Abstract
Calcium channel α2δ subunit is a glycosylated structural subunit consistent of the α2 subunit and the δ peptide. Previous studies have indicated distinctive α2 subunit expression in rat spinal cord and dorsal root ganglia (DRG). This study examined whether differential glycosylation underlies the molecular basis of distinct α2δ subunits. The migration patterns of deglycosylated α2 subunits from rat spinal cord, DRG, brain and skeletal muscle were compared in Western blots. The data reported indicate that there are two forms of the α2 subunit in DRG that are different from the α2 subunit in other tissues examined, at least at the glycosylation level. Thus, post-translational modification may be important in tissue specific and functional expression of the α2δ subunit.