Expression and regulation of cyclic nucleotide phosphodiesterases in human and rat pancreatic islets.
(2010) In PLoS ONE 5(12).- Abstract
- As shown by transgenic mouse models and by using phosphodiesterase 3 (PDE3) inhibitors, PDE3B has an important role in the regulation of insulin secretion in pancreatic β-cells. However, very little is known about the regulation of the enzyme. Here, we show that PDE3B is activated in response to high glucose, insulin and cAMP elevation in rat pancreatic islets and INS-1 (832/13) cells. Activation by glucose was not affected by the presence of diazoxide. PDE3B activation was coupled to an increase as well as a decrease in total phosphorylation of the enzyme. In addition to PDE3B, several other PDEs were detected in human pancreatic islets: PDE1, PDE3, PDE4C, PDE7A, PDE8A and PDE10A. We conclude that PDE3B is activated in response to agents... (More)
- As shown by transgenic mouse models and by using phosphodiesterase 3 (PDE3) inhibitors, PDE3B has an important role in the regulation of insulin secretion in pancreatic β-cells. However, very little is known about the regulation of the enzyme. Here, we show that PDE3B is activated in response to high glucose, insulin and cAMP elevation in rat pancreatic islets and INS-1 (832/13) cells. Activation by glucose was not affected by the presence of diazoxide. PDE3B activation was coupled to an increase as well as a decrease in total phosphorylation of the enzyme. In addition to PDE3B, several other PDEs were detected in human pancreatic islets: PDE1, PDE3, PDE4C, PDE7A, PDE8A and PDE10A. We conclude that PDE3B is activated in response to agents relevant for β-cell function and that activation is linked to increased as well as decreased phosphorylation of the enzyme. Moreover, we conclude that several PDEs are present in human pancreatic islets. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1756465
- author
- Heimann, Emilia
LU
; Jones, Helena
LU
; Resjö, Svante
LU
; Manganiello, Vincent C
; Stenson, Lena
LU
and Degerman, Eva
LU
- organization
- publishing date
- 2010
- type
- Contribution to journal
- publication status
- published
- subject
- in
- PLoS ONE
- volume
- 5
- issue
- 12
- article number
- e14191
- publisher
- Public Library of Science (PLoS)
- external identifiers
-
- wos:000284821300008
- pmid:21152070
- scopus:78649816005
- pmid:21152070
- ISSN
- 1932-6203
- DOI
- 10.1371/journal.pone.0014191
- language
- English
- LU publication?
- yes
- id
- 5791fe36-cfa0-48f9-b67a-5dcf6ef0d093 (old id 1756465)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/21152070?dopt=Abstract
- date added to LUP
- 2016-04-04 09:37:22
- date last changed
- 2025-04-04 15:14:33
@article{5791fe36-cfa0-48f9-b67a-5dcf6ef0d093, abstract = {{As shown by transgenic mouse models and by using phosphodiesterase 3 (PDE3) inhibitors, PDE3B has an important role in the regulation of insulin secretion in pancreatic β-cells. However, very little is known about the regulation of the enzyme. Here, we show that PDE3B is activated in response to high glucose, insulin and cAMP elevation in rat pancreatic islets and INS-1 (832/13) cells. Activation by glucose was not affected by the presence of diazoxide. PDE3B activation was coupled to an increase as well as a decrease in total phosphorylation of the enzyme. In addition to PDE3B, several other PDEs were detected in human pancreatic islets: PDE1, PDE3, PDE4C, PDE7A, PDE8A and PDE10A. We conclude that PDE3B is activated in response to agents relevant for β-cell function and that activation is linked to increased as well as decreased phosphorylation of the enzyme. Moreover, we conclude that several PDEs are present in human pancreatic islets.}}, author = {{Heimann, Emilia and Jones, Helena and Resjö, Svante and Manganiello, Vincent C and Stenson, Lena and Degerman, Eva}}, issn = {{1932-6203}}, language = {{eng}}, number = {{12}}, publisher = {{Public Library of Science (PLoS)}}, series = {{PLoS ONE}}, title = {{Expression and regulation of cyclic nucleotide phosphodiesterases in human and rat pancreatic islets.}}, url = {{https://lup.lub.lu.se/search/files/5373343/1762841.pdf}}, doi = {{10.1371/journal.pone.0014191}}, volume = {{5}}, year = {{2010}}, }