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

Lopez-Aparicio, Pilar ; Rascon, Ana LU ; Manganiello, Vincent C ; Andersson, Karl-Erik LU orcid ; Belfrage, Per and Degerman, Eva LU orcid (1992) In Biochemical and Biophysical Research Communications 186(1). p.517-523
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... (More)
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. (Less)
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author
; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biochemical and Biophysical Research Communications
volume
186
issue
1
pages
517 - 523
publisher
Elsevier
external identifiers
  • pmid:1321613
  • scopus:0026672906
ISSN
1090-2104
DOI
10.1016/S0006-291X(05)80838-1
language
English
LU publication?
yes
id
49ae2dcb-3df3-4eeb-a8ca-b143a576e891 (old id 1106731)
date added to LUP
2016-04-01 15:37:24
date last changed
2025-10-14 11:39:07
@article{49ae2dcb-3df3-4eeb-a8ca-b143a576e891,
  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.}},
  author       = {{Lopez-Aparicio, Pilar and Rascon, Ana and Manganiello, Vincent C and Andersson, Karl-Erik and Belfrage, Per and Degerman, Eva}},
  issn         = {{1090-2104}},
  language     = {{eng}},
  number       = {{1}},
  pages        = {{517--523}},
  publisher    = {{Elsevier}},
  series       = {{Biochemical and Biophysical Research Communications}},
  title        = {{Insulin induced phosphorylation and activation of the cGMP-inhibited cAMP phosphodiesterase in human platelets}},
  url          = {{http://dx.doi.org/10.1016/S0006-291X(05)80838-1}},
  doi          = {{10.1016/S0006-291X(05)80838-1}},
  volume       = {{186}},
  year         = {{1992}},
}