Hypokinetic stress and neuronal porosome complex in the rat brain: the electron microscopic study.

Japaridze, NJ and Okuneva, VG and Qsovreli, MG and Surmava, AG and Lordkipanidze, TG and Kiladze, Maia and Zhvania, Mzia G Hypokinetic stress and neuronal porosome complex in the rat brain: the electron microscopic study. Micron, 43 (9). pp. 948-953. ISSN 0968-4328

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Porosomes are the universal secretory machinery in cells, where membrane-bound secretory vesicles transiently dock and fuse to release intravesicular contents to the outside of the cell during cell secretion. Studies using atomic force microscopy, electron microscopy, electron density and 3D contour mapping, provided rich nanoscale information on the structure and assembly of proteins within the neuronal porosome complex in normal brain. However it remains uncertain whether pathological conditions that alter process of neurotransmission, provoke alterations in the porosome structure also. To determine if porosomes are altered in disease states, the current study was undertaken for first time using high resolution electron microscope. One of pathologies that produce subtle alteration at the presynaptic terminals has been demonstrated to be hypokinetic stress. The central nucleus of amygdale is the brain region, where such alterations are mostly expressed. We have examined the width and depth of the neuronal porosome complex and their alterations provoked by chronic hypokinetic stress in above mentioned limbic region. Specifically, we have demonstrated that despite alterations in the presynaptic terminals and synaptic transmission provoked by this pathological condition in this region, the final step/structure in neurosecretion--the porosome--remains unaffected: the morphometric analysis of the depth and diameter of this cup-shaped structure at the presynaptic membrane point out to the heterogeneity of porosome dimensions, but with unchanged fluctuation in norm and pathology.

Item Type: Article
Subjects: Q Science > QP Physiology
Divisions: Institutes > Institute of Chemical Biology
Depositing User: Professor Mzia (Ia) G Zhvania
Date Deposited: 20 Jan 2014 09:22
Last Modified: 16 Apr 2015 08:43
URI: http://eprints.iliauni.edu.ge/id/eprint/238

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