cAMP oscillations restrict protein kinase A redistribution in insulin-secreting cells

Biochem Soc Trans. 2006 Aug;34(Pt 4):498-501. doi: 10.1042/BST0340498.

Abstract

Activation of hormone receptors was recently found to evoke oscillations of the cAMP concentration ([cAMP]) beneath the plasma membrane of insulin-secreting cells. Here we investigate how different time courses of cAMP signals influence the generation of cytoplasmic Ca(2+) signals and nuclear translocation of the PKA (protein kinase A) catalytic subunit in individual INS-1 beta-cells. [cAMP] was measured with a fluorescent translocation biosensor and ratiometric evanescent wave microscopy. Analysis of PKA nuclear translocation was performed with epifluorescence microscopy and FlAsH (fluorescein arsenical helix binder) labelling of tetracysteine-tagged PKA-Calpha subunit. Both oscillatory and stable elevations of [cAMP] induced by intermittent or constant inhibition of phosphodiesterases with isobutylmethylxanthine evoked Ca(2+) spiking. During [cAMP] oscillations, the Ca(2+) spiking was restricted to the periods of elevated [cAMP]. In contrast, only stable [cAMP] elevation induced nuclear entry of FlAsH-labelled PKA-Calpha. These results indicate that oscillations of [cAMP] lead to selective target activation by restricting the spatial redistribution of PKA.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Active Transport, Cell Nucleus
  • Animals
  • Calcium / metabolism
  • Catalytic Domain
  • Cell Line, Tumor
  • Cyclic AMP / metabolism*
  • Cyclic AMP-Dependent Protein Kinases / metabolism*
  • Insulin-Secreting Cells / metabolism*
  • Rats

Substances

  • Cyclic AMP
  • Cyclic AMP-Dependent Protein Kinases
  • Calcium