Insulin induced phosphorylation and activation of the cGMP-inhibited cAMP phosphodiesterase in human platelets
Författare
Summary, in 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.
Publiceringsår
1992
Språk
Engelska
Sidor
517-523
Publikation/Tidskrift/Serie
Biochemical and Biophysical Research Communications
Volym
186
Issue
1
Dokumenttyp
Artikel i tidskrift
Förlag
Elsevier
Ämne
- Biological Sciences
Status
Published
Forskningsgrupp
- Insulin Signal Transduction
ISBN/ISSN/Övrigt
- ISSN: 1090-2104