Acetylcholinesterase Adaptation

Gisiger, V., Belisle, M., and Gardiner, P.F., Acetylcholinesterase adaptation to voluntary wheel running is proportional to the volume of activity in fast, but not slow, rat hind limb muscles, Eur. J. NeuroscL, 6, 673, 1994. 

Y. Song, Y. Zhang, C. L. Baja], and N. A. Baker. Continuum diffusion reaction rate calculations of wild-type and mutant mouse acetylcholinesterase Adaptive finite element analysis. Biophys. J.,... 

Baldwin, J. (1971). Adaptation of enzymes to temperature acetylcholinesterases in the central nervous system of fishes. Comp. Biochem. Physiol. 40 181-187. 

Evron, T., Greenberg, D., Mor, T.S., Soreq, H. (2007). Adaptive changes in acetylcholinesterase gene expression as mediators of recovery from chemical and biological insults. Toxicology 233 97-107. 

Ben-Shaul, Y., BenMoyal-Segal, L., Ben-Ari, S., Bergman, H., Soreq, H. (2006). Adaptive acetylcholinesterase splicing patterns attenuate 1 -methyl-4-phenyl-l, 2,3,6-tetrahydropyridine-induced Parkinsonism in mice. EJNS 23 2915-22. Benmoyal-Segal, L., Vander, T., Shifman, S., Bryk, B., Ebstein, R.P., Marcus, E.L., Stessman, J., Darvasi, A., Herishanu, Y., Friedman, A., Soreq, H. (2005). Acetylcholinesterase/para-oxonase interactions increase the risk of insecticide-induced Parkinson s disease. FASEB J. 19 452. ... 

FIGURE 3.4 Mechanism of action of acetylcholinesterase inhibition (A) Structure of AChE (B) normal functioning of AChE (C) inhibition of AChE by nerve agent sarin. (Adapted from Somani et al. )... 

It appeared that cholinergic transmission performed other new functions. It can modulate various aspects of immune function, both innate and adaptive. Cholinergic transmission influences immune cell proliferation, cytokine production, differentiation of T-helper cells, and antigen presentation. These effects are mediated by cholinergic mAChR and nAQiR and other cholinergic components present in immune cells, for example, a7 nAQiR has the ability to induce anti-inflammatory activity [89]. This is probably one of the reasons why acetylcholinesterase inhibitors (AChEIs) act far broader than just to the inhibition of AChE. 

Several established protocols have been adapted for 96-well plate readers including catalase, hyaluronidase, acetylcholinesterase, protein phosphatases and membrane-bound ATPases (22-26). In several instances these have involved novel protocols that are well suited to the ELISA format. For example, a sensitive, rapid microtitre-based assay for hyaluronidase activity was described by Frost and Stem (23). The free carboxyl groups of hyaluronan are biotinylated in a one-step reaction using biotin-hydrazide. This substrate is then covalently coupled to a 96-well microtitre plate. At the completion of the enzyme reaction, residual substrate is detected with an avidin-peroxidase reaction that can be read in a standard ELISA plate reader. Because the substrate is covalently bound to the microtitre plate, artefacts such as pH-dependent displacement of the biotinylated substrate do not occur. The sensitivity permits rapid measurement of hyaluronidase activity from cultured cells and biological samples, with an interassay variation of less than 5%. 

Fig. 3. Scattergram of the correlation between the values of n (Hill coefficient) and the ratio double bond index per saturated fatty acids from membrane erythrocytes lipid. The equation of the regression line and overall correlation coefficient r with its significance are included A, (Na+, K+)-ATPase B, acetylcholinesterase C, (Mg2+)-ATPase D, (Ca2+, Mg2+)-ATPase. Diet supplements a, hydrogenated fat b, lard c, linseed oil d, olive oil e, fat-free f, corn oil and g, standard diet. (Adapted from Bloj et al., 1973a and Galo et al., 1975).

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