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  • Title: Insulin induced phosphorylation and activation of the cGMP-inhibited cAMP phosphodiesterase in human platelets.
    Author: López-Aparicio P, Rascón A, Manganiello VC, Andersson KE, Belfrage P, Degerman E.
    Journal: Biochem Biophys Res Commun; 1992 Jul 15; 186(1):517-23. PubMed ID: 1321613.
    Abstract:
    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.
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