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G Testylier

Publications and source records attributed to G Testylier.

4 recordsLinked to original sources

Rapid postmortem decrease in the ectocellular acetylcholinesterase activity in rat striatum as assessed by in vivo microspectrophotometry.

The acetylcholinesterase (AChE) activity in striatum rat was determined before and shortly after death using the in vivo microspectrophotometric method. This technique allowed us to monitor the Ellman colorimetric reaction directly inside the brain using an optical probe implanted in a live animal and to determine locally the AChE activity. Whatever the cause of the animals death, we observed a drastic postmortem decrease of the AChE activity of about 35-50%, 10 min after death. We have verified that the postmortem decrease of brain temperature or pH and postmortem optical properties changes could only explain a fraction of the AChE activity fall (16%). This phenomenon seems to be related to events strictly localized at the cellular level, since local injection of cyanide at the measuring site promotes a decrease of the enzymatic activity (40%) close to the levels observed after death. The origin of this rapid postmortem fall of the AChE activity is discussed. The technical properties of the microspectrophotometric method exclude a decrease of the ectocellular pool of enzyme after death. Our results allow us to envisage the existence of an in vivo endogenous regulation of the AChE activity which disappears shortly after death.

Acetylcholinesterase

In vivo spectrophotometric determination of striatal acetylcholinesterase activity: the modulation induced by the antidepressant amitriptyline.

A new technology called in vivo spectrophotometry was applied to the quantitative determination of the variations in local acetylcholinesterase (AChE) activities. Repeated measurements of the enzyme activities in the same live animal allowed the study of the in vivo inhibition of AChE by amitriptyline. Interactions between AChE and this tricyclic antidepressant were investigated at the striatal level in anesthetized rats. In this anesthetized model, AChE assays were shown to be stable for approximately 8 h. The dose-effect relationship was explored in the 2.5- to 50-mg/kg amitriptyline range. A reversible inhibition was observed after acute amitriptyline administration. The maximum of inhibition appeared between 90 and 210 min after the intoxication and reached up to 22% for the 50-mg/kg dose. The threshold dose was established as 8 mg/kg. Evidence for an indirect interaction between tricyclic antidepressant and AChE was demonstrated when the total integrity of the biological system was preserved.

Acetylcholinesterase

Demonstration of functional acetylcholinesterase on the soma of individual neurones of Aplysia by in vivo microspectrophotometry.

The presence of functional acetylcholinesterase is demonstrated in vivo on somatic membranes of single ganglionic neurones of Aplysia using concurrently microspectrophotometry and electrophysiology. The similarity of the effects of an irreversible blocker of acetylcholinesterase and of phospholipase C from Bacillus cereus suggests that acetylcholinesterase is anchored in the membrane via phosphatidylinositol.

Acetylcholinesterase

Spectrophotometry in vivo, a technique for local and direct enzymatic assays: application to brain acetylcholinesterase.

In vivo enzymology is not widely studied due to the lack of a well-adapted technology. We have developed a system that allows local and long-term spectrophotometric assays in brain tissue of live animals. It utilizes a miniaturized optical probe consisting of a multibarrel micropipette for reagent injections and optical fibers for light absorption measurements. We have applied this system to the colorimetric determination of brain acetylcholinesterase activity in rats. The reproducibility of the assay was demonstrated by repetitive assays over 24 hr, its specificity was established through the use of a highly specific organophosphorus inhibitor, and the activities measured in different brain areas agreed with the known distribution of acetylcholinesterase. No electroencephalographic abnormalities and no change in vigilance level were observed in the experimental animals. This methodology should prove to be useful for the colorimetric measurement of different enzymes or metabolites in various organs.

Acetylcholinesterase