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<abstract xmlns="http://eprints.org/ep2/data/2.0">Abstract—It is well established that during cell secretion, membrane�bound secretory vesicles dock and fuse&#13;
at the base of supramolecular cup�shaped structures at the cell plasma membrane called “porosomes”, to&#13;
expel intra�vesicular contents to the outside. In neurons, it has been demonstrated that 12–17 nm cup�&#13;
shaped lipoprotein structure possessing a central plug are present at the presynaptic membrane, where 50 nm&#13;
in diameter synaptic vesicles transiently dock and fuse to release neurotransmitters. In the past decade, the&#13;
neuronal porosome has been isolated and its major chemical composition determined. Additionally, the&#13;
porosome has been both structurally and functionally reconstituted into artificial lipid membrane, establish�&#13;
ing its role as the secretory portal in neurons. Studies utilizing atomic force and electron microscopy, com�&#13;
bined with electron density and 3D contour mapping, provide at the nanoscale, the structure and assembly&#13;
of proteins within the neuronal porosome. In the current study, ultrahigh resolution imaging of the presynap�&#13;
tic membrane of isolated brains from both rats and cats, demonstrate for the first time, the presence of neu�&#13;
ronal porosomes in cat brain, and further confirms the presence of porosomes at the presynaptic membrane&#13;
in rat brain synaptosomes. Results from the present study further confirm the cup�shaped morphology of&#13;
porosomes in the rat brain, and demonstrates their similar shape and size in the cat nerve terminal. The study&#13;
also demonstrates for the first time, the universal presence of similar porosomes in different species of mam�&#13;
mals.&#13;
</abstract>
