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Regulation of CCAAT/enhancer-binding protein family members by stimulation of glutamate receptors in cultured rat cortical astrocytes


Regulation of CCAAT/enhancer-binding protein family members by stimulation of glutamate receptors in cultured rat cortical astrocytes



Journal of Biological Chemistry 271(38): 23520-23527



ISSN/ISBN: 0021-9258

PMID: 8798561

DOI: 10.1074/jbc.271.38.23520

Regulation of mRNA levels, DNA binding activities, and phosphorylation of CCAAT/enhancer-binding protein (C/EBP) family members by stimulation of glutamate receptors were studied in cultured rat cortical astrocytes. Indirect immunofluorescence and immunoblot analyses with specific antibodies to C/EBP family members revealed that both C/EBP-beta and C/EBP-delta but not C/EBP-alpha are expressed in the nuclei of astrocytes. After exposure to glutamate, C/EBP-beta mRNA levels increased within 10 min, reached the maximal level at about 1 h, and returned to the basal level within 6 h. In contrast, C/EBP-delta mRNA levels decreased by 6 h and were recovered within 12 h. These changes in mRNA levels were accompanied by an increase and a decrease in proteins for C/EBP-beta and C/EBP-delta, respectively. Elevation of C/EBP-beta mRNA levels by glutamate treatment required an increase in intracellular Ca-2+ concentration and depended on activations of protein kinase C and calmodulin-dependent protein kinases. Gel mobility shift analysis using nuclear extracts from the glutamate-treated cells showed increases in C/EBP site binding activities 2 h after the exposure to glutamate. Moreover, glutamate stimulated phosphorylation of C/EBP-beta in 32P-labeled astrocytes in a Ca-2+-dependent manner. These results suggest that glutamate regulates functions of C/EBP family members in brain astrocytes through changes in mRNA levels of C/EBP-beta and C/EBP-delta as well as through phosphorylation of C/EBP-beta.

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