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Insulin induced phosphorylation and activation of the cGMP-inhibited cAMP phosphodiesterase in human platelets

  • Pilar Lopez-Aparicio
  • Ana Rascon
  • Vincent C Manganiello
  • Karl-Erik Andersson
  • Per Belfrage
  • Eva Degerman
Publishing year: 1992
Language: English
Pages: 517-523
Publication/Series: Biochemical and Biophysical Research Communications
Volume: 186
Issue: 1
Document type: Journal article
Publisher: Elsevier

Abstract english

Insulin induced phosphorylation and activation of the cGMP inhibited cAMP phosphodiesterase (cGI-PDE) in human platelets were demonstrated after isolation of the enzyme with specific polyclonal cGI-PDE antibodies. The demonstration of this insulin effect required suppression of basal cGI-PDE phosphorylation, through the use of the protein kinase inhibitor H-7 (1-(5-isoquinolinylsulfonyl)-2-methylpiperazine). The human platelet insulin receptor beta-subunit, previously identified as a 97 kDa polypeptide, was detected with the use of wheat germ agglutinin chromatography and anti-phosphotyrosine antibodies. These results suggest that insulin, through phosphorylation/activation of cGI-PDE, could decrease cAMP/cAMP dependent protein kinase (cAMP-PK) activity and thereby make the platelets more sensitive towards aggregating agents.


  • Biological Sciences


  • Insulin Signal Transduction
  • ISSN: 1090-2104
Eva Degerman
E-mail: eva [dot] degerman [at] med [dot] lu [dot] se


Insulin Signal Transduction

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