Electron Microscopic Morphometry of Isolated Rat Brain Porosome Complex

Zhvania, Mzia G and Lordkipanidze, Tamar and Ksovreli, Mariam and Okuneva, Vera (2015) Electron Microscopic Morphometry of Isolated Rat Brain Porosome Complex. Neuroscience Research, 100. pp. 17-20. (In Press)

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Porosomes are the universal secretory portals at the cell plasma membrane where membrane-bound secretory vesicles dock and transiently fuse via the kiss-and-run mechanism of cellular secretion, to release intravesicular cargo to the outside of the cell. Through this porosome-mediated mechanism of cell secretion, the accumulation of partially empty secretory vesicles in cells following a secretory episode, and the existence of neurotransmitter transporters at the synaptic vesicle membrane for rapid filling following neurotransmission, is explained. In the past decade a great volume of work from different laboratories provide molecular insights on the structure, function, and composition of the porosome complex, especially the neuronal porosome. In rat neurons 12-17 nm cup-shaped lipoprotein porosomes, possessing a central plug are present at the presynaptic membrane sometimes with docked synaptic vesicles. Although earlier studies have greatly progressed our understanding of the morphology and the proteome and limited lipidome of the neuronal porosome complex, the current study was carried out to determine the morphology of the bare protein backbone of the neuronal porosome complex. Results from our study demonstrate that although the eight-fold symmetry of the immunoisolated porosome is maintained, and the central plug is preserved in the isolated structures, there is a loss in the average size of the porosome complex, possibly due to a loss of lipids from the complex

Item Type: Article
Subjects: Q Science > QI Neuroscience
Divisions: Institutes > Institute of Chemical Biology
Depositing User: Professor Mzia (Ia) G Zhvania
Date Deposited: 10 Nov 2015 06:00
Last Modified: 10 Nov 2015 06:00
URI: http://eprints.iliauni.edu.ge/id/eprint/3833

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