In situ hybridization histochemical study on the mRNA for protein phosphatase in the brain of adult rats.

点击翻译按钮获取中文摘要

The present study disclosed widespread expression with differential intensity of mRNAs for alpha and beta isoforms of type 2A protein phosphatase (PP2A-alpha and -beta) and type 2C protein phosphatase (PP2C) in the adult rat brain by in situ hybridization analysis. Expression signals of mRNA for PP2C were observed most highly in the granule cells and Purkinje cells of the cerebellum, the pyramidal cells of the hippocampus and granule cells of the dentate gyrus, and plexus choroideus, whereas moderate levels of its expression were observed in the medial habenula, piriform cortex, the pineal body, and several discrete nuclei of the brain stem. Weak expression of PP2C mRNA was observed in mitral and internal granule cells of the olfactory bulb, spinal cord gray matter, the cerebralneocortex, thalamic and hypothalamic nuclel. Only faint expression of it was detected in the caudate putamen. The gene expression of PP2A was observed intensely in the piriform cortex, the cerebellar Purkinje an … More d granule cell layrs, and the hippocampal pyramidal and dentate granule cell layrs, and the locus ceruleus, whereas the moderate levels of its expression were observed in the olfactory mitral cells and the pontine nuclei. The cerebral neocortex expressed the mRNA moderately to weakly without any laminar patterns, whereas the expression level in the caudate-putamen was very low.The high expression was observed in the hippocampal formation, the cerebellar Purkinje cell and granule cell layrs, suggesting the occurrence of very active phosphorylation-dephosphorylation cycle in these neurons. The gene expression for PP2A is similar to that of PP2C, except for the plexus choroideus and ependyma. This similarity is well compatible with the fact that these PPs have broad and overlapping specificities in vitro. It is necessary to examine the detailed localization of mRNA for type 1 protein phosphatase to analyze the reversal of the Ca^<2+>-independent activity of Ca^<2+>/calmodulin dependent protein kinase II by autophosphorylation. Less