Полимеризация тубулина и его колхицинсвязывающая активность в различных структурах головного мозга в норме и при шизофрении

Abstract

Introduction: abnormalities of neuronal cytoskeleton in mental disorders require to study microtubules and their proteins. Tubulin (the main protein of microtubules) has specific properties: reversibly polymerize into microtubules and bind mitotic poison colchicine in equimolar quantities. Objective: to evaluate the process of tubulin polymerization by light scattering change and to determine the level of colchicine binding (colchicine binding activity of tubulin) in various brain structures in healthy and schizophrenia brains. Material and methods: autopsy brain samples from patients with schizophrenia (n = 6) and from the control group (n = 9) were studied. Samples of the prefrontal (area 10), temporal (area 21), cingulate cortex (area 23/24) and thalamus were isolated (Brodmann's areas). Measurements of light scattering during tubulin polymerization and colchicine-binding activity of tubulin were determined as described earlier. Results: tubulin polymerization was not disturbed in schizophrenia as compared to controls, except for the cingulate cortex that showed slight but significant decrease in light scattering. At the same time, the binding of colchicine in schizophrenia was reduced in all examined areas of the cortex. This decrease was not associated with age, sex, and postmortem interval since the groups were matched by these factors. The tubulin colchicine-binding activity in thalamus remained at the same level both in control and schizophrenia, but it was lower than in the areas of the cortex. Conclusion: Decreased activity and hence decreased amount of tubulin in the cerebral cortical areas without changes of the tubulin polymerization in microtubules have been shown in schizophrenia. The results confirm the literature data on the changes in the cytoskeleton in cortical areas in schizophrenia.