Characterisation of spinophilin immunoreactivity in postmortem human brain homogenates

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Spinophilin is a multifunctional scaffold protein that regulates the formation and function of dendritic spines and plays a role in neuronal migration. The distinct roles of spinophilin depend on its localization and the direct interaction with other proteins, which may target spinophilin to specific locations within the cell. Several studies suggest a role of spinophilin in the pathophysiology of neurological or psychiatric diseases. However, the majority have been performed in animals or cultured cells. Thus, the aim of the present study was to characterise the regional and subcellular expression of spinophilin immunoreactivity by western blot in postmortem human brain. Two specific immunoreactive bands for spinophilin were observed: an intense band migrating at around 120 kDa, which seems to correspond to the apparent molecular weight of spinophilin described by other authors, and a less intense band of around 95 kDa. This second form seems to be a proteolysis or cleavage product of the ˜120 kDa spinophilin. Interestingly, the subcellular distribution of both bands was different. In membrane fraction, the ˜120 kDa spinophilin band was the most abundant, whereas in cytosol it was the ˜95 kDa form. Furthermore, a different regional distribution for ˜120 kDa spinophilin band was observed, with the highest expression in prefrontal cortex, followed by hippocampus and cerebellum, and the lowest in caudate nucleus. Altogether, these results constitute a useful reference for future studies of spinophilin in pathological and non-pathological human brain tissues.

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