Insulin induced phosphorylation and activation of the cGMP-inhibited cAMP phosphodiesterase in human platelets
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1106731
- author
- Lopez-Aparicio, Pilar ; Rascon, Ana LU ; Manganiello, Vincent C ; Andersson, Karl-Erik LU ; Belfrage, Per and Degerman, Eva LU
- organization
- publishing date
- 1992
- 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
- 2021-01-31 05:37:51
@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}}, }