Role of PDE3B in insulin-induced glucose uptake, GLUT-4 translocation and lipogenesis in primary rat adipocytes.
Zmuda-Trzebiatowska, Emilia LU ; Oknianska, Alina LU ; Manganiello, Vincent and Degerman, Eva LU
(2006)
In Cellular Signalling
18(3).
p.382-390
- Abstract
- In adipocytes, phosphorylation and activation of PDE3B is a key event in the antilipolytic action of insulin. The role of PDE4, another PDE present in adipocytes, is not yet known. In this work we investigate the role of PDE3B and PDE4 in insulin-induced glucose uptake, GLUT-4 translocation and lipogenesis. Inhibition of PDE3 (OPC3911, milrinone) but not PDE4 (RO 20-1724) lowered insulin-induced glucose uptake and lipogenesis, especially in the presence of isoproterenol (a general beta-adrenergic agonist), CL316243, a selective beta 3-adrenergic agonist, and pituitary adenylate cyclase-activating peptide. The inhibitory effect of OPC3911 was associated with reduced translocation of GLUT-4 from the cytosol to the plasma membrane. Both... (More)
- In adipocytes, phosphorylation and activation of PDE3B is a key event in the antilipolytic action of insulin. The role of PDE4, another PDE present in adipocytes, is not yet known. In this work we investigate the role of PDE3B and PDE4 in insulin-induced glucose uptake, GLUT-4 translocation and lipogenesis. Inhibition of PDE3 (OPC3911, milrinone) but not PDE4 (RO 20-1724) lowered insulin-induced glucose uptake and lipogenesis, especially in the presence of isoproterenol (a general beta-adrenergic agonist), CL316243, a selective beta 3-adrenergic agonist, and pituitary adenylate cyclase-activating peptide. The inhibitory effect of OPC3911 was associated with reduced translocation of GLUT-4 from the cytosol to the plasma membrane. Both OPC3911 and RO 20-1724 increased protein kinase A (PKA) activity and lipolysis. H89, a PKA inhibitor, did not affect OPC3911-mediated inhibition of insulin-induced glucose uptake and lipogenesis, whereas 8-pCPT-2'-O-Me-cAMP, an Epac agonist which mediates PKA independent cAMP signaling events, mimicked all the effects of OPC3911. Insulin-mediated activation of protein kinase B, a kinase involved in insulin-induced glucose uptake, was apparently not altered by OPC3911. In summary, our data suggest that PDE3B, but not PDE4, contributes to the regulation of insulin-induced glucose uptake, GLUT-4 translocation, and lipogenesis presumably by regulation of a cAMP/Epac signalling mechanisms. (c) 2005 Elsevier Inc. All rights reserved. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/139989
- author
- Zmuda-Trzebiatowska, Emilia
LU
; Oknianska, Alina
LU
; Manganiello, Vincent
and Degerman, Eva
LU
- organization
- publishing date
- 2006
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- PDE3B, PDE4, Epac, GLUT-4, glucose uptake, lipogenesis, adipocyte, CYCLIC-NUCLEOTIDE PHOSPHODIESTERASE, MEDIATED SIGNAL-TRANSDUCTION, DEPENDENT PROTEIN-KINASE, PANCREATIC BETA-CELL, ADIPOSE-CELLS, FAT-CELLS, GLUT4-CONTAINING VESICLES, CAMP-PHOSPHODIESTERASE, ANTILIPOLYTIC ACTION, TRANSPORTER GLUT4
- in
- Cellular Signalling
- volume
- 18
- issue
- 3
- pages
- 382 - 390
- publisher
- Elsevier
- external identifiers
-
- wos:000233954800012
- scopus:27844585184
- ISSN
- 1873-3913
- DOI
- 10.1016/j.cellsig.2005.05.007
- language
- English
- LU publication?
- yes
- id
- 4d0b133f-d28d-4c4a-ae6c-94d4d78af90b (old id 139989)
- alternative location
- http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=15961276&query_hl=58
- date added to LUP
- 2016-04-01 12:08:21
- date last changed
- 2022-05-06 22:23:31
@article{4d0b133f-d28d-4c4a-ae6c-94d4d78af90b,
abstract = {{In adipocytes, phosphorylation and activation of PDE3B is a key event in the antilipolytic action of insulin. The role of PDE4, another PDE present in adipocytes, is not yet known. In this work we investigate the role of PDE3B and PDE4 in insulin-induced glucose uptake, GLUT-4 translocation and lipogenesis. Inhibition of PDE3 (OPC3911, milrinone) but not PDE4 (RO 20-1724) lowered insulin-induced glucose uptake and lipogenesis, especially in the presence of isoproterenol (a general beta-adrenergic agonist), CL316243, a selective beta 3-adrenergic agonist, and pituitary adenylate cyclase-activating peptide. The inhibitory effect of OPC3911 was associated with reduced translocation of GLUT-4 from the cytosol to the plasma membrane. Both OPC3911 and RO 20-1724 increased protein kinase A (PKA) activity and lipolysis. H89, a PKA inhibitor, did not affect OPC3911-mediated inhibition of insulin-induced glucose uptake and lipogenesis, whereas 8-pCPT-2'-O-Me-cAMP, an Epac agonist which mediates PKA independent cAMP signaling events, mimicked all the effects of OPC3911. Insulin-mediated activation of protein kinase B, a kinase involved in insulin-induced glucose uptake, was apparently not altered by OPC3911. In summary, our data suggest that PDE3B, but not PDE4, contributes to the regulation of insulin-induced glucose uptake, GLUT-4 translocation, and lipogenesis presumably by regulation of a cAMP/Epac signalling mechanisms. (c) 2005 Elsevier Inc. All rights reserved.}},
author = {{Zmuda-Trzebiatowska, Emilia and Oknianska, Alina and Manganiello, Vincent and Degerman, Eva}},
issn = {{1873-3913}},
keywords = {{PDE3B; PDE4; Epac; GLUT-4; glucose uptake; lipogenesis; adipocyte; CYCLIC-NUCLEOTIDE PHOSPHODIESTERASE; MEDIATED SIGNAL-TRANSDUCTION; DEPENDENT PROTEIN-KINASE; PANCREATIC BETA-CELL; ADIPOSE-CELLS; FAT-CELLS; GLUT4-CONTAINING VESICLES; CAMP-PHOSPHODIESTERASE; ANTILIPOLYTIC ACTION; TRANSPORTER GLUT4}},
language = {{eng}},
number = {{3}},
pages = {{382--390}},
publisher = {{Elsevier}},
series = {{Cellular Signalling}},
title = {{Role of PDE3B in insulin-induced glucose uptake, GLUT-4 translocation and lipogenesis in primary rat adipocytes.}},
url = {{https://lup.lub.lu.se/search/files/2797645/624752.pdf}},
doi = {{10.1016/j.cellsig.2005.05.007}},
volume = {{18}},
year = {{2006}},
}