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Insulin-induced translocation of protein kinase B to the plasma membrane in rat adipocytes

Göransson, Olga LU orcid ; Wijkander, Jonny ; Manganiello, V and Degerman, Eva LU orcid (1998) In Biochemical and Biophysical Research Communications 246(1). p.249-254
Abstract
Protein kinase B (PKB) has previously been shown to be activated in response to insulin and growth factor stimulation. The activation mechanism has been suggested to involve translocation of PKB to membranes, where it is phosphorylated and activated. Insulin-induced translocation of PKB has not been demonstrated in a physiological target cell. Therefore we have used the primary rat adipocyte to investigate insulin-induced translocation of PKB. In the presence of 1 nM insulin translocation of PKB was detected within 30 seconds and was blocked by wortmannin, a selective phosphatidylinositol 3-kinase inhibitor. This translocation was potentiated by the tyrosine phosphatase inhibitor vanadate. Subcellular localization studies revealed that PKB... (More)
Protein kinase B (PKB) has previously been shown to be activated in response to insulin and growth factor stimulation. The activation mechanism has been suggested to involve translocation of PKB to membranes, where it is phosphorylated and activated. Insulin-induced translocation of PKB has not been demonstrated in a physiological target cell. Therefore we have used the primary rat adipocyte to investigate insulin-induced translocation of PKB. In the presence of 1 nM insulin translocation of PKB was detected within 30 seconds and was blocked by wortmannin, a selective phosphatidylinositol 3-kinase inhibitor. This translocation was potentiated by the tyrosine phosphatase inhibitor vanadate. Subcellular localization studies revealed that PKB translocated to the plasma membrane. (Less)
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author
; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
insulin, adipocyte, protein kinase B, plasma membrane, phosphatidylinositol 3-kinase
in
Biochemical and Biophysical Research Communications
volume
246
issue
1
pages
249 - 254
publisher
Elsevier
external identifiers
  • pmid:9600101
  • scopus:0344157383
ISSN
1090-2104
DOI
10.1006/bbrc.1998.8602
language
English
LU publication?
yes
id
8a6db71c-f935-4b90-bf6b-c8fd45dab84d (old id 1112738)
date added to LUP
2016-04-01 16:48:21
date last changed
2024-04-12 07:51:12
@article{8a6db71c-f935-4b90-bf6b-c8fd45dab84d,
  abstract     = {{Protein kinase B (PKB) has previously been shown to be activated in response to insulin and growth factor stimulation. The activation mechanism has been suggested to involve translocation of PKB to membranes, where it is phosphorylated and activated. Insulin-induced translocation of PKB has not been demonstrated in a physiological target cell. Therefore we have used the primary rat adipocyte to investigate insulin-induced translocation of PKB. In the presence of 1 nM insulin translocation of PKB was detected within 30 seconds and was blocked by wortmannin, a selective phosphatidylinositol 3-kinase inhibitor. This translocation was potentiated by the tyrosine phosphatase inhibitor vanadate. Subcellular localization studies revealed that PKB translocated to the plasma membrane.}},
  author       = {{Göransson, Olga and Wijkander, Jonny and Manganiello, V and Degerman, Eva}},
  issn         = {{1090-2104}},
  keywords     = {{insulin; adipocyte; protein kinase B; plasma membrane; phosphatidylinositol 3-kinase}},
  language     = {{eng}},
  number       = {{1}},
  pages        = {{249--254}},
  publisher    = {{Elsevier}},
  series       = {{Biochemical and Biophysical Research Communications}},
  title        = {{Insulin-induced translocation of protein kinase B to the plasma membrane in rat adipocytes}},
  url          = {{http://dx.doi.org/10.1006/bbrc.1998.8602}},
  doi          = {{10.1006/bbrc.1998.8602}},
  volume       = {{246}},
  year         = {{1998}},
}