Ferroportin1 is a newly discovered transmembrane iron export protein. It plays a key role in Fe2+ transport across the basal membrane of enterocytes in the gut. It has been suggested that this protein might have the same role in Fe2+ transport across the abluminal membrane of the blood-brain barrier as it works in enterocytes. However, the presence of ferroportin1 in the brain has not been well determined. In the present study, we investigated expression of ferroportin1 protein in different brain regions, including cortex, hippocampus, striatum and substantia nigra, in developing male Sprague-Dawley rats. The results provided direct evidence for the existence of ferroportin1 protein in the rat brain. All brain areas examined have the ability to synthesize ferroportin1 protein. The findings also showed that age has a significant effect on the expression of ferroportin1 protein in the cortex, hippocampus, striatum and substantia nigra of the rat brain.
The aim of this study was to find a way to efficiently separate neuronal cells from the cerebral cortex of adult rats, providing a reference method for rapid acquisition of neuronal cells from the adult rat brain. Fifteen SD rats were randomly divided into three groups, with five SD rats in each group. Then, neuron cells were isolated from the adult rat cerebral cortex by the grinding method, the trypsin method, and the collagenase II method, respectively. The expression of anti-NeuN in the neurons of each group was analyzed by flow cytometry. The acquisition rates and morphology of neurons of each group were observed by immunofluorescence staining. The grinding or collagenase II method is more suitable for rapid acquisition of neuronal cells from an adult rat's cerebral cortex. The number of neuron cells obtained by the trypsin method were very few, so it is not convenient for later experiments.
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