Mouse acetylcholinesterase

Thioesters play a paramount biochemical role in the metabolism of fatty acids and lipids. Indeed, fatty acyl-coenzyme A thioesters are pivotal in fatty acid anabolism and catabolism, in protein acylation, and in the synthesis of triacylglycerols, phospholipids and cholesterol esters [145], It is in these reactions that the peculiar reactivity of thioesters is of such significance. Many hydrolases, and mainly mitochondrial thiolester hydrolases (EC 3.1.2), are able to cleave thioesters. In addition, cholinesterases and carboxylesterases show some activity, but this is not a constant property of these enzymes since, for example, carboxylesterases from human monocytes were found to be inactive toward some endogenous thioesters [35] [146], In contrast, allococaine benzoyl thioester was found to be a good substrate of pig liver esterase, human and mouse butyrylcholinesterase, and mouse acetylcholinesterase [147],... 

Rachinsky, T. L, Camp, S., Li, Y., Ek-strom, J., Newton, M., Taylor, P. Molecular Cloning of Mouse Acetylcholinesterase Tissue Distribution of Alternatively Spliced mRNA Species. Neuron 1990, 5, 317-327. 

Paraoanu, L.E., Layer, P.G. (2004). Mouse acetylcholinesterase interacts in yeast with the extracellular matrix component laminin-1 beta. FEBS Lett. 576 161. ... 

Bernard, P., Kireev, D.B., Chretien, J.R., Fortier, P.-L. and Coppet, L. (1999) Automated docking of 82 N-benzylpiperidine derivatives to mouse acetylcholinesterase and comparative molecular field analysis with natural alignment. /. Comput. Aid. Mol. Des., 13, 355-371. 

Tabun-inhibited enzyme (an O-ethyl N,N-dimethylamidophosphoro derivative) is slow to reactivate and Heilbronn (1963) found no detectable spontaneous reactivation with human acetylcholinesterase. The reasons for this are becoming more clear. Tabun binding of mouse acetylcholinesterase causes conformational changes in the enzyme that may stabilize the enzyme-inhibitor complex even without ageing of the complex (Ekstrom et al., 2006). 

Bourne Y, Taylor P, Bougis PE et al. (1999). Crystal structure of mouse acetylcholinesterase. A peripheral site-occluding loop in a tetrameric assembly. J Biol Chem, 274, 2963-2970. 

Figure 6.3 Crystal structure of the mouse acetylcholinesterase-2 gallamine homodimer complex with 30% homology of 532 residues from the C-terminal cholinesterase part of human thyroglobulin (Tg). The three-dimensional structure of mouse acetylcholinesterase homodimer complex homological to part III of human Tg in Figure 6.1 was experimentally determined at a resolution of 2.20A using X-ray diffraction (Bourne et al., 2003 ExPASy access number P21836). A model of the molecule was constructed using CAChe software (Fujitsu Ltd, Japan) according to the XYZ coordinates from Protein Data Bank file (code 1 N5M.pdb).

D. Zhang, J. Suen, Y. Zhang, Z. Radic, R Taylor, M. Holst, C. Baja], N. A. Baker, and J. A. McCammon. Tetrameric mouse acetylcholinesterase Continuum diffusion rate calculations by solving the steady-state Smoluchowski equation using finite element methods. Biophys. J., 88(33 1659-1665,2005. 

Figure 8 Thermodynamic cycle illustrating the numerical procedure that calculates the rigid-body electrostatic contribution to the dissociation energy of a complex between mouse acetylcholinesterase (large molecule) and fasciculin-2 (small molecule) (complex PDB ID IMAH ). The steps are (1) complex dissociation in a homogeneous dielectric, (2) transfer of isolated components from a homogeneous dielectric into solution with an inhomogeneous dielectric, (3) complex dissociation in an inhomogeneous dielectric, and (4) transfer of complex from a homogeneous dielectric into solution with an inhomogeneous dielectric.

Carson K.A. and Burd G.D. (1980). Localization of acetylcholinesterase in the main and accessory bulbs of the mouse by light and electron microscopic histochemistry. J Comp Neurol 191, 353-371. 

