Protein kinase B is expressed in pancreatic beta cells and activated upon stimulation with insulin-like growth factor I
(1998) In Biochemical and Biophysical Research Communications 250(1). p.181-186- Abstract
- Protein kinase B (PKB) is involved in signaling to a multitude of important cellular events and is activated by insulin and growth factors, including insulin-like growth factor I (IGF-I). We show here expression of PKB in pancreatic islets and in the beta cell lines HIT-T15, INS-1, and RINm5F. Expression of PKB mRNA and the presence of PKB isoforms (alpha, beta, and gamma) were assessed by Northern blot analysis and RT-PCR, respectively. Antibodies recognizing different parts of PKB isoforms were employed to demonstrate PKB protein expression by immunoblot analysis. By use of immunohistochemistry in rat and mouse pancreatic tissue sections, PKB was localized to predominantly beta cells. Regulation of PKB was examined in INS-1 and RINm5F... (More)
- Protein kinase B (PKB) is involved in signaling to a multitude of important cellular events and is activated by insulin and growth factors, including insulin-like growth factor I (IGF-I). We show here expression of PKB in pancreatic islets and in the beta cell lines HIT-T15, INS-1, and RINm5F. Expression of PKB mRNA and the presence of PKB isoforms (alpha, beta, and gamma) were assessed by Northern blot analysis and RT-PCR, respectively. Antibodies recognizing different parts of PKB isoforms were employed to demonstrate PKB protein expression by immunoblot analysis. By use of immunohistochemistry in rat and mouse pancreatic tissue sections, PKB was localized to predominantly beta cells. Regulation of PKB was examined in INS-1 and RINm5F cells; upon stimulation with IGF-I (5-10 min), PKB was phosphorylated and activated (approximately 3-fold) by a wortmannin-sensitive mechanism, indicating involvement of phosphatidylinositol-3 kinase. The possible participation of PKB in signal transduction pathways modulating cAMP-dependent insulin secretion and in proliferation of beta cells is discussed. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1112669
- author
- Stenson, Lena LU ; Mulder, Hindrik LU ; Manganiello, V ; Sundler, Frank LU ; Ahrén, Bo LU ; Holm, Cecilia LU and Degerman, Eva LU
- organization
- publishing date
- 1998
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biochemical and Biophysical Research Communications
- volume
- 250
- issue
- 1
- pages
- 181 - 186
- publisher
- Elsevier
- external identifiers
-
- pmid:9735353
- scopus:0032497288
- ISSN
- 1090-2104
- DOI
- 10.1006/bbrc.1998.9166
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Molecular Endocrinology (013212018), Medicine (Lund) (013230025), Neuroendocrine Cell Biology (013212008), Molecular Metabolism (013212001), Insulin Signal Transduction (013212014)
- id
- b8f60ec1-b06b-42bf-9a7c-d3abbc0be1f5 (old id 1112669)
- date added to LUP
- 2016-04-01 15:29:20
- date last changed
- 2024-01-10 15:50:40
@article{b8f60ec1-b06b-42bf-9a7c-d3abbc0be1f5, abstract = {{Protein kinase B (PKB) is involved in signaling to a multitude of important cellular events and is activated by insulin and growth factors, including insulin-like growth factor I (IGF-I). We show here expression of PKB in pancreatic islets and in the beta cell lines HIT-T15, INS-1, and RINm5F. Expression of PKB mRNA and the presence of PKB isoforms (alpha, beta, and gamma) were assessed by Northern blot analysis and RT-PCR, respectively. Antibodies recognizing different parts of PKB isoforms were employed to demonstrate PKB protein expression by immunoblot analysis. By use of immunohistochemistry in rat and mouse pancreatic tissue sections, PKB was localized to predominantly beta cells. Regulation of PKB was examined in INS-1 and RINm5F cells; upon stimulation with IGF-I (5-10 min), PKB was phosphorylated and activated (approximately 3-fold) by a wortmannin-sensitive mechanism, indicating involvement of phosphatidylinositol-3 kinase. The possible participation of PKB in signal transduction pathways modulating cAMP-dependent insulin secretion and in proliferation of beta cells is discussed.}}, author = {{Stenson, Lena and Mulder, Hindrik and Manganiello, V and Sundler, Frank and Ahrén, Bo and Holm, Cecilia and Degerman, Eva}}, issn = {{1090-2104}}, language = {{eng}}, number = {{1}}, pages = {{181--186}}, publisher = {{Elsevier}}, series = {{Biochemical and Biophysical Research Communications}}, title = {{Protein kinase B is expressed in pancreatic beta cells and activated upon stimulation with insulin-like growth factor I}}, url = {{http://dx.doi.org/10.1006/bbrc.1998.9166}}, doi = {{10.1006/bbrc.1998.9166}}, volume = {{250}}, year = {{1998}}, }