. Molecular and cell biology of cholinesterases. Prog. Neurobiol. 41, 31-91.
18. Mazzi, V., 1977. Manuale di tecniche istologiche e istochimiche, (Piccin, ed.). Padova, Italy.
19. Messenger, J. B., 1996. Neurotransmitters of cephalopods. Invertebr. Neurosci. 2, 95-114.
20. Osterman, L.A., 1986. Methods of protein and nucleic acid research. Springer-Verlag, Heidelberg, pp. 130-139.
21. Ralston, S.J., Main, A.R., Kilpatrick, B.F., Chasson, A.L., 1983. Use of procainamide gels in the purification of human and horse serum cholinesterases. Biochem. J. 211, 243-250.
22. Rosenberry, T.L., 1975. Acetylcholinesterase. Adv. Enzymol. 43, 103-218.
23. Rosenberry, T.L., Scoggin, D.M., 1984. Structure of human erythrocyte acetylcholinesterase. Characterization of inter-subunit disulfide bonding and detergent interaction. J. biol. Chem. 259, 5643-5652.
24. Silver, A., 1974. The biology of cholinesterases. North-Holland, Amsterdam.
25. Stenersen, J., 1980. Esterases of earthworms. Part I: Characterization of the cholinesterases in Eisenia foetida (Savigny) by substrates and inhibitors. Comp. Biochem. Physiol. 66C, 37-44.
26. Talesa, V., Contenti, S., Principato, G.B., Pascolini, R., Giovannini, E., Rosi, G., 1992a. Cholinesterase from Maia verrucosa and Palinurus vulgaris: a comparative study. Comp. Biochem. Physiol. 101C, 499-503.
27. Talesa, V., Principato, G. B., Mangiabene, C., Giovannini, E., Norton, S. J., Rosi, G., 1992b. Cholinesterase in the cnidarians Velellavelella (Hydrozoa: Syphonophora) and Actinia equina (Anthozoa: Actiniaria): a comparative study. J. exp. Zool. 263, 367-373.
28. Talesa, V., Principato, G.B., Giovannini, E., Di Giovanni, M.V., Rosi, G., 1993. Dimeric forms of cholinesterase in Sipunculus nudus. Eur. J. Biochem. 215, 267-275.
29. Talesa, V., Principato, G.B., Giovannini, E., Norton, S.J., Rosi, G., 1994. Presence of a soluble tetrameric (blood) and membrane-bound dimeric forms of cholinesterase in the mollusk Murex brandaris (Gastropoda: Neogastropoda). J. exp. Zool. 270, 233-244.
30. Talesa, V., Grauso, M., Giovannini, E., Rosi, G., Toutant, J.-P., 1995a. Acetylcholinesterase in tentacles of Octopus vulgaris (Cephalopoda). Histochemical localization and characterization of a specific high salt-soluble and heparin-soluble fraction of globular forms. Neurochem. Int. 27, 201-211.
31. Talesa, V., Grauso, M., Giovannini, E., Rosi, G., Toutant, J.-P., 1995b. Solubilization, molecular forms, purification and substrate specificity of two acetylcholinesterases in the medicinal leech (Hirudo medicinalis). Biochem. J. 306, 687-692.
32. Talesa, V., Romani, R., Rosi, G., Giovannini, E., 1996. Acetylcholinesterase in Dendrobaena veneta (Oligochaeta: Opisthopora) is present with forms sensitive and insensitive to phosphatidylinositol phospholipase C. Biochemical characterization and histochemical localization in the nervous system. Eur. J. Biochem. 238, 538-548.
33. Toutant, J.-P., Arpagaus, M., Fournier, D., 1988. Native molecular forms of head acetylcholinesterase from adult Drosophila melanogaster: quaternary structure and hydrophobic character. J. Neurochem. 50, 209-218.
34. Wächtler, K., 1988. Phylogeny of the cholinergic synapse. In: Whittaker, V.P. (Ed.). The cholinergic synapse. Springer-Verlag, Berlin, Heidelberg, pp. 57-80.
35. Young, J.Z., 1971. The anatomy of the nervous system of Octopus vulgaris. Clarendon Press, Oxford, pp. 443-480.