Bajgar, J., Jakl, A., Hrdina, V. 1972. The Influence of obldoxlme on acetylcholinesterase activity In different parts of the mouse brain following lsopropylmethylphosphonofluorldate Intoxication. Europ. J. Pharmacol. 19 199-202. 

Anatoxin-a(s) was first detected by the mouse bioassay. However, the technique most commonly used for its detection is HPLC, coupled to MS detection. The irreversible inhibitory power of this toxin towards acetylcholinesterase has been described [60] and the corresponding colorimetric inhibition assay has also been developed [61-63]. To date, no antibodies towards anatoxin-a(s) have been produced. 

Farchi, N., Soreq, H., Hochner, B. (2003). Chronic acetylcholinesterase overexpression induces multilevelled aberrations in mouse neuromuscular physiology. J. Physiol. 546 165-73. 

Johnson, G., Moore, S.W. (2003). Human acetylcholinesterase binds to mouse laminin-1 and human collagen IV by an electrostatic mechanism at the peripheral anionic site. Neuro-sci. Lett. 337 37-40. 

Thiermann, H., Worek, F., Szinicz, L., Eyer, P. (2005). Effects of oximes on muscle force and acetylcholinesterase activity in isolated mouse hemidiaphragm exposed to Paraoxon. Toxicology 214 190-7. 

Da Silva, A.P., Farina, M., Franco, J.L., Dafre, A.L., Kassa, J., Kuca, K. (2008). Temporal effects of newly developed oximes (K027, K048) on malathion-induced acetylcholinesterase inhibition and lipid peroxidation in mouse prefrontal cortex. Neurotoxicology 29 184-9. 

The bispyridinium oxime HI-6, which is a powerful reactivator of imaged organophosphate-inhibited acetylcholinesterase, is eliminated by renal excretion. The allometric equations expressing the relationship between pharmacokinetic parameters describing the elimination of HI-6 and body weight of various mammalian species (mouse, rat, rabbit, Rhesus monkey, Beagle dog, sheep and man) are ... 

Catalpol. Zhang et al. [233] studied the neuroprotective effects of catalpol, an iridoid glycoside isolated from the fresh rehmannia roots, on the cholinergic system and inflammatory cytokines in the senescent mouse brain induced by D-galactose. Acetylcholinesterase (AChE) activity increased in senescent mouse brain and choline acetyltransferase (ChAT) decreased in the basal forebrain of senescent mouse. Muscarinic acetylcholine receptor Ml (mAChRl) expression declined and the levels of tumor necrosis factor (TNF-a), interleukin-ip (IL-ip), and advanced glycation end products... 

Duysen, E.G. et al.. Evidence for nonacetylcholinesterase targets of organophosphorus nerve agent supersensitivity of acetylcholinesterase knockout mouse to VX lethality, J. Pharmacol. Exp. Ther., 299, 528, 2001. 

Chen Y, Shoshami E, Constantini S, Weinstock M (1998) Rivastigmine, a brain selective acetylcholinesterase inhibitor, ameliorates cognitive and motor deficits induced by closed-head injury in the mouse. J Neurotrauma 15 231-237. 

Dong H, Csernansky CA, Martin MV, Bertchume A, VaUera D, Csernansky JG (2005) Acetylcholinesterase inhibitors amehorate behavioural deficits in the Tg2576 mouse model of Alzheimer s disease. Psychopharmacology (Berlin) 181 145-152. 

Henderson NS (1977) Acetylcholinesterase isozymes in developing mouse tissues. J. Exp. Zool, 199, 41-50. 

Carson, K.A.( 1984b) Localization of acetylcholinesterase-positive neurons projecting to the mouse main olfactory bulb. Brain Res. Bull., 12, 635-639. 

Al-Ani, A. T., Tunnicliff, G., Rick, J. T. and Kerkut, G. A. (1970) GABA production, acetylcholinesterase activity and biogenic amine levels in brain for mouse strains differing in spontaneous activity and reactivity. Life Sci., 9,21-27. 

Sadasivudu B, Murthy CRK, Rao GN, et al. 1983. Studies on acetylcholinesterase and gamma-glutamyltranspeptides in mouse brain in ammonia toxicity. J Neurosci Res 9 127-134. 

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