We have performed several studies to find support for the above hypothesis. Identification of the GBB esterase activity in mammals was the first objective of the studies. Surprisingly, we have managed to reveal the existence of this enzymatic activity in the rat blood serum. An in-chain substituted derivative of GBB ester that can be detected spectrophotometrically for the HPLC purposes was synthesized and used in the study. The substance was stable in aqueous solutions, but if incubated with the rat blood serum the HPLC revealed a peak corresponding to the GBB analogue. Up to 60% of the initial 3. 10-4 M ester were hydrolysed in an hour. Acetylcholine did not compete with the reaction; it was insensitive to acetylcholine inhibitors. Moreover, purified acetylcholinesterase could not catalyze the reaction, butirylcholinesterase was also inactive. Thus, we concluded that a specific enzyme GBB-esterase is active in mammals. The study is in progress [93]. Existence of the GBB esterase cannot exclude the action of GBB esters via acetylcholine receptors, as the substance can bind them. Recent in vitro data obtained by Dambrova et al. [94] showed that GBB methyl ester is a potent agonist for m-type of acetylcholine receptors; GBB affinity to these receptors is much lower. A computer model of the molecular interactions between the GBB ethyl and methyl esters and the active centre of acetylcholine indicates that acetylcholine and GBB ethyl ester have the same binding modes [6]. This is a clear indication of a possibility for hydrolysis of GBB esters by this enzyme. Concerning the following transducers of the GBB esterase signaling pathway, nitric oxide appeared to be the probable, as it was reported that Mildronate and -butyrobetaine GBB ; composition eliminated vasoconstriction produced by nitric oxide synthase NOS ; inhibitors [81]. We hypothesized that Mildronate might act also via a nitric oxide-dependent mechanism. In a preliminary study [95] we tried to reveal Mildronate possible effects on nitric oxide NO ; concentration in rat organs. Changes in the NO content in different rat tissues brain cortex, cerebellum, liver, heart, kidneys ; were evaluated after Mildronate administration by the electron paramagnetic resonance method EPR ; . It was revealed that Mildronate 50 mg kg, i p ; triggered a slight but reproducible wave-like increase in the NO level in the brain cortex and cerebellum 30 minutes after the drug administration. Administering the NOS inhibitor N-nitro L-arginine 50 mg kg; i.p. ; , at the same time caused a pronounced decrease of the NO concentration that indicates the necessity of NOS activation to produce the Mildronate effect. This was the first indication of a putative NO-dependent mechanism of the drug action. Interestingly, the effect was pronounced in the brain, where "the not understandable" carnitine biosythesis takes place. Moreover, the time course of the effect resembled that for of Mildronate vascular effects described by Enina et al. [33]. In our later studies the NO-producing effects of Mildronate were studied in comparison with -butyrobetaine and GBB esters. We observed an induced transient increase in nitric oxide NO ; concentrations in the rat blood and myocardium, produced by Mildronate, GBB and GBB methyl ester [96]. The latter produced a similar effect to GBB and Mildronate at 100- times lower concentration. In vitro, these compounds neither modified the activities of purified neuronal and endothelial recombinant nitric oxide synthases NOSs ; , nor were they able to interact with their active sites. GBB induced vasodilatation at high concentrations only EC50 5 x 10-5 M ; , Mildronate alone displayed no vasodilating effect, however enhanced the GBB vasodilating activity. GBB methyl and ethyl esters were found to be more potent vasodilators EC50 2.5 x 10-6 M ; . Pre-treatment of aortic rings with NOS inhibitor N-nitro-L-arginine methyl ester abolished the vasodilating effects of the compounds [96]. The above results provide evidence that GBB methyl and ethyl esters are potent NO- and endothelium-dependent vasodilators. While Mildronate alone elicits no activity, it sharply enhances the activity of GBB in endothelium- and NOS-dependent responses. These data suggest that fast anti-ischemic effects of Mildronate may be in part related to the stimulation of NO formation by endothelium. As none of the studied compounds could modify the NOS activity in vitro, we think that our results suggest that some receptor-mediated mechanisms are participate in activation of NO formation in the blood vessels. Both still hypothetic GBB esterdependent. Camps require careful medical organization. Here, secure facilities were provided for medical supplies, while children's own medicines were individually re-labelled. First-aid facilities, for instance, hiperprolactinemia.
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