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Dipyridamole stimulates types II cAMP-dependent protein kinase in vitro

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Abstract

Dipyridamole activates in vitro type II CAMP-dependent protein kinase. This agent stimulates the autophosphorylation of the regulatory subunit in the presence of CAMP but not so in the absence of the cyclic nucleotide. The activation was also observed with exogenous substrates such as casein, histone 2A and MAP 2. This stimulation did not seem to be related to the cAMP binding to the R II subunit of the enzyme. Competition binding experiments showed that dipyridamole does not compete with adenosine for the A1 receptor. The results suggest that the reported regulatory properties of dipyridamole on lipid metabolism (González-Nicolás et al. Int J Biochem 21: 883–888, 1989) might be mediated through a direct action — an activation — on the catalytic subunit of a cAMP-dependent protein kinase.

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Authors and Affiliations

  1. Centro de Biología Molecular (UAMICSIC), Universidad Autonóma, 28049, Madrid, Spain

    Juan S. Jiménez & María J. Benítez

  2. Departamento de Química-Fisica Aplicada (UAM), Universidad de Castilla-La Mancha, 13071, Ciudad Real, Spain

    Carmen G. Lechuga, Gema Alonso & Francisco J. Moreno

  3. Facultad de Ciencias Químicas, Universidad de Castilla-La Mancha, 13071, Ciudad Real, Spain

    Manuel Ros

Authors
  1. Juan S. Jiménez
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  2. Carmen G. Lechuga
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  3. Gema Alonso
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  4. María J. Benítez
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  5. Manuel Ros
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  6. Francisco J. Moreno
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Jiménez, J.S., Lechuga, C.G., Alonso, G. et al. Dipyridamole stimulates types II cAMP-dependent protein kinase in vitro . Mol Cell Biochem 109, 9–15 (1992). https://doi.org/10.1007/BF00230868

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  • DOI: https://doi.org/10.1007/BF00230868

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