Characterization of protein changes associated with olfactory social conditioning in rats
The purpose of this study is to compare proteome profiles from the neocortex of socially conditioned rats, as a strategy for analyzing the underlying molecular mechanism of learning. Insular cortex samples were obtained from rats subjected to an odor-odor association task. Subcellular fractionation of the rat insular cortex was analyzed using IEF/SDS-PAGE two-dimensional protein analysis. Protein patterns in the gel were visualized with silver stain and computer analyzed with PDQuest software. Spots of interest were selected for identification by molecular weight and isoelectric point as parameters for protein identification on SWISS-PROT, a public database. Of 11 spots selected, 64% appeared concomitantly in groups exposed to a novel odor. Some of the candidate matches for selected spots include calcineurin B subunit isoform 2, syntenin-1, voltage-dependent calcium channel gamma-5 subunit, apelin receptor and, other regulatory and modulatory proteins. These proteins represent prime candidates for future confirmation by mass spectrometry. These results demonstrate molecular changes which may underlie the mechanism of learning. ^
Biology, Molecular|Biology, Neuroscience
Lozano, Jose J, "Characterization of protein changes associated with olfactory social conditioning in rats" (2005). ETD Collection for University of Texas, El Paso. AAI1427727.