Protein phosphorylation in primary astrocyte cultures treated with and without dibutyryl cyclic AMP

Joseph T. Neary, Maria del Pilar Gutierrez, Luz Oliva B. Norenberg, Michael D. Norenberg

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Protein phosphorylation was investigated in primary rat astrocyte cultures treated with and without dibutyryl cyclic AMP. Astrocytes maintained in dibutyryl cyclic AMP for several weeks displayed increased phosphate incorporation in 5 protein bands (55, 52, 45, 43 and 28 kDa) while incorporation in one band (42 kDa) was decreased. Phosphate incorporation in several other protein bands was unchanged. Calcium-dependent phosphate incorporation was also altered by prior exposure of the cells to dibutyryl cyclic AMP: addition of calcium to broken cell preparations resulted in increased incorporation in 75, 53 and 52 kDa while decreased incorporation occurred in 100 kDa. These differences in protein phosphorylation may be related to the previously reported biochemical and morphological changes brought about by dibutyryl cyclic AMP and may provide insights into the mechanisms of reactive gliosis.

Original languageEnglish (US)
Pages (from-to)164-168
Number of pages5
JournalBrain Research
Issue number1
StatePublished - Apr 28 1987



  • Astrocyte
  • Calcium
  • Cyclic adenosine monophosphate
  • Protein phosphorylation

ASJC Scopus subject areas

  • Developmental Biology
  • Molecular Biology
  • Clinical Neurology
  • Neuroscience(all)

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