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Eva Degerman

Eva Degerman

Professor

Eva Degerman

Protein kinase A-dependent activation of PDE4 (cAMP-specific cyclic nucleotide phosphodiesterase) in cultured bovine vascular smooth muscle cells

Author

  • Dag Ekholm
  • Per Belfrage
  • Vincent Manganiello
  • Eva Degerman

Summary, in English

Incubation of cultured bovine vascular smooth muscle cells (VSMC) with forskolin increased cAMP as measured by an increase in cAMP-dependent protein kinase (PKA) activation (PKA ratio). Forskolin also produced a concentration- and time-dependent increase in activity (3-5-fold within 15 min) of a PDE4 (cAMP-specific cyclic nucleotide phosphodiesterase). The increase in PDE4 activity was not affected by cycloheximide and thus not likely due to increased synthesis of the enzyme. Activation, which was preserved during partial purification of the enzyme by chromatography on Sephacryl S-200 and MonoQ, was most likely due to a covalent modification. Incubation of cell homogenates with the catalytic subunit of PKA (PKA(c)) induced a approximately 5-fold activation of PDE4 with a time course similar to that in intact cells after forskolin addition. The forskolin-mediated activation was reversed during incubation of homogenates at room temperature for two hours. Addition of PKA(c) resulted in rapid reactivation of PDE4. These data are consistent with the hypothesis that rapid, reversible activation of PDE4 in cultured VSMC is mediated by PKA.

Department/s

  • Insulin Signal Transduction

Publishing year

1997

Language

English

Pages

64-70

Publication/Series

Biochimica et biophysica acta

Volume

1356

Issue

1

Document type

Journal article

Publisher

Elsevier

Topic

  • Biological Sciences

Keywords

  • Phosphodiesterase
  • Smooth muscle cells
  • cAMP dependent protein kinase
  • Rolipram
  • Forskolin

Status

Published

Research group

  • Insulin Signal Transduction

ISBN/ISSN/Other

  • ISSN: 0006-3002